RiceWiki - User contributions [en]

Os02g0100200

2014-06-08T08:42:38Z

Zhishp: /* Ligands */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.<ref name="ref5"/>
Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:<ref name="ref5"/><ref name="ref6"/>

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.<ref name="ref7"/>

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

[[File:800px-Type_ii_nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.<ref name="ref8"/>
Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
<ref name="ref5">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 8521507.</ref>
<ref name="ref6">Jump up to: a b Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref7">Linja MJ, Porkka KP, Kang Z, Savinainen KJ, Jänne OA, Tammela TL, Vessella RL, Palvimo JJ, Visakorpi T (February 2004). "Expression of androgen receptor coregulators in prostate cancer". Clin. Cancer Res. 10 (3): 1032–40. doi:10.1158/1078-0432.CCR-0990-3. PMID 14871982.</ref>
<ref name="ref8">Klinge CM, Bodenner DL, Desai D, Niles RM, Traish AM (May 1997). "Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro". Nucleic Acids Res. 25 (10): 1903–12. doi:10.1093/nar/25.10.1903. PMC 146682. PMID 9115356.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T08:05:42Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.<ref name="ref5"/>
Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:<ref name="ref5"/><ref name="ref6"/>

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.<ref name="ref7"/>

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

[[File:800px-Type_ii_nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.<ref name="ref8"/>
Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
<ref name="ref5">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 8521507.</ref>
<ref name="ref6">Jump up to: a b Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref7">Linja MJ, Porkka KP, Kang Z, Savinainen KJ, Jänne OA, Tammela TL, Vessella RL, Palvimo JJ, Visakorpi T (February 2004). "Expression of androgen receptor coregulators in prostate cancer". Clin. Cancer Res. 10 (3): 1032–40. doi:10.1158/1078-0432.CCR-0990-3. PMID 14871982.</ref>
<ref name="ref8">Klinge CM, Bodenner DL, Desai D, Niles RM, Traish AM (May 1997). "Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro". Nucleic Acids Res. 25 (10): 1903–12. doi:10.1093/nar/25.10.1903. PMC 146682. PMID 9115356.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T08:03:45Z

Zhishp: /* References */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

[[File:800px-Type_ii_nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
<ref name="ref5">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 8521507.</ref>
<ref name="ref6">Jump up to: a b Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref7">Linja MJ, Porkka KP, Kang Z, Savinainen KJ, Jänne OA, Tammela TL, Vessella RL, Palvimo JJ, Visakorpi T (February 2004). "Expression of androgen receptor coregulators in prostate cancer". Clin. Cancer Res. 10 (3): 1032–40. doi:10.1158/1078-0432.CCR-0990-3. PMID 14871982.</ref>
<ref name="ref8">Klinge CM, Bodenner DL, Desai D, Niles RM, Traish AM (May 1997). "Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro". Nucleic Acids Res. 25 (10): 1903–12. doi:10.1093/nar/25.10.1903. PMC 146682. PMID 9115356.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:53:32Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

[[File:800px-Type_ii_nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:51:32Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

[[File:800px-Type_ii_nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

File:800px-Type ii nuclear receptor action.png

2014-06-08T07:50:23Z

Zhishp: This figure depicts the mechanism of a class II nuclear receptor (NR) which, regardless of ligand binding status is located in the nucleus bound to DNA. For the purpose of illustration, the nuclear receptor shown here is the thyroid hormone receptor (TR)

This figure depicts the mechanism of a class II nuclear receptor (NR) which, regardless of ligand binding status is located in the nucleus bound to DNA. For the purpose of illustration, the nuclear receptor shown here is the thyroid hormone receptor (TR) heterodimerized to the RXR. In the absence of ligand, the TR is bound to corepressor protein. Ligand binding to TR causes a dissociation of corepressor and recruitment of coactivator protein which in turn recruit additional proteins such as RNA polymerase that are responsible for transcription of downstream DNA into RNA and eventually protein which results in a change in cell function.

Os02g0100200

2014-06-08T07:48:49Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:48:14Z

Zhishp: /* Nuclear receptors */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:47:05Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

[[File:800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]

Type II

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:46:17Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I

Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

[[800px-Nuclear_receptor_action.png|200px|thumb|left|alt text]]
Type II

Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II

nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III

Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV

Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

File:800px-Nuclear receptor action.png

2014-06-08T07:44:26Z

Zhishp: This figure depicts the mechanism of a class I nuclear receptor (NR) which, in the absence of ligand, is located in the cytosol. Hormone binding triggers dissociation of heat shock proteins (HSP), dimerization, and translocation to the nucleus where it bi

This figure depicts the mechanism of a class I nuclear receptor (NR) which, in the absence of ligand, is located in the cytosol. Hormone binding triggers dissociation of heat shock proteins (HSP), dimerization, and translocation to the nucleus where it binds to a specific sequence of DNA known as a hormone response element (HRE). The nuclear receptor DNA complex in turn recruits other proteins that are responsible for translation of downstream DNA into RNA and eventually protein which results in a change in cell function

Os02g0100200

2014-06-08T07:42:57Z

Zhishp: /* Mechanism of action */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

====Mechanism of action====
Nuclear receptors are multifunctional proteins that transduce signals of their cognate ligands. Nuclear receptors (NRs) may be classified into two broad classes according to their mechanism of action and subcellular distribution in the absence of ligand.

Small lipophilic substances such as natural hormones diffuse through the cell membrane and bind to nuclear receptors located in the cytosol (type I NR) or nucleus (type II NR) of the cell. Binding causes a conformational change in the receptor which, depending on the class of receptor, triggers a cascade of downstream events that direct the NRs to DNA transcription regulation sites which result in up or down-regulation of gene expression. In addition, two additional classes, type III which are a variant of type I, and type IV that bind DNA as monomers have also been identified.[4]

Accordingly, nuclear receptors may be subdivided into the following four mechanistic classes:[4][5]

Type I[edit]
Ligand binding to type I nuclear receptors in the cytosol results in the dissociation of heat shock proteins, homo-dimerization, translocation (i.e., active transport) from the cytoplasm into the cell nucleus, and binding to specific sequences of DNA known as hormone response elements (HREs). Type I nuclear receptors bind to HREs consisting of two half-sites separated by a variable length of DNA, and the second half-site has a sequence inverted from the first (inverted repeat). Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.[22]

It has been noted that some of the NR subfamily 2 nuclear receptors may bind to direct repeat instead of inverted repeat HREs. In addition, some nuclear receptors that bind either as monomers or dimers, with only a single DNA binding domain of the receptor attaching to a single half site HRE. These nuclear receptors are considered orphan receptors, as their endogenous ligands still unknown.

