ATP6V1G3

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ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3
Identifiers
Symbol(s) ATP6V1G3; Vma10; ATP6G3; MGC119810; MGC119813
External IDs MGI: 2450548 HomoloGene: 13630
Orthologs
Human Mouse
Entrez 127124 338375
Ensembl ENSG00000151418 ENSMUSG00000026394
Uniprot Q96LB4 n/a
Refseq NM_133262 (mRNA)
NP_573569 (protein)		 NM_177397 (mRNA)
NP_796371 (protein)
Location Chr 1: 196.76 - 196.78 Mb Chr 1: 140.09 - 140.11 Mb
Pubmed search [1] [2]

ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3, also known as ATP6V1G3, is a human gene.[1]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes one of three G subunit proteins. Transcript variants encoding different isoforms have been found for this gene.[1]

[edit] References

  1. ^ a b Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3.

[edit] Further reading

  • Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 ( Pt 3): 697–712. PMID 9210392. 
  • Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887. 
  • Nelson N, Harvey WR (1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases.". Physiol. Rev. 79 (2): 361–85. PMID 10221984. 
  • Forgac M (1999). "Structure and properties of the vacuolar (H+)-ATPases.". J. Biol. Chem. 274 (19): 12951–4. PMID 10224039. 
  • Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3–5. PMID 10340843. 
  • Wieczorek H, Brown D, Grinstein S, et al. (1999). "Animal plasma membrane energization by proton-motive V-ATPases.". Bioessays 21 (8): 637–48. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860. 
  • Nishi T, Forgac M (2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps.". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511. 
  • Kawasaki-Nishi S, Nishi T, Forgac M (2003). "Proton translocation driven by ATP hydrolysis in V-ATPases.". FEBS Lett. 545 (1): 76–85. PMID 12788495. 
  • Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453–7. PMID 14597263. 
  • Brown D, Lui B, Gluck S, Sabolić I (1992). "A plasma membrane proton ATPase in specialized cells of rat epididymis.". Am. J. Physiol. 263 (4 Pt 1): C913–6. PMID 1415677. 
  • Smith AN, Borthwick KJ, Karet FE (2003). "Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis.". Gene 297 (1-2): 169–77. PMID 12384298. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
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