VMA10/YHR039C-A Summary Help

Standard Name VMA10 1
Systematic Name YHR039C-A
Alias YHR039C-B
Feature Type ORF, Verified
Description Subunit G of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; involved in vacuolar acidification; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits (1 and see Summary Paragraph)
Also known as: YHR039BC
Chromosomal Location
ChrVIII:187679 to 187173 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All VMA10 GO evidence and references
  View Computational GO annotations for VMA10
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
92 total interaction(s) for 33 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 38
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 18
  • Co-crystal Structure: 3
  • Co-fractionation: 5
  • Far Western: 2
  • PCA: 2
  • Protein-peptide: 7
  • Reconstituted Complex: 4
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Lethality: 1
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 5
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 114
Molecular Weight (Da) 12,713
Isoelectric Point (pI) 9.77
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVIII:187679 to 187173 | 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..3 187679..187677 2011-02-03 1996-07-31
Intron 4..165 187676..187515 2011-02-03 1996-07-31
CDS 166..507 187514..187173 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 SGDIDS000002100

VMA10 encodes the G subunit of the yeast V-ATPase V1 domain (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 2, 3, 4 and 5.

The vma10 null mutant is viable but lacks vacuolar (H )-ATPase activity, cannot grow at neutral pH, and fails to accumulate quinacrine in the vacuole (1). In the absence of Vma10p, the remaining V1 subunits do not associate with the vacuolar membrane (6). A specific interaction between Vma10p and the V-ATPase E subunit (Vma4p) has been detected (7).

Last updated: 2000-05-16 Contact SGD

References cited on this page View Complete Literature Guide for VMA10
1) Supekova L, et al.  (1995) The Saccharomyces cerevisiae VMA10 is an intron-containing gene encoding a novel 13-kDa subunit of vacuolar H(+)-ATPase. J Biol Chem 270(23):13726-32
2) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
3) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
4) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
5) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
6) Graham LA, et al.  (1995) VMA8 encodes a 32-kDa V1 subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase required for function and assembly of the enzyme complex. J Biol Chem 270(25):15037-44
7) Tomashek JJ, et al.  (1997) V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase. J Biol Chem 272(42):26787-93