ATPase, H+ transporting, lysosomal V0 subunit a1

ATP6V0A1
Identifiers
Aliases	ATP6V0A1, Atp6v0a1, AA959968, ATP6a1, Atp6n1, Atp6n1a, Atpv0a1, Vpp-1, Vpp1, Stv1, Vph1, a1, ATPase, H+ transporting, lysosomal V0 subunit a1, ATP6N1, ATP6N1A, VPP1, ATPase H+ transporting V0 subunit a1
External IDs	MGI: 103286 HomoloGene: 3795 GeneCards: ATP6V0A1
Gene ontology Molecular function • ATPase binding • proton-transporting ATPase activity, rotational mechanism • protein binding • hydrogen ion transmembrane transporter activity Cellular component • cytoplasm • integral component of membrane • proton-transporting V-type ATPase, V0 domain • phagocytic vesicle membrane • Golgi apparatus • cell • intracellular membrane-bounded organelle • membrane • vacuolar proton-transporting V-type ATPase, V0 domain • melanosome • plasma membrane • nucleoplasm • vacuolar proton-transporting V-type ATPase complex • endosome membrane • extracellular exosome • cytoplasmic vesicle membrane • cytoplasmic vesicle Biological process • insulin receptor signaling pathway • transferrin transport • vacuolar proton-transporting V-type ATPase complex assembly • toxin transport • ion transport • proton transport • ion transmembrane transport • transport • ATP synthesis coupled proton transport • ATP hydrolysis coupled proton transport • regulation of macroautophagy • vacuolar acidification • phagosome acidification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	535	11975
Ensembl	ENSG00000033627	ENSMUSG00000019302
UniProt	Q93050	Q9Z1G4
RefSeq (mRNA)	NM_001130020 NM_001130021 NM_005177	NM_001243049 NM_001243050 NM_001243051 NM_016920
RefSeq (protein)	NP_001123492.1 NP_001123493.1 NP_005168.2	NP_001229979.1 NP_001229980.1 NP_058616.1
Location (UCSC)	Chr 17: 42.46 – 42.52 Mb	Chr 11: 101.01 – 101.06 Mb
PubMed search	[1]	[2]
Wikidata

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V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.^[3][4]

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.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Brody LC, Abel KJ, Castilla LH, Couch FJ, McKinley DR, Yin G, Ho PP, Merajver S, Chandrasekharappa SC, Xu J, et al. (Jul 1995). "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17". Genomics. 25 (1): 238–47. doi:10.1016/0888-7543(95)80131-5. PMID 7774924.
4. "Entrez Gene: ATP6V0A1 ATPase, H+ transporting, lysosomal V0 subunit a1".

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 (3): 697–712. doi:10.1042/bj3240697. PMC 1218484. 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. doi:10.1074/jbc.274.19.12951. PMID 10224039.
• Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3–5. doi:10.1023/A:1001884227654. 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. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
• Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell. 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. 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.
• 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.