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Gene Review

VMA3  -  H(+)-transporting V0 sector ATPase subunit c

Saccharomyces cerevisiae S288c

Synonyms: CLS7, CUP5, GEF2, Guanine nucleotide exchange factor 2, V-ATPase 16 kDa proteolipid subunit 1, ...
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Disease relevance of CUP5


High impact information on CUP5

  • Since disruption of GEF2, a subunit of the vacuolar H+-ATPase, leads to a similar phenotype, it was previously suggested that the chloride conductance provided by Gef1p is necessary for vacuolar acidification [3].
  • We report here that the immunosuppressants FK506 and cyclosporin A cause general growth inhibition of the vma3 mutant [4].
  • Ca(2+)-sensitive mutants of the yeast Saccharomyces cerevisiae showing a Pet- phenotype (cls7-cls11) have lesions in a system for maintaining intracellular Ca2+ homeostasis (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1986) J. Gen. Microbiol. 132, 979-988) [5].
  • The deduced amino acid sequence shows 56.7% identity, and significant coincidence in amino acid composition with the 16-kDa subunit c (a VMA3 gene product) of the yeast vacuolar membrane H(+)-ATPase [6].
  • To investigate functional and structural roles of the subunit c for vacuolar acidification and protein transport to the vacuole, haploid mutants with the disrupted VMA3 gene were constructed [7].

Biological context of CUP5

  • One CLS gene, CLS7, was located on the left arm of chromosome V [8].
  • Cloning of structural genes for the three subunits of the H+-ATPase (VMA1, VMA2, and VMA3) and their nucleotide sequence determination have been accomplished, which provide greater advantages for molecular biological studies on the structure-function relationship and biogenesis of the enzyme complex [9].
  • The cDNA for the Nephrops proteolipid complements a mutation in the yeast VMA3 gene, resulting in assembly of a hybrid H(+)-ATPase comprising yeast catalytic subunits and Nephrops integral membrane components [10].
  • A defect in mitochondrial function may be the cause of the petite phenotype: the rate of oxygen consumption by intact gef2 cells and by mitochondrial fractions isolated from gef2 mutants was reduced 60%-75% relative to wild type [11].

Anatomical context of CUP5

  • Using a vma3 mutation that impairs the Ca2+ sequestering activity into the vacuole, we have shown that the cls2 mutation results in 3.4-fold increase in the Ca2+ pool that is not exchangeable with extracellular Ca2+ [1].
  • Functional expression of Acetabularia acetabulum vacuolar H(+)-pyrophosphatase in a yeast VMA3-deficient strain [12].
  • Two translation products from the other two cDNAs were demonstrated not to be localized in vacuolar membranes, and thus could not complement the function of the VMA3-deficient strain [13].

Associations of CUP5 with chemical compounds


Other interactions of CUP5

  • In this study we demonstrate that proteins encoded by genes previously demonstrated to play critical roles in vacuole assembly for acidification, PEP3, PEP5 and VMA3, are also required for normal copper and iron metal ion homeostasis [14].
  • A vma3 mutant defective in vacuolar acidification showed no reduction of vacuolar pH after application of hydrostatic pressure, indicating that the transient acidification is mediated through the function of vacuolar H(+)-ATPase [15].


  1. Yeast Cls2p/Csg2p localized on the endoplasmic reticulum membrane regulates a non-exchangeable intracellular Ca2+ pool cooperatively with calcineurin. Tanida, I., Takita, Y., Hasegawa, A., Ohya, Y., Anraku, Y. FEBS Lett. (1996) [Pubmed]
  2. Antifungal activity of amiodarone is mediated by disruption of calcium homeostasis. Gupta, S.S., Ton, V.K., Beaudry, V., Rulli, S., Cunningham, K., Rao, R. J. Biol. Chem. (2003) [Pubmed]
  3. Golgi localization and functionally important domains in the NH2 and COOH terminus of the yeast CLC putative chloride channel Gef1p. Schwappach, B., Stobrawa, S., Hechenberger, M., Steinmeyer, K., Jentsch, T.J. J. Biol. Chem. (1998) [Pubmed]
  4. Cooperation of calcineurin and vacuolar H(+)-ATPase in intracellular Ca2+ homeostasis of yeast cells. Tanida, I., Hasegawa, A., Iida, H., Ohya, Y., Anraku, Y. J. Biol. Chem. (1995) [Pubmed]
  5. Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity. Ohya, Y., Umemoto, N., Tanida, I., Ohta, A., Iida, H., Anraku, Y. J. Biol. Chem. (1991) [Pubmed]
  6. VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity. Umemoto, N., Ohya, Y., Anraku, Y. J. Biol. Chem. (1991) [Pubmed]
  7. Roles of the VMA3 gene product, subunit c of the vacuolar membrane H(+)-ATPase on vacuolar acidification and protein transport. A study with VMA3-disrupted mutants of Saccharomyces cerevisiae. Umemoto, N., Yoshihisa, T., Hirata, R., Anraku, Y. J. Biol. Chem. (1990) [Pubmed]
  8. Isolation and characterization of Ca2+-sensitive mutants of Saccharomyces cerevisiae. Ohya, Y., Ohsumi, Y., Anraku, Y. J. Gen. Microbiol. (1986) [Pubmed]
  9. Structure and function of the yeast vacuolar membrane proton ATPase. Anraku, Y., Umemoto, N., Hirata, R., Wada, Y. J. Bioenerg. Biomembr. (1989) [Pubmed]
  10. Functional properties of a hybrid vacuolar H(+)-ATPase in Saccharomyces cells expressing the Nephrops 16-kDa proteolipid. Harrison, M.A., Jones, P.C., Kim, Y.I., Finbow, M.E., Findlay, J.B. Eur. J. Biochem. (1994) [Pubmed]
  11. The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism. Eide, D.J., Bridgham, J.T., Zhao, Z., Mattoon, J.R. Mol. Gen. Genet. (1993) [Pubmed]
  12. Functional expression of Acetabularia acetabulum vacuolar H(+)-pyrophosphatase in a yeast VMA3-deficient strain. Ikeda, M., Umami, K., Hinohara, M., Tanimura, Y., Ohmae, A., Nakanishi, Y., Maeshima, M. J. Exp. Bot. (2002) [Pubmed]
  13. Expression of V-ATPase proteolipid subunit of Acetabularia acetabulum in a VMA3-deficient strain of Saccharomyces cerevisiae and its complementation study. Ikeda, M., Hinohara, M., Umami, K., Taguro, Y., Okada, Y., Wada, Y., Nakanishi, Y., Maeshima, M. Eur. J. Biochem. (2001) [Pubmed]
  14. Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription. Szczypka, M.S., Zhu, Z., Silar, P., Thiele, D.J. Yeast (1997) [Pubmed]
  15. Analysis of intracellular pH in the yeast Saccharomyces cerevisiae under elevated hydrostatic pressure: a study in baro- (piezo-) physiology. Abe, F., Horikoshi, K. Extremophiles (1998) [Pubmed]
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