The nuclear receptor/DNA complex then recruits other proteins that transcribe DNA downstream from the HRE into messenger RNA and eventually protein, which causes a change in cell function.

Type II[edit]
Type II receptors, in contrast to type I, are retained in the nucleus regardless of the ligand binding status and in addition bind as hetero-dimers (usually with RXR) to DNA. In the absence of ligand, type II nuclear receptors are often complexed with corepressor proteins. Ligand binding to the nuclear receptor causes dissociation of corepressor and recruitment of coactivator proteins. Additional proteins including RNA polymerase are then recruited to the NR/DNA complex that transcribe DNA into messenger RNA.

Type II nuclear receptors include principally subfamily 1, for example the retinoic acid receptor, retinoid X receptor and thyroid hormone receptor.[23]

Type III[edit]
Type III nuclear receptors (principally NR subfamily 2) are similar to type I receptors in that both classes bind to DNA as homodimers. However, type III nuclear receptors, in contrast to type I, bind to direct repeat instead of inverted repeat HREs.

Type IV[edit]
Type IV nuclear receptors bind either as monomers or dimers, but only a single DNA binding domain of the receptor binds to a single half site HRE. Examples of type IV receptors are found in most of the NR subfamilies.

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:39:46Z

Zhishp: /* Nuclear receptors */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

====Mechanism of action====

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:37:40Z

Zhishp: /* stucture */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

[[File:800px-Nuclear Receptor Structure.png|200px|thumb|left|alt text]]

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

File:800px-Nuclear Receptor Structure.png

2014-06-08T07:36:03Z

Zhishp:

Os02g0100200

2014-06-08T07:34:37Z

Zhishp: /* stucture */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:

(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.

(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.

(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.

(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding(E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.

====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:33:27Z

Zhishp: /* Nuclear receptors */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:
(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.
(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).
(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.
(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.
(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding (E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.
====Nuclear receptors====

Subfamily 3: Estrogen Receptor-like

Group A: Estrogen receptor (Sex hormones: Estrogen)

1: Estrogen receptor-α (ERα; NR3A1, ESR1)

2: Estrogen receptor-β (ERβ; NR3A2, ESR2)

Group B: Estrogen related receptor

1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)

2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)

3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)

Group C: 3-Ketosteroid receptor

1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)

2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)

3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)

4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:29:25Z

Zhishp: /* Evolution */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===stucture===
Nuclear receptors are modular in structure and contain the following domains:
(A-B) N-terminal regulatory domain: Contains the activation function 1 (AF-1) whose action is independent of the presence of ligand.The transcriptional activation of AF-1 is normally very weak, but it does synergize with AF-2 in the E-domain (see below) to produce a more robust upregulation of gene expression. The A-B domain is highly variable in sequence between various nuclear receptors.
(C) DNA-binding domain (DBD): Highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).
(D) Hinge region: Thought to be a flexible domain that connects the DBD with the LBD. Influences intracellular trafficking and subcellular distribution.
(E) Ligand binding domain (LBD): Moderately conserved in sequence and highly conserved in structure between the various nuclear receptors. The structure of the LBD is referred to as an alpha helical sandwich fold in which three anti parallel alpha helices (the "sandwich filling") are flanked by two alpha helices on one side and three on the other (the "bread"). The ligand binding cavity is within the interior of the LBD and just below three anti parallel alpha helical sandwich "filling". Along with the DBD, the LBD contributes to the dimerization interface of the receptor and in addition, binds coactivator and corepressor proteins. The LBD also contains the activation function 2 (AF-2) whose action is dependent on the presence of bound ligand.
(F) C-terminal domain: Highly variable in sequence between various nuclear receptors.
The N-terminal (A/B), DNA-binding (C), and ligand binding (E) domains are independently well folded and structurally stable while the hinge region (D) and optional C-terminal (F) domains may be conformationally flexible and disordered.
====Nuclear receptors====
=====Subfamily 3: Estrogen Receptor-like=====
======Group A: Estrogen receptor (Sex hormones: Estrogen)======
1: Estrogen receptor-α (ERα; NR3A1, ESR1)
2: Estrogen receptor-β (ERβ; NR3A2, ESR2)
======Group B: Estrogen related receptor======
1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)
2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)
3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)
======Group C: 3-Ketosteroid receptors======
1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)
2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)
3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)
4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:26:41Z

Zhishp: /* Expression */

Please input one-sentence summary here.

==Annotated Information==
===Function===
Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription.
===Ligands===
Ligands that bind to and activate nuclear receptors include lipophilic substances such as endogenous hormones, vitamins A and D, and xenobiotic endocrine disruptors. Because the expression of a large number of genes is regulated by nuclear receptors, ligands that activate these receptors can have profound effects on the organism. Many of these regulated genes are associated with various diseases, which explains why the molecular targets of approximately 13% of U.S. Food and Drug Administration (FDA) approved drugs are nuclear receptors.
A number of nuclear receptors, referred to as orphan receptors, have no known (or at least generally agreed upon) endogenous ligands. Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and/or sterols with relatively low affinity. These receptors hence may function as metabolic sensors. Other nuclear receptors, such as CAR and PXR appear to function as xenobiotic sensors up-regulating the expression of cytochrome P450 enzymes that metabolize these xenobiotics.
[[File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg|200px|thumb|left|alt text]]

===Expression===
'''Genomic'''
Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.<ref name="ref1"/><ref name="ref2"/> Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus.

Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus.

After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA.

Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors.

'''Non-genomic'''
The cell membrane aldosterone receptor has shown to increase the activity of the basolateral Na/K ATPase, ENaC sodium channels and ROMK potassium channels of the principal cell in the distal tubule and cortical collecting duct of nephrons (as well as in the large bowel and possibly in sweat glands).

