Biology:ATP6V1G1
 Generic protein structure example |
V-type proton ATPase subunit G 1 is an enzyme that in humans is encoded by the ATP6V1G1 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of three V1 domain G subunit proteins. Pseudogenes of this gene have been characterized.[2]
References
- ↑ "Identification of genes expressed in human CD34+ hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc Natl Acad Sci U S A 95 (14): 8175–80. Aug 1998. doi:10.1073/pnas.95.14.8175. PMID 9653160. Bibcode: 1998PNAS...95.8175M.
- ↑ 2.0 2.1 "Entrez Gene: ATP6V1G1 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=9550.
External links
- Human ATP6V1G1 genome location and ATP6V1G1 gene details page in the UCSC Genome Browser.
Further reading
- "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (Pt 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.
- "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. 2001. doi:10.1101/gr.140200. PMID 11042152.
- "Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis". Gene 297 (1–2): 169–77. 2003. doi:10.1016/S0378-1119(02)00884-3. PMID 12384298.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
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