ATP6V0A2

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 124,766,641 bp [2] End 124,801,519 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve stromal cell of endometrium skin of abdomen endothelial cell body of stomach gastric mucosa monocyte minor salivary gland upper lobe of left lung rectum Top expressed in secondary oocyte intestinal villus jejunum crypt of lieberkuhn of small intestine entorhinal cortex duodenum large intestine colon esophagus thymus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATPase binding proton-transporting ATPase activity, rotational mechanism protein binding proton 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 acrosomal vesicle vacuolar proton-transporting V-type ATPase complex endosome membrane plasma 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: 124.77 – 124.8 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]}

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. S2CID   23318808.
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. S2CID   21122465.
• 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. S2CID   10507213.
• 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. S2CID   17519696.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID   31733518.
• 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. S2CID   23246611.
• 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. S2CID   7827573.
• 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. S2CID   37937722.

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.