There is some evidence that certain steroid hormone receptors can extend through lipid bilayer membranes at the surface of cells and might be able to interact with hormones that remain outside of cells.<ref name="ref3"/>
Steroid hormone receptors can also function outside of the nucleus and couple to cytoplasmic signal transduction proteins such as PI3k and Akt kinase.<ref name="ref4"/>

===Evolution===
====Nuclear receptors====
=====Subfamily 3: Estrogen Receptor-like=====
======Group A: Estrogen receptor (Sex hormones: Estrogen)======
1: Estrogen receptor-α (ERα; NR3A1, ESR1)
2: Estrogen receptor-β (ERβ; NR3A2, ESR2)
======Group B: Estrogen related receptor======
1: Estrogen-related receptor-α (ERRα; NR3B1, ESRRA)
2: Estrogen-related receptor-β (ERRβ; NR3B2, ESRRB)
3: Estrogen-related receptor-γ (ERRγ; NR3B3, ESRRG)
======Group C: 3-Ketosteroid receptors======
1: Glucocorticoid receptor (GR; NR3C1) (Cortisol)
2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone)
3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone)
4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone)

==Labs working on this gene==
Please input related labs here.

=='''References'''==
<references>
<ref name="ref1">Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM (1995). "The nuclear receptor superfamily: the second decade". Cell 83 (6): 835–9. doi:10.1016/0092-8674(95)90199-X. PMID 852.</ref>
<ref name="ref2">Novac N, Heinzel T (2004). "Nuclear receptors: overview and classification". Curr Drug Targets Inflamm Allergy 3 (4): 335–46. doi:10.2174/1568010042634541. PMID 15584884.</ref>
<ref name="ref3">Luconi M, Francavilla F, Porazzi I, Macerola B, Forti G, Baldi E (August 2004). "Human spermatozoa as a model for studying membrane receptors mediating rapid nongenomic effects of progesterone and estrogens". Steroids 69 (8–9): 553–9. doi:10.1016/j.steroids.2004.05.013. PMID 15288769.</ref>
<ref name="ref4">Aquila S, Sisci D, Gentile M, Middea E, Catalano S, Carpino A, Rago V, Andò S (March 2004). "Estrogen receptor (ER)alpha and ER beta are both expressed in human ejaculated spermatozoa: evidence of their direct interaction with phosphatidylinositol-3-OH kinase/Akt pathway". J. Clin. Endocrinol. Metab. 89 (3): 1443–51. doi:10.1210/jc.2003-031681. PMID 15001646.</ref>
</references>

