ATP6V0A2

V-type proton ATPase 116 kDa subunit a isoform 2 also known as V-ATPase 116 kDa isoform a2 is an enzyme that in humans is encoded by the ATP6V0A2 gene.[5][6][7]

ATP6V0A2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LX4
Identifiers
Aliases	ATP6V0A2, A2, ARCL, ARCL2A, ATP6A2, ATP6N1D, J6B7, RTF, STV1, TJ6, TJ6M, TJ6S, VPH1, WSS, ATPase H+ transporting V0 subunit a2
External IDs	OMIM: 611716 MGI: 104855 HomoloGene: 56523 GeneCards: ATP6V0A2
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.31 Start 123,712,318 bp[1] End 123,761,755 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 F Start 124,628,576 bp[2] End 124,724,455 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ATPase binding • proton-transporting ATPase activity, rotational mechanism • GO:0001948 protein binding • hydrogen ion transmembrane transporter activity Cellular component • integral component of membrane • endosome • proton-transporting V-type ATPase, V0 domain • phagocytic vesicle membrane • membrane • vacuolar proton-transporting V-type ATPase, V0 domain • lysosomal membrane • Acrosome • vacuolar proton-transporting V-type ATPase complex • endosome membrane • cell membrane • intracellular organelle • perinuclear region of cytoplasm Biological process • insulin receptor signaling pathway • transferrin transport • vacuolar proton-transporting V-type ATPase complex assembly • ion transport • vacuolar acidification • ion transmembrane transport • immune response • ATP synthesis coupled proton transport • regulation of macroautophagy • phagosome acidification • cellular iron ion homeostasis • cellular response to increased oxygen levels • transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	23545	21871
Ensembl	ENSG00000185344	ENSMUSG00000038023
UniProt	Q9Y487	P15920
RefSeq (mRNA)	NM_012463	NM_011596
RefSeq (protein)	NP_036595	NP_035726
Location (UCSC)	Chr 12: 123.71 – 123.76 Mb	Chr 5: 124.63 – 124.72 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

V-ATPase 116 kDa isoform a2 is a subunit of the vacuolar ATPase (v-ATPase), an heteromultimeric enzyme that is present in intracellular vesicles and in the plasma membrane of specialized cells, and which is essential for the acidification of diverse cellular components. V-ATPase consists of a membrane peripheral V(1) domain for ATP hydrolysis, and an integral membrane V(0) domain for proton translocation. The subunit encoded by this gene is a component of the V(0) domain.[7]

Clinical significance

Mutations in this gene are a cause of both cutis laxa type II and wrinkly skin syndrome.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000185344 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000038023 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Lee C, Ghoshal K, Beaman KD (Jan 1991). "Cloning of a cDNA for a T cell produced molecule with a putative immune regulatory role". Mol Immunol. 27 (11): 1137–1144. doi:10.1016/0161-5890(90)90102-6. PMID 2247090.
6. Kornak U, Reynders E, Dimopoulou A, van Reeuwijk J, Fischer B, Rajab A, Budde B, Nurnberg P, Foulquier F, Lefeber D, Urban Z, Gruenewald S, Annaert W, Brunner HG, van Bokhoven H, Wevers R, Morava E, Matthijs G, Van Maldergem L, Mundlos S (Dec 2007). "Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2". Nat Genet. 40 (1): 32–34. doi:10.1038/ng.2007.45. PMID 18157129.
7. "Entrez Gene: ATP6V0A2 ATPase, H+ transporting, lysosomal V0 subunit a2".

Further reading

• 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): 453–457. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
• 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Smith AN, Lovering RC, Futai M, et al. (2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Mol. Cell. 12 (4): 801–803. doi:10.1016/S1097-2765(03)00397-6. PMID 14580332.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
• Derks R, Beaman K (2005). "Regeneration and tolerance factor modulates the effect of adenosine triphosphate-induced interleukin 1 beta secretion in human macrophages". Hum. Immunol. 65 (7): 676–682. doi:10.1016/j.humimm.2004.04.006. PMID 15301855.
• Derks RA, Beaman KD (2005). "Regeneration and tolerance factor prevents bystander T-cell death associated with human immunodeficiency virus infection". Clin. Diagn. Lab. Immunol. 11 (5): 835–840. doi:10.1128/CDLI.11.5.835-840.2004. PMC 515283. PMID 15358640.
• Lattuada D, Mangioni S, Viganò P, et al. (2005). "The placental immunomodulatory cytokine regeneration and tolerance factor is also expressed by both human cycling and early pregnant endometrium". Am. J. Reprod. Immunol. 52 (3): 224–231. doi:10.1111/j.1600-0897.2004.00210.x. PMID 15373763.
• Hurtado-Lorenzo A, Skinner M, El Annan J, et al. (2006). "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway". Nat. Cell Biol. 8 (2): 124–136. doi:10.1038/ncb1348. PMID 16415858.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ntrivalas E, Gilman-Sachs A, Kwak-Kim J, Beaman K (2007). "The N-terminus domain of the a2 isoform of vacuolar ATPase can regulate interleukin-1beta production from mononuclear cells in co-culture with JEG-3 choriocarcinoma cells". Am. J. Reprod. Immunol. 57 (3): 201–209. doi:10.1111/j.1600-0897.2006.00463.x. PMID 17295899.

External links

• GeneReviews/NCBI/NIH/UW entry on ATP6V0A2-Related Autosomal Recessive Cutis Laxa
• OMIM entries on ATP6V0A2-Related Autosomal Recessive Cutis Laxa
• Human ATP6V0A2 genome location and ATP6V0A2 gene details page in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.