ATP6V1G2

ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2
Identifiers
Symbols	ATP6V1G2 ; ATP6G; ATP6G2; NG38; VMA10
External IDs	OMIM: 606853 MGI: 1913487 HomoloGene: 41518 IUPHAR: 820 GeneCards: ATP6V1G2 Gene
EC number	3.6.3.14
Gene ontology Molecular function • hydrogen-exporting ATPase activity, phosphorylative mechanism Cellular component • cytosol • vacuolar proton-transporting V-type ATPase complex • integral component of synaptic vesicle membrane • melanosome Biological process • cellular iron ion homeostasis • metabolic process • insulin receptor signaling pathway • transferrin transport • ion transmembrane transport • interaction with host • transmembrane transport • phagosome maturation • hydrogen ion transmembrane transport Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	534	66237
Ensembl	ENSG00000206445	ENSMUSG00000024403
UniProt	O95670	Q9WTT4
RefSeq (mRNA)	NM_001204078	NM_023179
RefSeq (protein)	NP_001191007	NP_075668
Location (UCSC)	Chr 6: 31.54 – 31.55 Mb	Chr 17: 35.23 – 35.24 Mb
PubMed search

V-type proton ATPase subunit G 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.^[1][2]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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 encoded protein is one of three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. Alternatively spliced transcript variants encoding different isoforms have been described.^[2]

References

1. Neville MJ, Campbell RD (May 1999). "A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC". J Immunol 162 (8): 4745–54. PMID 10202016.
2. "Entrez Gene: ATP6V1G2 ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G2".

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 (3): 697–712. PMC 1218484. 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. 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.
• 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. 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.
• Smith AN, Borthwick KJ, Karet FE (2003). "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.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.