==Structured Information==
{{JaponicaGene|
GeneName = Os02g0100200|
Description = Steroid nuclear receptor, ligand-binding domain containing protein|
Version = NM_001052115.1 GI:115443600 GeneID:4327972|
Length = 4599 bp|
Definition = Oryza sativa Japonica Group Os02g0100200, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 2|Chromosome 2]]|
AP = Chromosome 2:9298..13896|
CDS = 9542..9762,11085..11196,11328..12749,12830..13624|
GCID = <gbrowseImage1>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008395:9298..13896
source=RiceChromosome02
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagactgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactag</cdnaseq>|
AA = <aaseq>MRKRTASDRIRVPSSNPAPSPSPPPPPPPPEEPAVPMPHVGARR STRVFVPKTPRPPQPSDPARVLRSGKRLAFSESPADAHWFQCKPNNCFHVHDHQRQLH DDPKPPPPPLPRTRSFGIVYSRKRRRRLPEPKEDTRFAIVFTRKRPKVAPFQHHAPND LATIPCSSSREFASRTGFFDSHFLTLVDCIPTNKADAAMLIVLVDSSCSGSSQHFLRL LLSVLRWMRSCRRGKVRNLASFLSSDAVATALALRGLHFVQLQCRRDCALSQRALVQC GWCELRGAKDSEPLLSVNFLAVPSYFQILHLLIALESMYLPAVIRTRMHLVGGAEEIY PRTLLEEDSESLSTGDTDPAVDLCSNKLCSVAQDYVPLEEIAGVVVHGLRLKKHQRKR SSMRHPLSRQRLAARFPDKVVATNQTDVARQTEADAPPSVSPELPLEPVKPKAALEIS LDLLENMDDSDVSTPIGSNGKQKRSSLKSPIERMNERLALAEVRQNIDSVHCRANLLI IQPDRCWREEGAEVMLEPSESNEWCIAVKIHGVNRISLKPSEQRFYVVNRFTHAYILA VDDGLKIEFSDKWDWLLFKELQIEGRERNSQGKMIPIPGVNEVSDDMGVIGTYPFSRP VPDYIRMADDEVGRALSRDSVYDLDSEDEQWLTQLNHSDSDRKSAHLNHISYEDFEKM ITTFEKDAFNNPEGTSDLDQILSRYPTLEKDHNVLAVHEYWINKRYKKGVPLLRILQG ATLRRGQLSQRSIKKKRSFKRQRSQAGRGKPDICLQDANGAEEEALRRVVEAERAATQ AGETAVRLRSRAQRLMAKAELVAYKSIMALRIAEAARISDSSRDLVLTTLD</aaseq>|
DNA = <dnaseqindica>4135..4355#2701..2812#1148..2569#273..1067#acccgcaaccccaacggaggaggaagggaagaagggaggaaaccctaaaattcctcttctccttctgctctcgattcgattcgatctcgtcgccacgcccccgcccccgcccccgccccgccccgcaagccgccgatctgttgcgcctcgtcaagaccccccagcccaagatctgattcgtttcgattccgagctgagcagcagcaggagcaggaggaggaggaggagctcatcgatttggtggttgctgatgggcggcgcatccatgttggatgaggaagcgcactgcatctgatcgcattcgggtcccctccagcaaccccgcgccatcgccgtcgccgccgccgccgccgccgccgccggaggaacctgccgtgcccatgccgcatgttggggcccgccgctccacgcgcgtcttcgtgcccaagacgcccaggccgcctcagccttctgatcctgccagggtcctccgctccggcaagcgcctcgccttctccgaatcccccgccgacgcccactggttccagtgcaagcccaacaactgcttccacgtccatgaccaccaacgccaacttcacgacgaccccaagccaccgccgccgcctctgccgcgcacaaggtccttcgggatcgtctacagcaggaagcgccgccgccgcctccccgaacccaaggaggacaccaggtttgccattgtcttcactaggaagagacccaaggtcgccccttttcagcaccacgccccgaacgaccttgccaccatcccatgctcctcttccagggagtttgcctccaggactggcttctttgattcccatttcttgaccctggtggattgtattcccactaataaagctgacgctgccatgcttattgtccttgtggattcatcttgctctgggagctctcagcacttcttgcgcctcctcctctctgtgctgcgctggatgcgtagctgccgacggggcaaggtccgaaaccttgcctcctttctctcgtccgatgctgtcgccactgcgcttgcattgcggggattgcattttgtccagcttcaatgccggagagacgtaagccttctacagacttaaaaagtgtgccagttttagttccttgtacacctggttaatgtgtatgccttttcttgcagtgtgcattgtcacagagggctttggtgcaatgtggctggtgtgagcttcgtggtgccaaggattctgaaccattgttgtctgtcaatttcttggcagtcccttcttacttccagattttgcacttgttaatagcactcgagtcaatgtatcttccagctgtgattcgtacgagaatgcatttggttggtggagctgaagaaatttatcctcgcaccctattggaggaggattctgaatctctgagcactggggatactgatcctgctgttgacctgtgtagcaacaaactttgcagtgtggctcaagattatgtgccccttgaagagattgcaggagtggtggtccatggtctgaggctaaagaagcatcaaaggaagagaagctctatgcggcatcccctcagtcgacagcgtcttgctgcaagatttcccgacaaggtagttgcaacaaaccagaccgatgtggctagacagacagaagcggatgcgccaccctcagttagtccggagcttccactggagcctgtcaaacctaaagcagcactggaaatctctcttgatttgcttgaaaacatggatgacagtgatgtttcaactcctataggatcaaatgggaagcaaaagaggtcttctttgaaaagtcccattgagcgcatgaatgaaaggttggctttggctgaggttagacagaatatagattctgttcactgcagagcaaaccttttaattattcaacctgataggtgctggagggaagaaggcgctgaagttatgctggaaccatcggaatcaaatgagtggtgtatagctgtgaagatacatggtgtcaatagaatatctctgaagccttcggagcagaggttttatgttgttaaccggttcacccatgcctatattttggcagttgatgatggattgaagattgagttctctgataaatgggactggcttttgtttaaggagttgcaaattgagggtcgggagcgcaattcccagggaaagatgataccaattcctggtgtaaatgaggtttctgatgacatgggagtgattggaacatatcctttttcacgccctgtgccagactatatcagaatggcggatgatgaggttgggcgagctctctcaagggactctgtatatgatctggattctgaggatgaacagtggctcacccagttgaatcattcagattctgacagaaaaagcgcacatcttaatcatatttcttatgaagattttgaaaagatgattaccacgtttgaaaaggatgctttcaacaaccctgaaggaactagtgatttggatcagattctttccagataccctactttggaaaaggaccataatgtccttgctgtgcatgaatattggataaacaagagatataagaaaggtgtaccactgctaaggatattgcaggtattttttgactttatcccttccccaaatattaatacaaagctggaaccttcacaaagattaccctctattgtctgcatatcctgaacttctggttatattttctaaatgttaaccttcttgatcattagggtgcaacactaagacgaggacaactgtcacaaagatctattaagaaaaaaagatctttcaagagacaaagaagccaagctggccgtggaaagcctgacatatgcttgcaaggtactgatgttttctccttgatgtctatcttactagagaattgggaccgccattggcgtggcccttcacttagttgaagcaagaaagcatcataaaagatacaagaagcttctttatccatttgtccgaagagtgacctcaattgatttcggaagccatgtgaatctttttttctttcacataagaaaccacatccttctatgcctgaaatatcaagcactcctaatattatatctaatcctacattttagcatctgtaaggttacagtgttagtttccctgcctctggtgtattaccaattttccatatcaaggtgcacaaagttgctaagtagatggccatggtattttagctacattcgatccagttggaaatagttgggtgtaaacatgtgtatatataattactttgataagaatggttacagaaaaatgcatgcataatttgtagtaatcggcaaactaacaaatctattggaaatgataacttctcactccatcccaaaatttatccagaagttgctatattttggggaggaggtggtaataaatttctacttgccacccttagtagatactacacagttaataaaatagcactaattgtggcatatataaatatgaaccttggatataacgtagaatacttgttgtgtaatgttatgtaaggaactctactaaaatatgaagcatgttatatgttctatcatatttttggtgaatgaaccactagtaattttgggcctatgtattcacaaacgaaacaactctcctatgaggcctaacaatagaatgcttgctccttgtgaggagagagtcctcggtgaattactttgggacaggttacagttagctattcagccagtgtctcaaacccttaataaatgctaatgtttagggcaaatagcacttatcatcaaaactatgattcagatgagatccatcatcgcagcttgtcgccaagaccaccttgttcacttgtagctttttcatccttttccaataatagttgcagatttattcttcaccttgtccctctcatctgctaggtgattcaactcctgtagcagcagatctgtgcaatcctagttcacaaacaatacaaactgcaaaacaatccagatcatgcttgatgaaagcatgctccctgtaattatgaagaaactaattactagtaacatttatgaccattgttccactggtacatgcatgcaagtttgtgtaccataacgtagcgtttttttatcccgatgttgcagactaagttcctactgaggggaaataatcttgtgttgtcttttactcgacatgttgatggacagatgctaatggtgctgaagaggaggctttgcggagagttgtggaagccgaacgtgctgcaacacaggcaggagaaacagctgttcgtctgcgcagtagagctcagcgtctcatggcaaaggctgagctggtggcatacaaatctattatggccctcaggattgctgaggctgctaggatatctgactcgtcacgggatcttgttttgacgaccctcgactagtgaagaatgtgagtgagatgttcattgatttgtgtgaagagcatagtagccaatagtttgttttcctcttttttgccgcatcatttcaatgctacgtggtatttggctttcgggtaagctgtgggctgtgggtctcttttttcctccccacctgttttaactttgtgaagccaatctttgtagcggatgcttgaactcaactgtaatctcttgtgtacatgatagtggttagttagattgtgtg</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001052115.1 RefSeq:Os02g0100200]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 2]]
[[Category:Chromosome 2]]

