Biology:ATPase, H+ transporting, lysosomal V0 subunit a1
 Generic protein structure example |
V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.[1][2]
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.[2]
References
- ↑ "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17". Genomics 25 (1): 238–47. Jul 1995. doi:10.1016/0888-7543(95)80131-5. PMID 7774924. https://zenodo.org/record/1258609.
- ↑ 2.0 2.1 "Entrez Gene: ATP6V0A1 ATPase, H+ transporting, lysosomal V0 subunit a1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=535.
External links
- Human ATP6V0A1 genome location and ATP6V0A1 gene details page in the UCSC Genome Browser.
Further reading
- "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 (3): 697–712. 1997. doi:10.1042/bj3240697. PMID 9210392.
- "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13: 779–808. 1998. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
- "Vacuolar and plasma membrane proton-adenosinetriphosphatases.". Physiol. Rev. 79 (2): 361–85. 1999. doi:10.1152/physrev.1999.79.2.361. 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.
- "Animal plasma membrane energization by proton-motive V-ATPases.". BioEssays 21 (8): 637–48. 1999. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860.
- "The vacuolar (H+)-ATPases--nature's most versatile proton pumps.". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. 2002. doi:10.1038/nrm729. PMID 11836511.
- "Proton translocation driven by ATP hydrolysis in V-ATPases.". FEBS Lett. 545 (1): 76–85. 2003. 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.
- "Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump.". J. Biol. Chem. 266 (6): 3877–81. 1991. doi:10.1016/S0021-9258(19)67875-0. PMID 1704894.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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