VMA7/YGR020C Summary Help

Standard Name VMA7
Systematic Name YGR020C
Feature Type ORF, Verified
Description Subunit F of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; the V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase) has eight subunits (1, 2 and see Summary Paragraph)
Chromosomal Location
ChrVII:527329 to 526973 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All VMA7 GO evidence and references
  View Computational GO annotations for VMA7
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
94 total interaction(s) for 46 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 43
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 6
  • Co-fractionation: 4
  • PCA: 15
  • Protein-peptide: 4
  • Two-hybrid: 1

Genetic Interactions
  • Negative Genetic: 3
  • Synthetic Growth Defect: 11
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 118
Molecular Weight (Da) 13,461
Isoelectric Point (pI) 4.78
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:527329 to 526973 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..357 527329..526973 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
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
Primary SGDIDS000003252

VMA7 encodes the F subunit of the yeast V-ATPase V1 domain (1, 3). 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 2, 4, 5 and 6.

The vma7 null mutant is viable but lacks vacuolar (H )-ATPase activity, cannot grow at neutral pH, and fails to accumulate quinacrine in the vacuole (1, 3). The remaining V1 subunits are present at normal levels but are not assembled onto the vacuolar membrane in the vma7 null mutant; V0 subunit levels are reduced in the vma7 null (1, 3). A specific interaction between Vma7p and the V-ATPase D subunit (Vma8p) has been detected (7).

Last updated: 2000-05-16 Contact SGD

References cited on this page View Complete Literature Guide for VMA7
1) Graham LA, et al.  (1994) VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase complex. J Biol Chem 269(42):25974-7
2) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
3) Nelson H, et al.  (1994) The Saccharomyces cerevisiae VMA7 gene encodes a 14-kDa subunit of the vacuolar H(+)-ATPase catalytic sector. J Biol Chem 269(39):24150-5
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
7) Tomashek JJ, et al.  (1997) V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase. J Biol Chem 272(42):26787-93