Os02g0100200

2014-06-08T07:25:09Z

Zhishp: /* References */

Os02g0100200

2014-06-08T07:18:11Z

Zhishp: /* References */

Os02g0100200

2014-06-08T07:16:55Z

Zhishp: /* References */

Os02g0100200

2014-06-08T07:11:31Z

Zhishp: /* Expression */

Os02g0100200

2014-06-08T07:03:48Z

Zhishp: /* Ligands */

Os05g0108800

2014-06-08T07:01:43Z

Zhishp: /* Expression */

''Os05g0108800'' encodes the protein Cytochrome b5.
==Annotated Information==
The sequence of ''Os05g0108800''is same to ''Cb5'' in tobacco, which encodes cytochrome b5.
===Function===
cytochrome b5 is a small haem protein associated with the endoplasmic reticulum of higher plants, animals and fungi<ref name="ref1&2"/> . The role of cytochrome b5 in plants is involving in the desaturation of acyl-complex lipids in oilseeds<ref name="ref3&4"/> .
A full-length clone encoding cytochrome b5 has been isolated from a tobacco leaf cDNA library in lambda gt11 by PCR using degenerate primers. Southern analysis indicated that more than one gene encodes cytochrome b5 in the tobacco genome. In vitro transcription and translation studies of the cDNA indicated that the protein inserts into the ER membrane by a non-SRP-mediated pathway and that the C-terminus of the protein is required for targeting and insertion<ref name="ref5"/> .

===Expression===
In the developing tobacco seed the mRNA is abundant at very early stages (< 10 days after flowering).<ref name="ref5"/> 
[[File:640px-1jex cyto b5.png|200px|thumb|left|alt text]]

===Evolution===
This cDNA encodes a protein of 139 residues which exhibits a high degree of homology to other cytochrome b5s, the message for which is expressed predominantly in developing seeds and in pigmented flower tissue.
You can also add sub-section(s) at will.

==Labs working on this gene==
Please input related labs here.

==References==
[1]Ozols J: Structure of cytochromeb 5 and its topology in the microsomal membrane. Biochim Biophys Acta 997 121–130 (1989).
[2]Rich PR, Bendall DS: Cytochrome components of plant microsomes. Eur J Biochem 55: 333–341 (1975).
[3]Kearns EV, Hugly S, Somerville CR: The role of cytochromeb 5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch Biochem Biophys 284: 431–436 (1991).
[4]Smith MA, Cross AR, Jones OTG, Griffiths WT, Stymne S, Stobart AK: Electron transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine 537–1 (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem J 272: 23–29 (1990).
[5]Mark A. Smith, A. Keith Stobart, Peter R. Shewry, Johnathan A. Napier:Tobacco cytochromeb 5: cDNA isolation, expression analysis andin vitro protein targeting. Plant Molecular Biology: 527-537(1994)

==Structured Information==
{{JaponicaGene|
GeneName = Os05g0108800|
Description = Cytochrome b5|
Version = NM_001060969.1 GI:115461668 GeneID:4337583|
Length = 1812 bp|
Definition = Oryza sativa Japonica Group Os05g0108800, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 5|Chromosome 5]]|
AP = Chromosome 5:470434..472245|
CDS = 470569..470658,471609..471675,471795..472051|
GCID = <gbrowseImage1>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttag</cdnaseq>|
AA = <aaseq>MSNDNKKVYTLEEVAKHNSKDDCWLIIGGKVYNVSKFLEDHPGG DDVLLSSTGKDATDDFEDVGHSTTARAMMDEYYVGDIDTSTIPARTKYVPPKQPHYNQ DKTPEFIIKILQFLVPLAILGLAVAIRIYTKSESA</aaseq>|
DNA = <dnaseqindica>136..225#1176..1242#1362..1618#atccccacgagacgagaaacctagcaaaaatctcgtctttcgccgcgctctccctcctctgattcctgctgttcttgatcttggatctcaattcccaaccaagaacacacagacagagaaaggaaggagaagaagatgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtctcatcttttgtttttcttttcttttcacgcttttacttacttgtactattcgatttcatgtttcgattcgtttcgttggttcttggttccctatcctccaacaacgtcctgagacctcgatctggtcggagtccacgaccagatcttggccgcggcgcagatctggccctccagccgccggcgtggggaccttgccagatctggtcttctccgacggtggccaacttctcttgtcccttggttgcagccaccaaacctcttcctcccctcctcgatccaaccttggtcttgttcatcgactggccactaaaccccaaataagcgagatagaatttggattcgtttcgttggttattgtttctctgatgctgtgatggtggctagatcatggcagatctgcccagtaaagtcgaattttgtttgattccaccgcacctcctgaggaatcggtccaatcctgtgaattcttctcttctttcctgctgattggattgtctacatgggctttacctggaaacaggggtgagtgctagcagattcaaacatcatggactgactgctcctaaacaagttccatatgaaaacctgttctacatgctttttttcttttactcttcactcgttgtcagtcaaacactgcaaaatttgtccctgcgcctattctgcaagagcttcttgttagtacaactgaagaatcaatcctctgttccaacttggcatctggacagaataatgaatgtttcataggaaaggctcagctcaactaagtaaatcatgttgattggccttaaaacacacttcattaagagtctgttttttttatattggacatgataagaataatatggctgttttttattattaatgttttttcttggtaacagtgcttctattgatgaacctaccctgtttacctgatctcaccagtgttctgcaatactatccaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggtacgccttctcaattctcatgttctggccttctgagtagtgaccactactgatgaattaactgagtttgcaatggatggtttagcttacactttgaaatatacatggaccttctgcaggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttagtgctgttctcttagtgttataagagtggaaggtaccgaataagttagcaagagttttgtgtgattcataccagtgtaacatgtcatgaattcgtcgaatgttctgaagatgctgtgggttttgtggtcctgggatgtccacttcggtaaagatcgataagattcaaagtactcgttaatcgttatacattctga</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001060969.1 RefSeq:Os05g0108800]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 5]]
[[Category:Chromosome 5]]

