ATP6V1G3
ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | ATP6V1G3 ; ATP6G3; Vma10 | ||||||||||||
External IDs | MGI: 2450548 HomoloGene: 13630 IUPHAR: 821 GeneCards: ATP6V1G3 Gene | ||||||||||||
EC number | 3.6.3.14 | ||||||||||||
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Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 127124 | 338375 | |||||||||||
Ensembl | ENSG00000151418 | ENSMUSG00000026394 | |||||||||||
UniProt | Q96LB4 | Q8BMC1 | |||||||||||
RefSeq (mRNA) | NM_133262 | NM_177397 | |||||||||||
RefSeq (protein) | NP_573569 | NP_796371 | |||||||||||
Location (UCSC) |
Chr 1: 198.52 – 198.54 Mb |
Chr 1: 138.27 – 138.29 Mb | |||||||||||
PubMed search | |||||||||||||
V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.[1][2]
Function
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 G subunit proteins. Transcript variants encoding different isoforms have been found for this gene.[2]
References
- ↑ Stevens TH, Forgac M (Feb 1998). "Structure, function and regulation of the vacuolar (H+)-ATPase". Annual Review of Cell and Developmental Biology 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
- 1 2 "Entrez Gene: ATP6V1G3 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G3".
Further reading
- Finbow ME, Harrison MA (Jun 1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". The Biochemical Journal 324 (Pt 3): 697–712. doi:10.1042/bj3240697. PMC 1218484. PMID 9210392.
- Nelson N, Harvey WR (Apr 1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiological Reviews 79 (2): 361–85. PMID 10221984.
- Forgac M (May 1999). "Structure and properties of the vacuolar (H+)-ATPases". The Journal of Biological Chemistry 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
- Kane PM (Feb 1999). "Introduction: V-ATPases 1992-1998". Journal of Bioenergetics and Biomembranes 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
- Wieczorek H, Brown D, Grinstein S, Ehrenfeld J, Harvey WR (Aug 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 (Feb 2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nature Reviews Molecular Cell Biology 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511.
- Kawasaki-Nishi S, Nishi T, Forgac M (Jun 2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Letters 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
- Morel N (Oct 2003). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biology of the Cell / Under the Auspices of the European Cell Biology Organization 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
- Brown D, Lui B, Gluck S, Sabolić I (Oct 1992). "A plasma membrane proton ATPase in specialized cells of rat epididymis". The American Journal of Physiology 263 (4 Pt 1): C913–6. PMID 1415677.
- Smith AN, Borthwick KJ, Karet FE (Sep 2002). "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. doi:10.1016/S0378-1119(02)00884-3. PMID 12384298.