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ATP6V0A1 - Wikipedia, the free encyclopedia

ATP6V0A1

From Wikipedia, the free encyclopedia


ATPase, H+ transporting, lysosomal V0 subunit a1
Identifiers
Symbol(s) ATP6V0A1; ATP6N1; ATP6N1A; DKFZp781J1951; Stv1; VPP1; Vph1; a1
External IDs OMIM: 192130 MGI103286 HomoloGene3795
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 535 11975
Ensembl ENSG00000033627 ENSMUSG00000019302
Uniprot Q93050 Q9Z1G4
Refseq NM_005177 (mRNA)
NP_005168 (protein)
NM_016920 (mRNA)
NP_058616 (protein)
Location Chr 17: 37.86 - 37.93 Mb Chr 11: 100.83 - 100.88 Mb
Pubmed search [1] [2]

ATPase, H+ transporting, lysosomal V0 subunit a1, also known as ATP6V0A1, 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 A subunit proteins and the encoded protein is associated with clathrin-coated vesicles. The occurrence of splice variants encoding different protein products has been reported, but the full-length natures of these transcripts have not been determined.[1]

[edit] References

[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. 
  • Perin MS, Fried VA, Stone DK, et al. (1991). "Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump.". J. Biol. Chem. 266 (6): 3877–81. PMID 1704894. 
  • Brody LC, Abel KJ, Castilla LH, et al. (1995). "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17.". Genomics 25 (1): 238–47. PMID 7774924. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. 


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