|Other Names||V-type proton ATPase 116 kDa subunit a isoform 1, V-ATPase 116 kDa isoform a1, Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit, Vacuolar adenosine triphosphatase subunit Ac116, Vacuolar proton pump subunit 1, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1, ATP6V0A1, ATP6N1, ATP6N1A, VPP1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||ATP6N1, ATP6N1A, VPP1|
|Function||Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity).|
|Cellular Location||Cytoplasmic vesicle membrane; Multi-pass membrane protein. Melanosome. Note=Coated vesicle. Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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ATP6V0A1 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.
Antonacopoulou, A.G., et al. Anticancer Res. 28 (2B), 1221-1227 (2008) Norgett, E.E., et al. J. Biol. Chem. 282(19):14421-14427(2007)Chi, A., et al. J. Proteome Res. 5(11):3135-3144(2006)
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