Difference between revisions of "Os12g0100500"

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Please input one-sentence summary here.
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The rice gene '''''Os12g0100500''''' was not functionally studied yet.
  
 
==Annotated Information==
 
==Annotated Information==
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''Os12g0100500'' in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein [Hordeum vulgare subsp. vulgare]. This gene is predicted to be coding Lysophospholipase [Lipid metabolism]; COG2267.   
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* ''Os12g0100500'' in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein.  
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* This gene is predicted to be coding Lysophospholipase [Lipid metabolism]; COG2267.   
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===Gene Symbol===
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*'''''Os12g0100500''''' '''''<=>''''' '''''COG2267, OsCOG2267'''''
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===Function===
 
===Function===
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In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction
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* In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction
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* 2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate
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2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate
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* Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate.
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Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate.
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* This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.  
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This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008. Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.[1] Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids,[2] the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.[2]
 
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===Expression===
 
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Please input expression information here.
 
  
 
===Evolution===
 
===Evolution===
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Please input evolution information here.
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* This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008.
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* Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.
 +
* Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids,
 +
* the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.
  
 
You can also add sub-section(s) at will.
 
You can also add sub-section(s) at will.
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==References==
 
==References==
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[1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
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* [1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
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[2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.
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* [2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.
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==Structured Information==
 
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{{JaponicaGene|
 
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GeneName = Os12g0100500|
 
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Description = Alpha/beta hydrolase family protein|
 
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Version = NM_001071764.1 GI:115486849 GeneID:4351238|
 
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Length = 1294 bp|
 
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Definition = Oryza sativa Japonica Group Os12g0100500, complete gene.|
 
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Source = Oryza sativa Japonica Group
 
  
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  ORGANISM  Oryza sativa Japonica Group
 
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            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 
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            Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
 
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            clade; Ehrhartoideae; Oryzeae; Oryza.
 
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|
 
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Chromosome = [[:category:Japonica Chromosome 12|Chromosome 12]]|
 
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AP = Chromosome 12:11806..13099|
 
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CDS = 11806..12363,12659..13099|
 
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GCID = <gbrowseImage1>
 
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name=NC_008405:11806..13099
 
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source=RiceChromosome12
 
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preset=GeneLocation
 
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</gbrowseImage1>|
 
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GSID = <gbrowseImage2>
 
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name=NC_008405:11806..13099
 
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source=RiceChromosome12
 
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preset=GeneLocation
 
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</gbrowseImage2>|
 
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CDNA = <cdnaseq>atgagcagcagcagcggcggcgatgggggtgggtacaattactcggaggattgggtggtgaattcgcgagggatgcggctcttcacctgcgcgtggattcccaaggagagcagtagaggcgtggtttgcctgtgccatgggtacgcggtggagtgcagcgtgacgatgcgcggcacggcggagcggctggccagggcgggctacgccgtccacggcatcgactacgagggccacggccactccgacggcctccagggctacgtccccgacctcgacgccctcgtccgcgactgcgactccttcttctccaccgccaccgcctccttcccccgccgcagattcctcctcggcgagtccatgggcggcgccgtcgcccttcttctccaccgcttgcgccccgacttctggaccggcgccattctcgtcgcccccatgtgcaagatcgcggaggagatgcggccgcacccgatggtggtgagcgtgctgaaggtgatgacaagcatcataccgacgtggcgggtggtgccgacgaatgacgtgatcgacctggcatacaggatgcaggggaagcgagacgagatccgagggaacccactgtgctacaagggcaggccccgcctcaagaccgcctacgagctgctccgcgtcagcatcctcatcgagtccaccatcctcccccacgtctccctccccttcctcatcctccacggcgccgccgaccgggtcaccgacccctccgtcagcgacctcctctaccgctccgcctccaccaccgacaagaccttccacctctacaccggcatgtggcacgccctcacctccggcgaactccctcacaacatcgatgccgtcttccgcgacatcatcgactggctccaccacaggacatcccccacctccgcttcacatgtgcaggaccacgacttaagtacgtctttcgaggcggagcgcaaggccaagcacgacgacaccatccattgcggcaagcaaacatcatag</cdnaseq>|
 
