VMA5/YKL080W Summary Help

Standard Name VMA5
Systematic Name YKL080W
Alias CSL5 , VAT3
Feature Type ORF, Verified
Description Subunit C 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
ChrXI:285030 to 286208 | ORF Map | GBrowse
Gene Ontology Annotations All VMA5 GO evidence and references
  View Computational GO annotations for VMA5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Classical genetics
Large-scale survey
112 total interaction(s) for 78 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 27
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 9
  • Biochemical Activity: 3
  • Co-crystal Structure: 2
  • Co-fractionation: 1
  • FRET: 2
  • PCA: 6
  • Protein-peptide: 10
  • Reconstituted Complex: 1
  • Two-hybrid: 8

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 20
  • Positive Genetic: 5
  • Synthetic Growth Defect: 7
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 6
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 392
Molecular Weight (Da) 44,188
Isoelectric Point (pI) 6.65
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXI:285030 to 286208 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1179 285030..286208 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 SGDIDS000001563

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).

Last updated: 2000-05-15 Contact SGD

References cited on this page View Complete Literature Guide for VMA5
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