| Standard Name | VMA5 (see Nomenclature conflict Note) |
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| Systematic Name | YKL080W |
| Alias | CSL5 , VAT3 |
| Feature Type | ORF, Verified |
| Description | Subunit C of the eight-subunit V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane (1, 2 and see Summary Paragraph) |
| Chromosomal Location | |
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| View Computational GO annotations for VMA5 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| 107 total interaction(s) for 77 unique genes/features. | |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000001563 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| CBF2 | Nomenclature conflict | CSL5 has been used in the literature to refer to both CBF2/YGR140W (Baker, RE. et al. (1998) Genetics 149:73; PMID:9584087), which encodes a centromere binding factor (CBF3a), and VMA5/YKL080W (White, WH. and Johnson, DI. (1997) Genetics 147:43; PMID: 9286667), which encodes subunit C of a vacuolar H(+)-ATPase. |
VMA5 encodes the C subunit of the yeast V-ATPase V1 domain (2, 1). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that have been identified in many eukaryotes, where they acidify intracellular vacuolar compartments. Vacuolar acidification is important for many cellular processes, including endocytosis, targeting of newly synthesized lysosomal enzymes, and other molecular targeting processes. The V-ATPase consists of two separable domains. The V1 domain has eight known subunits, is peripherally associated with the vacuolar membrane, and catalyzes ATP hydrolysis. The V0 domain is an integral membrane structure of five subunits, and transports protons across the membrane. The structure, function, and assembly of V-ATPases are reviewed in references 3, 4, 5 and 6.
The vma5 null mutant is viable but lacks vacuolar (H )-ATPase activity, cannot grow at neutral pH, and is sensitive to high or low calcium levels in the medium (2, 1). Vma5p is required for the V1 domain to assemble onto the vacuolar membrane (2, 1).
| 1) | Ho MN, et al. (1993) Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase. J Biol Chem 268(1):221-7 |
| 2) | Beltran C, et al. (1992) Cloning and mutational analysis of the gene encoding subunit C of yeast vacuolar H(+)-ATPase. J Biol Chem 267(2):774-9 |
| 3) | Forgac M (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4 |
| 4) | Graham LA and Stevens TH (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47 |
| 5) | Kane PM (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56 |
| 6) | Stevens TH and Forgac M (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808 |





