ATP6V1G3

ATP6V1G3
Identifiers
Aliases	ATP6V1G3, ATP6G3, Vma10, ATPase H+ transporting V1 subunit G3
External IDs	MGI: 2450548 HomoloGene: 13630 GeneCards: ATP6V1G3
Gene ontology Molecular function • ATPase binding • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances • hydrogen-exporting ATPase activity, phosphorylative mechanism Cellular component • cytosol • plasma membrane • vacuolar proton-transporting V-type ATPase complex Biological process • hydrogen ion transmembrane transport • insulin receptor signaling pathway • ion transmembrane transport • ion transport • proton transport • transferrin transport • transport • phagosome acidification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	127124	338375
Ensembl	n/a	ENSMUSG00000026394
UniProt	Q96LB4	Q8BMC1
RefSeq (mRNA)	NM_133262 NM_133326 NM_001320218	NM_177397
RefSeq (protein)	NP_573569.1 NP_579872.1 NP_001307147.1	NP_796371.1
Location (UCSC)	Chr 1: 198.52 – 198.54 Mb	Chr 1: 138.27 – 138.29 Mb
PubMed search	[1]	[2]
Wikidata

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V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.^[3][4]

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.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "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.