View source for ATPase, H+ transporting, lysosomal V0 subunit a1

{{Infobox_gene}}
'''V-type proton ATPase 116 kDa subunit a isoform 1''' is an [[enzyme]] that in humans is encoded by the ''ATP6V0A1'' [[gene]].<ref name="pmid7774924">{{cite journal | vauthors = Brody LC, Abel KJ, Castilla LH, Couch FJ, McKinley DR, Yin G, Ho PP, Merajver S, Chandrasekharappa SC, Xu J | title = Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17 | journal = Genomics | volume = 25 | issue = 1 | pages = 238–47 |date=Jul 1995 | pmid = 7774924 | pmc =  | doi =10.1016/0888-7543(95)80131-5  |display-authors=etal}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0A1 ATPase, H+ transporting, lysosomal V0 subunit a1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=535| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 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.<ref name="entrez"/>
}}

==References==
{{reflist}}

==External links==
* {{UCSC gene info|ATP6V0A1}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | vauthors=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes. |journal=Biochem. J. |volume=324 |issue=  3|pages= 697–712 |year= 1997 |pmid= 9210392  | pmc=1218484 |doi=  10.1042/bj3240697}}
*{{cite journal  | vauthors=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779–808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
*{{cite journal  | vauthors=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases. |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361–85 |year= 1999 |pmid= 10221984 |doi=  }}
*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951–4 |year= 1999 |pmid= 10224039 |doi=  10.1074/jbc.274.19.12951}}
*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998. |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3–5 |year= 1999 |pmid= 10340843 |doi=  10.1023/A:1001884227654}}
*{{cite journal  | vauthors=Wieczorek H, Brown D, Grinstein S |title=Animal plasma membrane energization by proton-motive V-ATPases. |journal=BioEssays |volume=21 |issue= 8 |pages= 637–48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W |display-authors=etal}}
*{{cite journal  | vauthors=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94–103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
*{{cite journal  | vauthors=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases. |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76–85 |year= 2003 |pmid= 12788495 |doi=  10.1016/S0014-5793(03)00396-X}}
*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase. |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453–7 |year= 2004 |pmid= 14597263 |doi=  10.1016/S0248-4900(03)00075-3}}
*{{cite journal  | vauthors=Perin MS, Fried VA, Stone DK |title=Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3877–81 |year= 1991 |pmid= 1704894 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=  10.1016/S0378-1119(97)00411-3|display-authors=etal}}
}}
{{refend}}

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