VMA13/YPR036W Summary Help

Standard Name VMA13
Systematic Name YPR036W
Alias CLS11
Feature Type ORF, Verified
Description Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits (1, 2, 3 and see Summary Paragraph)
Chromosomal Location
ChrXVI:643836 to 645272 | ORF Map | GBrowse
Gene Ontology Annotations All VMA13 GO evidence and references
  View Computational GO annotations for VMA13
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
153 total interaction(s) for 92 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 33
  • Affinity Capture-Western: 12
  • Biochemical Activity: 1
  • Co-crystal Structure: 1
  • Co-fractionation: 1
  • Co-purification: 2
  • PCA: 17
  • Protein-peptide: 13
  • Reconstituted Complex: 5
  • Two-hybrid: 5

Genetic Interactions
  • Negative Genetic: 34
  • Positive Genetic: 1
  • Synthetic Growth Defect: 2
  • Synthetic Haploinsufficiency: 13
  • Synthetic Lethality: 7
  • Synthetic Rescue: 6

Expression Summary
Length (a.a.) 478
Molecular Weight (Da) 54,415
Isoelectric Point (pI) 6.31
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:643836 to 645272 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1437 643836..645272 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 SGDIDS000006240

VMA13 encodes the H subunit of the yeast V-ATPase V1 domain (1). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that 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.

In a vma13 null mutant, the remaining V1 subunits associate with the vacuolar membrane, but the complex is inactive and less stable than the wild type complex, suggesting that Vma13p is required for activity but not assembly of the V-ATPase (1). Free cytosolic V1 domains normally exist in a dynamic equilibrium with fully assembled V-ATPase complexes but are inactive; loss of Vma13p results in some ATPase activity in free V1 domains (7). Mutations in several V-ATPase subunits, including Vma13p, can cause calcium sensitivity due to loss of ATP-dependent Ca2 uptake (8).

V-ATPases have been identified in numerous eukaryotes (2, 6), and the genes encoding bovine and porcine V-ATPase H subunits have been cloned (9, 10).

Last updated: 2000-05-10 Contact SGD

References cited on this page View Complete Literature Guide for VMA13
1) Ho MN, et al.  (1993) VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae. J Biol Chem 268(24):18286-92
2) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
3) Keenan Curtis K and Kane PM  (2002) Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p. J Biol Chem 277(4):2716-24
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) Parra KJ, et al.  (2000) The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J Biol Chem 275(28):21761-7
8) Ohya Y, et al.  (1991) Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity. J Biol Chem 266(21):13971-7
9) Zhou Z, et al.  (1998) Molecular characterization of the 50- and 57-kDa subunits of the bovine vacuolar proton pump. J Biol Chem 273(10):5878-84
10) Hui D, et al.  (1999) Molecular cloning and chromosomal assignment of the porcine 54 and 56 kDa vacuolar H(+)-ATPase subunit gene (V-ATPase). Mamm Genome 10(3):266-70