Os05g0108800

2014-06-08T06:59:05Z

Zhishp: /* Expression */

''Os05g0108800'' encodes the protein Cytochrome b5.
==Annotated Information==
The sequence of ''Os05g0108800''is same to ''Cb5'' in tobacco, which encodes cytochrome b5.
===Function===
cytochrome b5 is a small haem protein associated with the endoplasmic reticulum of higher plants, animals and fungi<ref name="ref1&2"/> . The role of cytochrome b5 in plants is involving in the desaturation of acyl-complex lipids in oilseeds<ref name="ref3&4"/> .
A full-length clone encoding cytochrome b5 has been isolated from a tobacco leaf cDNA library in lambda gt11 by PCR using degenerate primers. Southern analysis indicated that more than one gene encodes cytochrome b5 in the tobacco genome. In vitro transcription and translation studies of the cDNA indicated that the protein inserts into the ER membrane by a non-SRP-mediated pathway and that the C-terminus of the protein is required for targeting and insertion<ref name="ref5"/> .

===Expression===
In the developing tobacco seed the mRNA is abundant at very early stages (< 10 days after flowering).<ref name="ref5"/> 
[[File:640px-1jex cyto b5.png]]

===Evolution===
This cDNA encodes a protein of 139 residues which exhibits a high degree of homology to other cytochrome b5s, the message for which is expressed predominantly in developing seeds and in pigmented flower tissue.
You can also add sub-section(s) at will.

==Labs working on this gene==
Please input related labs here.

==References==
[1]Ozols J: Structure of cytochromeb 5 and its topology in the microsomal membrane. Biochim Biophys Acta 997 121–130 (1989).
[2]Rich PR, Bendall DS: Cytochrome components of plant microsomes. Eur J Biochem 55: 333–341 (1975).
[3]Kearns EV, Hugly S, Somerville CR: The role of cytochromeb 5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch Biochem Biophys 284: 431–436 (1991).
[4]Smith MA, Cross AR, Jones OTG, Griffiths WT, Stymne S, Stobart AK: Electron transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine 537–1 (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem J 272: 23–29 (1990).
[5]Mark A. Smith, A. Keith Stobart, Peter R. Shewry, Johnathan A. Napier:Tobacco cytochromeb 5: cDNA isolation, expression analysis andin vitro protein targeting. Plant Molecular Biology: 527-537(1994)

==Structured Information==
{{JaponicaGene|
GeneName = Os05g0108800|
Description = Cytochrome b5|
Version = NM_001060969.1 GI:115461668 GeneID:4337583|
Length = 1812 bp|
Definition = Oryza sativa Japonica Group Os05g0108800, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 5|Chromosome 5]]|
AP = Chromosome 5:470434..472245|
CDS = 470569..470658,471609..471675,471795..472051|
GCID = <gbrowseImage1>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttag</cdnaseq>|
AA = <aaseq>MSNDNKKVYTLEEVAKHNSKDDCWLIIGGKVYNVSKFLEDHPGG DDVLLSSTGKDATDDFEDVGHSTTARAMMDEYYVGDIDTSTIPARTKYVPPKQPHYNQ DKTPEFIIKILQFLVPLAILGLAVAIRIYTKSESA</aaseq>|
DNA = <dnaseqindica>136..225#1176..1242#1362..1618#atccccacgagacgagaaacctagcaaaaatctcgtctttcgccgcgctctccctcctctgattcctgctgttcttgatcttggatctcaattcccaaccaagaacacacagacagagaaaggaaggagaagaagatgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtctcatcttttgtttttcttttcttttcacgcttttacttacttgtactattcgatttcatgtttcgattcgtttcgttggttcttggttccctatcctccaacaacgtcctgagacctcgatctggtcggagtccacgaccagatcttggccgcggcgcagatctggccctccagccgccggcgtggggaccttgccagatctggtcttctccgacggtggccaacttctcttgtcccttggttgcagccaccaaacctcttcctcccctcctcgatccaaccttggtcttgttcatcgactggccactaaaccccaaataagcgagatagaatttggattcgtttcgttggttattgtttctctgatgctgtgatggtggctagatcatggcagatctgcccagtaaagtcgaattttgtttgattccaccgcacctcctgaggaatcggtccaatcctgtgaattcttctcttctttcctgctgattggattgtctacatgggctttacctggaaacaggggtgagtgctagcagattcaaacatcatggactgactgctcctaaacaagttccatatgaaaacctgttctacatgctttttttcttttactcttcactcgttgtcagtcaaacactgcaaaatttgtccctgcgcctattctgcaagagcttcttgttagtacaactgaagaatcaatcctctgttccaacttggcatctggacagaataatgaatgtttcataggaaaggctcagctcaactaagtaaatcatgttgattggccttaaaacacacttcattaagagtctgttttttttatattggacatgataagaataatatggctgttttttattattaatgttttttcttggtaacagtgcttctattgatgaacctaccctgtttacctgatctcaccagtgttctgcaatactatccaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggtacgccttctcaattctcatgttctggccttctgagtagtgaccactactgatgaattaactgagtttgcaatggatggtttagcttacactttgaaatatacatggaccttctgcaggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttagtgctgttctcttagtgttataagagtggaaggtaccgaataagttagcaagagttttgtgtgattcataccagtgtaacatgtcatgaattcgtcgaatgttctgaagatgctgtgggttttgtggtcctgggatgtccacttcggtaaagatcgataagattcaaagtactcgttaatcgttatacattctga</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001060969.1 RefSeq:Os05g0108800]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 5]]
[[Category:Chromosome 5]]

Os05g0108800

2014-06-08T06:53:52Z

Zhishp: /* Expression */

''Os05g0108800'' encodes the protein Cytochrome b5.
==Annotated Information==
The sequence of ''Os05g0108800''is same to ''Cb5'' in tobacco, which encodes cytochrome b5.
===Function===
cytochrome b5 is a small haem protein associated with the endoplasmic reticulum of higher plants, animals and fungi<ref name="ref1&2"/> . The role of cytochrome b5 in plants is involving in the desaturation of acyl-complex lipids in oilseeds<ref name="ref3&4"/> .
A full-length clone encoding cytochrome b5 has been isolated from a tobacco leaf cDNA library in lambda gt11 by PCR using degenerate primers. Southern analysis indicated that more than one gene encodes cytochrome b5 in the tobacco genome. In vitro transcription and translation studies of the cDNA indicated that the protein inserts into the ER membrane by a non-SRP-mediated pathway and that the C-terminus of the protein is required for targeting and insertion<ref name="ref5"/> .

