ATP6V0A2

ATPase, H+ transporting, lysosomal V0 subunit a2
Identifiers
Symbols	ATP6V0A2 ; A2; ARCL; ARCL2A; ATP6A2; ATP6N1D; J6B7; RTF; STV1; TJ6; TJ6M; TJ6S; VPH1; WSS
External IDs	OMIM: 611716 MGI: 104855 HomoloGene: 56523 GeneCards: ATP6V0A2 Gene
EC number	3.6.3.6
Gene ontology Molecular function • protein binding • proton-transporting ATPase activity, rotational mechanism • ATPase binding Cellular component • vacuolar proton-transporting V-type ATPase, V0 domain • acrosomal vesicle • cytoplasm • lysosomal membrane • plasma membrane • focal adhesion • endosome membrane • integral component of membrane • vacuolar proton-transporting V-type ATPase complex • phagocytic vesicle membrane Biological process • cellular iron ion homeostasis • immune response • vacuolar acidification • insulin receptor signaling pathway • ATP synthesis coupled proton transport • ATP hydrolysis coupled proton transport • transferrin transport • ion transmembrane transport • interaction with host • transmembrane transport • vacuolar proton-transporting V-type ATPase complex assembly • phagosome maturation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
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

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.^[1][2][3]

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.^[3]

Clinical significance

Mutations in this gene are a cause of both cutis laxa type II and wrinkly skin syndrome.^[3]

References

1. 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.
2. 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.
3. "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

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