VMA6/YLR447C Summary Help

VMA6 BASIC INFORMATION

Standard Name VMA6
Systematic Name YLR447C
Feature Type ORF, Verified
Description Subunit d of the five-subunit V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found in the endomembrane system; stabilizes VO subunits; required for V1 domain assembly on the vacuolar membrane (1, 2 and see Summary Paragraph)
GO Annotations All VMA6 GO evidence and references
    View Computational GO annotations for VMA6
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All VMA6 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions VMA6 All interactions details and references
69 total interaction(s) for 44 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 7
  • Co-fractionation: 1
  • Co-purification: 1
  • PCA: 7
  • Reconstituted Complex: 3
  • Two-hybrid: 10
Genetic Interactions
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 10
  • Synthetic Rescue: 1
Sequence Information
ChrXII:1027890 to 1026853 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2006-01-09 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1038 1027890..1026853 2006-01-09 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004439

VMA6 RESOURCES

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Expression Summary histogram

ADDITIONAL INFORMATION for VMA6

SUMMARY PARAGRAPH for VMA6

VMA6 encodes the d subunit of the yeast V-ATPase V0 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, 3, 4 and 5.

The vma6 null mutant is viable but shows a growth defect at neutral pH and is sensitive to calcium (1). In the absence of Vma6p, the remaining V0 subunits are destabilized and the V1 domain does not assemble onto the vacuolar membrane (1).

V-ATPases have been identified in numerous eukaryotes (2, 5); Vma6p homologs have been identified in red beet and Arabidopsis (6).

Last updated: 2000-05-17

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for VMA6]

1) Bauerle C, et al.  (1993) The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector. J Biol Chem 268(17):12749-57
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) Bauerle C, et al.  (1998) Characterization of a red beet protein homologous to the essential 36-kilodalton subunit of the yeast V-type ATPase. Plant Physiol 117(3):859-67