Jump to content

ATP6V0A2

From Wikipedia, the free encyclopedia

ATP6V0A2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesATP6V0A2, A2, ARCL, ARCL2A, ATP6A2, ATP6N1D, J6B7, RTF, STV1, TJ6, TJ6M, TJ6S, VPH1, WSS, ATPase H+ transporting V0 subunit a2
External IDsOMIM: 611716; MGI: 104855; HomoloGene: 56523; GeneCards: ATP6V0A2; OMA:ATP6V0A2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012463

NM_011596

RefSeq (protein)

NP_036595

NP_035726

Location (UCSC)Chr 12: 123.71 – 123.76 MbChr 5: 124.77 – 124.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

[edit]

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

[edit]

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

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185344Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038023Ensembl, 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, et al. (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. ^ a b c "Entrez Gene: ATP6V0A2 ATPase, H+ transporting, lysosomal V0 subunit a2".

Further reading

[edit]
[edit]

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