===Expression===
In the developing tobacco seed the mRNA is abundant at very early stages (< 10 days after flowering).<ref name="ref5"/> 
[[File:cytochorome b5.jpg]]

===Evolution===
This cDNA encodes a protein of 139 residues which exhibits a high degree of homology to other cytochrome b5s, the message for which is expressed predominantly in developing seeds and in pigmented flower tissue.
You can also add sub-section(s) at will.

==Labs working on this gene==
Please input related labs here.

==References==
[1]Ozols J: Structure of cytochromeb 5 and its topology in the microsomal membrane. Biochim Biophys Acta 997 121–130 (1989).
[2]Rich PR, Bendall DS: Cytochrome components of plant microsomes. Eur J Biochem 55: 333–341 (1975).
[3]Kearns EV, Hugly S, Somerville CR: The role of cytochromeb 5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch Biochem Biophys 284: 431–436 (1991).
[4]Smith MA, Cross AR, Jones OTG, Griffiths WT, Stymne S, Stobart AK: Electron transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine 537–1 (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem J 272: 23–29 (1990).
[5]Mark A. Smith, A. Keith Stobart, Peter R. Shewry, Johnathan A. Napier:Tobacco cytochromeb 5: cDNA isolation, expression analysis andin vitro protein targeting. Plant Molecular Biology: 527-537(1994)

==Structured Information==
{{JaponicaGene|
GeneName = Os05g0108800|
Description = Cytochrome b5|
Version = NM_001060969.1 GI:115461668 GeneID:4337583|
Length = 1812 bp|
Definition = Oryza sativa Japonica Group Os05g0108800, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 5|Chromosome 5]]|
AP = Chromosome 5:470434..472245|
CDS = 470569..470658,471609..471675,471795..472051|
GCID = <gbrowseImage1>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttag</cdnaseq>|
AA = <aaseq>MSNDNKKVYTLEEVAKHNSKDDCWLIIGGKVYNVSKFLEDHPGG DDVLLSSTGKDATDDFEDVGHSTTARAMMDEYYVGDIDTSTIPARTKYVPPKQPHYNQ DKTPEFIIKILQFLVPLAILGLAVAIRIYTKSESA</aaseq>|
DNA = <dnaseqindica>136..225#1176..1242#1362..1618#atccccacgagacgagaaacctagcaaaaatctcgtctttcgccgcgctctccctcctctgattcctgctgttcttgatcttggatctcaattcccaaccaagaacacacagacagagaaaggaaggagaagaagatgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtctcatcttttgtttttcttttcttttcacgcttttacttacttgtactattcgatttcatgtttcgattcgtttcgttggttcttggttccctatcctccaacaacgtcctgagacctcgatctggtcggagtccacgaccagatcttggccgcggcgcagatctggccctccagccgccggcgtggggaccttgccagatctggtcttctccgacggtggccaacttctcttgtcccttggttgcagccaccaaacctcttcctcccctcctcgatccaaccttggtcttgttcatcgactggccactaaaccccaaataagcgagatagaatttggattcgtttcgttggttattgtttctctgatgctgtgatggtggctagatcatggcagatctgcccagtaaagtcgaattttgtttgattccaccgcacctcctgaggaatcggtccaatcctgtgaattcttctcttctttcctgctgattggattgtctacatgggctttacctggaaacaggggtgagtgctagcagattcaaacatcatggactgactgctcctaaacaagttccatatgaaaacctgttctacatgctttttttcttttactcttcactcgttgtcagtcaaacactgcaaaatttgtccctgcgcctattctgcaagagcttcttgttagtacaactgaagaatcaatcctctgttccaacttggcatctggacagaataatgaatgtttcataggaaaggctcagctcaactaagtaaatcatgttgattggccttaaaacacacttcattaagagtctgttttttttatattggacatgataagaataatatggctgttttttattattaatgttttttcttggtaacagtgcttctattgatgaacctaccctgtttacctgatctcaccagtgttctgcaatactatccaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggtacgccttctcaattctcatgttctggccttctgagtagtgaccactactgatgaattaactgagtttgcaatggatggtttagcttacactttgaaatatacatggaccttctgcaggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttagtgctgttctcttagtgttataagagtggaaggtaccgaataagttagcaagagttttgtgtgattcataccagtgtaacatgtcatgaattcgtcgaatgttctgaagatgctgtgggttttgtggtcctgggatgtccacttcggtaaagatcgataagattcaaagtactcgttaatcgttatacattctga</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001060969.1 RefSeq:Os05g0108800]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 5]]
[[Category:Chromosome 5]]

Os05g0108800

2014-06-08T06:53:29Z

Zhishp: /* Expression */

''Os05g0108800'' encodes the protein Cytochrome b5.
==Annotated Information==
The sequence of ''Os05g0108800''is same to ''Cb5'' in tobacco, which encodes cytochrome b5.
===Function===
cytochrome b5 is a small haem protein associated with the endoplasmic reticulum of higher plants, animals and fungi<ref name="ref1&2"/> . The role of cytochrome b5 in plants is involving in the desaturation of acyl-complex lipids in oilseeds<ref name="ref3&4"/> .
A full-length clone encoding cytochrome b5 has been isolated from a tobacco leaf cDNA library in lambda gt11 by PCR using degenerate primers. Southern analysis indicated that more than one gene encodes cytochrome b5 in the tobacco genome. In vitro transcription and translation studies of the cDNA indicated that the protein inserts into the ER membrane by a non-SRP-mediated pathway and that the C-terminus of the protein is required for targeting and insertion<ref name="ref5"/> .

