|
|
||
|
|
|
|
|
UniProt functional annotation for P22203 | ||
|
|
|
|
|
|
||
| UniProt code: P22203. |
|
||
| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
|
||
|
||
| Function: | |
Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. |
|
||
| Subunit: | |
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). VMA4 forms a homodimer within this complex and interacts directly with VMA5 and VMA10. Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V- ATPase. {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:15751969, ECO:0000269|PubMed:2145285, ECO:0000269|PubMed:8416931}. |
| Subcellular location: | |
Vacuole membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}. |
| Miscellaneous: | |
Present with 16134 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the V-ATPase E subunit family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.