VMA4/YOR332W Summary Help

VMA4 BASIC INFORMATION

Standard Name VMA4
Systematic Name YOR332W
Feature Type ORF, Verified
Description Subunit E of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane (1, 2 and see Summary Paragraph)
GO Annotations All VMA4 GO evidence and references
    View Computational GO annotations for VMA4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All VMA4 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions VMA4 All interactions details and references
73 total interaction(s) for 43 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 31
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 10
  • Biochemical Activity: 1
  • Co-fractionation: 3
  • Co-purification: 3
  • Reconstituted Complex: 1
  • Two-hybrid: 6
Genetic Interactions
  • Synthetic Growth Defect: 13
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 3
Sequence Information
ChrXV:943653 to 944354 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2006-01-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..702 943653..944354 2006-01-05 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000005859

VMA4 RESOURCES

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Expression Summary histogram

ADDITIONAL INFORMATION for VMA4

SUMMARY PARAGRAPH for VMA4

VMA4 encodes the E subunit of the yeast V-ATPase V1 domain (1, 2). 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 vma4 null mutant is viable but lacks vacuolar (H )-ATPase activity and cannot grow at neutral pH or on nonfermentable carbon sources (1, 2). A temperature sensitive vma4 mutant, which loses V-ATPase activity and vacuolar acidification upon incubation at high temperatures, shows abnormal bud morphology and delocalization of actin and chitin at the restrictive temperature (7). Vma4p is required for the V1 domain to assemble onto the vacuolar membrane (2).CC,PH, PI,

Last updated: 2000-05-16

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for VMA4]

1) Foury F  (1990) The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in Saccharomyces cerevisiae. J Biol Chem 265(30):18554-60
2) 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
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
7) Zhang JW, et al.  (1998) Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology. J Biol Chem 273(29):18470-80