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ATP6V0A1
Introduction
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]
References
References
Further reading
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.