===Expression===
In the developing tobacco seed the mRNA is abundant at very early stages (< 10 days after flowering).<ref name="ref5"/> 
[[File:cytochorome b5.png]]

===Evolution===
This cDNA encodes a protein of 139 residues which exhibits a high degree of homology to other cytochrome b5s, the message for which is expressed predominantly in developing seeds and in pigmented flower tissue.
You can also add sub-section(s) at will.

==Labs working on this gene==
Please input related labs here.

==References==
[1]Ozols J: Structure of cytochromeb 5 and its topology in the microsomal membrane. Biochim Biophys Acta 997 121–130 (1989).
[2]Rich PR, Bendall DS: Cytochrome components of plant microsomes. Eur J Biochem 55: 333–341 (1975).
[3]Kearns EV, Hugly S, Somerville CR: The role of cytochromeb 5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch Biochem Biophys 284: 431–436 (1991).
[4]Smith MA, Cross AR, Jones OTG, Griffiths WT, Stymne S, Stobart AK: Electron transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine 537–1 (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem J 272: 23–29 (1990).
[5]Mark A. Smith, A. Keith Stobart, Peter R. Shewry, Johnathan A. Napier:Tobacco cytochromeb 5: cDNA isolation, expression analysis andin vitro protein targeting. Plant Molecular Biology: 527-537(1994)

==Structured Information==
{{JaponicaGene|
GeneName = Os05g0108800|
Description = Cytochrome b5|
Version = NM_001060969.1 GI:115461668 GeneID:4337583|
Length = 1812 bp|
Definition = Oryza sativa Japonica Group Os05g0108800, complete gene.|
Source = Oryza sativa Japonica Group

ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
Chromosome = [[:category:Japonica Chromosome 5|Chromosome 5]]|
AP = Chromosome 5:470434..472245|
CDS = 470569..470658,471609..471675,471795..472051|
GCID = <gbrowseImage1>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008398:470434..472245
source=RiceChromosome05
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttag</cdnaseq>|
AA = <aaseq>MSNDNKKVYTLEEVAKHNSKDDCWLIIGGKVYNVSKFLEDHPGG DDVLLSSTGKDATDDFEDVGHSTTARAMMDEYYVGDIDTSTIPARTKYVPPKQPHYNQ DKTPEFIIKILQFLVPLAILGLAVAIRIYTKSESA</aaseq>|
DNA = <dnaseqindica>136..225#1176..1242#1362..1618#atccccacgagacgagaaacctagcaaaaatctcgtctttcgccgcgctctccctcctctgattcctgctgttcttgatcttggatctcaattcccaaccaagaacacacagacagagaaaggaaggagaagaagatgtcgaacgacaacaagaaggtgtataccctggaggaggtcgccaagcacaactccaaggacgactgctggctcatcatcggcggaaaggtctcatcttttgtttttcttttcttttcacgcttttacttacttgtactattcgatttcatgtttcgattcgtttcgttggttcttggttccctatcctccaacaacgtcctgagacctcgatctggtcggagtccacgaccagatcttggccgcggcgcagatctggccctccagccgccggcgtggggaccttgccagatctggtcttctccgacggtggccaacttctcttgtcccttggttgcagccaccaaacctcttcctcccctcctcgatccaaccttggtcttgttcatcgactggccactaaaccccaaataagcgagatagaatttggattcgtttcgttggttattgtttctctgatgctgtgatggtggctagatcatggcagatctgcccagtaaagtcgaattttgtttgattccaccgcacctcctgaggaatcggtccaatcctgtgaattcttctcttctttcctgctgattggattgtctacatgggctttacctggaaacaggggtgagtgctagcagattcaaacatcatggactgactgctcctaaacaagttccatatgaaaacctgttctacatgctttttttcttttactcttcactcgttgtcagtcaaacactgcaaaatttgtccctgcgcctattctgcaagagcttcttgttagtacaactgaagaatcaatcctctgttccaacttggcatctggacagaataatgaatgtttcataggaaaggctcagctcaactaagtaaatcatgttgattggccttaaaacacacttcattaagagtctgttttttttatattggacatgataagaataatatggctgttttttattattaatgttttttcttggtaacagtgcttctattgatgaacctaccctgtttacctgatctcaccagtgttctgcaatactatccaggtatacaatgtgtcgaaattccttgaggaccatccaggaggtgatgatgtcttgctatcttcaactggtacgccttctcaattctcatgttctggccttctgagtagtgaccactactgatgaattaactgagtttgcaatggatggtttagcttacactttgaaatatacatggaccttctgcaggcaaggacgcgactgacgattttgaggatgtcgggcacagcacgactgctcgtgcgatgatggatgagtattacgttggcgacatcgacacatccacaatacccgcgaggacgaagtacgttcccccaaagcaaccacactacaaccaggacaagaccccggagttcatcatcaagatcctccagttcttggttcccctcgccatattgggcctggctgttgcaattaggatctacaccaagtcggagtccgcttagtgctgttctcttagtgttataagagtggaaggtaccgaataagttagcaagagttttgtgtgattcataccagtgtaacatgtcatgaattcgtcgaatgttctgaagatgctgtgggttttgtggtcctgggatgtccacttcggtaaagatcgataagattcaaagtactcgttaatcgttatacattctga</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001060969.1 RefSeq:Os05g0108800]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 5]]
[[Category:Chromosome 5]]

Os02g0100200

2014-06-08T06:42:27Z

Zhishp: /* Ligands */

File:Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.jpg

2014-06-08T06:40:43Z

Zhishp:

Os02g0100200

2014-06-08T06:32:54Z

Zhishp: /* Ligands */

Os02g0100200

2014-06-08T06:31:58Z

Zhishp: /* Function */

Os02g0100200

2014-06-08T06:28:47Z

Zhishp: /* Evolution */

Os02g0100200

2014-06-08T06:27:43Z

Zhishp: /* Evolution */

Os02g0100200

2014-06-08T06:25:56Z

Zhishp: /* Evolution */

Os02g0100200

2014-06-08T06:23:20Z

Zhishp: /* Expression */

Os02g0100200

2014-06-08T06:22:39Z

Zhishp: /* Expression */

Os02g0100200

2014-06-08T06:19:21Z

Zhishp: /* Annotated Information */