Basic Information
Gene ID
Juni_Chr9.724.g
Position
Chr9:13521146-13523079 (-)
1933bp
Gene Type
gene
Gene Description (Protein Product)
P-P-bond-hydrolysis-driven protein transmembrane transporter activity
Organism
Also AS AT5G50460

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description


Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
GO Term Description GO Category
GO:0000003 reproduction BP
GO:0001555 oocyte growth BP
GO:0003006 developmental process involved in reproduction BP
GO:0003674 molecular_function MF
GO:0005215 transporter activity MF
GO:0005575 cellular_component CC
GO:0005623 obsolete cell CC
GO:0006810 transport BP
GO:0006886 intracellular protein transport BP
GO:0007276 gamete generation BP
GO:0007281 germ cell development BP
GO:0007292 female gamete generation BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0008320 protein transmembrane transporter activity MF
GO:0008565 obsolete protein transporter activity MF
GO:0009987 cellular process BP
GO:0009994 oocyte differentiation BP
GO:0015031 protein transport BP
GO:0015399 primary active transmembrane transporter activity MF
GO:0015405 ATPase-coupled transmembrane transporter activity MF
GO:0015450 protein-transporting ATPase activity MF
GO:0015833 peptide transport BP
GO:0016049 cell growth BP
GO:0019953 sexual reproduction BP
GO:0022412 cellular process involved in reproduction in multicellular organism BP
GO:0022414 reproductive process BP
GO:0022804 active transmembrane transporter activity MF
GO:0022857 transmembrane transporter activity MF
GO:0022884 macromolecule transmembrane transporter activity MF
GO:0030154 cell differentiation BP
GO:0030728 ovulation BP
GO:0032501 multicellular organismal process BP
GO:0032502 developmental process BP
GO:0032504 multicellular organism reproduction BP
GO:0033036 macromolecule localization BP
GO:0034613 protein localization BP
GO:0040007 growth BP
GO:0042886 amide transport BP
GO:0042887 amide transmembrane transporter activity MF
GO:0044703 multi-organism reproductive process BP
GO:0045184 establishment of protein localization BP
GO:0046907 intracellular transport BP
GO:0048468 cell development BP
GO:0048477 oogenesis BP
GO:0048588 developmental cell growth BP
GO:0048589 developmental growth BP
GO:0048599 oocyte development BP
GO:0048609 multicellular organismal reproductive process BP
GO:0048856 anatomical structure development BP
GO:0048869 cellular developmental process BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0051704 obsolete multi-organism process BP
GO:0055085 transmembrane transport BP
GO:0070727 cellular macromolecule localization BP
GO:0071702 organic substance transport BP
GO:0071705 nitrogen compound transport BP
GO:0071806 protein transmembrane transport BP
GO:1904680 peptide transmembrane transporter activity MF
KEGG Term Name Description
map04145 Phagosome Phagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is formed when the specific receptors on the phagocyte surface recognize ligands on the particle surface. After formation, nascent phagosomes progressively acquire digestive characteristics. This maturation of phagosomes involves regulated interaction with the other membrane organelles, including recycling endosomes, late endosomes and lysosomes. The fusion of phagosomes and lysosomes releases toxic products that kill most bacteria and degrade them into fragments. However, some bacteria have strategies to escape the bactericidal mechanisms associated with phagocytosis and survive within host phagocytes.
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
map03060 Protein export The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role.