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AA = <aaseq>MSSSSGGDGGGYNYSEDWVVNSRGMRLFTCAWIPKESSRGVVCL                    CHGYAVECSVTMRGTAERLARAGYAVHGIDYEGHGHSDGLQGYVPDLDALVRDCDSFF                    STATASFPRRRFLLGESMGGAVALLLHRLRPDFWTGAILVAPMCKIAEEMRPHPMVVS                    VLKVMTSIIPTWRVVPTNDVIDLAYRMQGKRDEIRGNPLCYKGRPRLKTAYELLRVSI                    LIESTILPHVSLPFLILHGAADRVTDPSVSDLLYRSASTTDKTFHLYTGMWHALTSGE                    LPHNIDAVFRDIIDWLHHRTSPTSASHVQDHDLSTSFEAERKAKHDDTIHCGKQTS</aaseq>|
 
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DNA = <dnaseqindica>737..1294#1..441#atgagcagcagcagcggcggcgatgggggtgggtacaattactcggaggattgggtggtgaattcgcgagggatgcggctcttcacctgcgcgtggattcccaaggagagcagtagaggcgtggtttgcctgtgccatgggtacgcggtggagtgcagcgtgacgatgcgcggcacggcggagcggctggccagggcgggctacgccgtccacggcatcgactacgagggccacggccactccgacggcctccagggctacgtccccgacctcgacgccctcgtccgcgactgcgactccttcttctccaccgccaccgcctccttcccccgccgcagattcctcctcggcgagtccatgggcggcgccgtcgcccttcttctccaccgcttgcgccccgacttctggaccggcgccattctcgtcgcccccatgtgcaaggtccgttcaactccatcttaacctttgactctgacttttcctttttctttttgcccgccacatgcatgccatccacgaatcattcagtctacatatgcgtccccaagattagattagatatttagattatactacataacagaacaggctgtctctttctcattttctaagctacctaccggccggccactttcagattattatcttcttttaacgcaacgcaaggaaacgtttctgactgcctcaaatatcatggatgcatgtggttgaatactagtaaaatgcgtggttgcagatcgcggaggagatgcggccgcacccgatggtggtgagcgtgctgaaggtgatgacaagcatcataccgacgtggcgggtggtgccgacgaatgacgtgatcgacctggcatacaggatgcaggggaagcgagacgagatccgagggaacccactgtgctacaagggcaggccccgcctcaagaccgcctacgagctgctccgcgtcagcatcctcatcgagtccaccatcctcccccacgtctccctccccttcctcatcctccacggcgccgccgaccgggtcaccgacccctccgtcagcgacctcctctaccgctccgcctccaccaccgacaagaccttccacctctacaccggcatgtggcacgccctcacctccggcgaactccctcacaacatcgatgccgtcttccgcgacatcatcgactggctccaccacaggacatcccccacctccgcttcacatgtgcaggaccacgacttaagtacgtctttcgaggcggagcgcaaggccaagcacgacgacaccatccattgcggcaagcaaacatcatag</dnaseqindica>|
 
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Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001071764.1 RefSeq:Os12g0100500]|
 
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}}
 
 
[[Category:Genes]]
 
[[Category:Genes]]
 
[[Category:Japonica mRNA]]
 
[[Category:Japonica mRNA]]
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[[Category:Japonica Chromosome 12]]
 
[[Category:Japonica Chromosome 12]]
 
[[Category:Chromosome 12]]
 
[[Category:Chromosome 12]]
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== Structured Information ==

Latest revision as of 09:29, 8 May 2017

The rice gene Os12g0100500 was not functionally studied yet.

Annotated Information

  • Os12g0100500 in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein.
  • This gene is predicted to be coding Lysophospholipase [Lipid metabolism]; COG2267.

Gene Symbol

  • Os12g0100500 <=> COG2267, OsCOG2267

Function

  • In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction
  • 2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate
  • Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate.
  • This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.

Evolution

  • This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008.
  • Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.
  • Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids,
  • the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.

You can also add sub-section(s) at will.

Labs working on this gene

Please input related labs here.

References

  • [1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
  • [2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.

Structured Information