ATP6V0A4

V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.

ATP6V0A4
Identifiers
Aliases	ATP6V0A4, A4, ATP6N1B, ATP6N2, RDRTA2, RTA1C, RTADR, STV1, VPH1, VPP2, ATPase H+ transporting V0 subunit a4, DRTA3
External IDs	OMIM: 605239; MGI: 2153480; HomoloGene: 39904; GeneCards: ATP6V0A4; OMA:ATP6V0A4 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q34 Start 138,706,294 bp End 138,799,560 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 B1 Start 38,025,418 bp End 38,101,521 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in renal medulla human kidney olfactory zone of nasal mucosa kidney tubule testicle parotid gland gonad skin of leg cartilage tissue skin of abdomen Top expressed in right kidney lip human kidney morula zygote proximal tubule blastocyst esophagus embryo yolk sac 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 plasma membrane apical part of cell brush border membrane lysosomal membrane apical plasma membrane brush border vacuolar proton-transporting V-type ATPase complex endosome membrane extracellular exosome Biological process insulin receptor signaling pathway excretion transferrin transport ossification vacuolar proton-transporting V-type ATPase complex assembly ion transport hearing vacuolar acidification ion transmembrane transport ATP synthesis coupled proton transport regulation of pH phagosome acidification transport proton transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 50617 140494 Ensembl ENSG00000105929 ENSMUSG00000038600 UniProt Q9HBG4 Q920R6 RefSeq (mRNA) NM_020632 NM_130840 NM_130841 NM_080467 RefSeq (protein) NP_065683 NP_570855 NP_570856 NP_536715 Location (UCSC) Chr 7: 138.71 – 138.8 Mb Chr 6: 38.03 – 38.1 Mb PubMed search
Wikidata
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Function

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. This gene is one of four genes in man and mouse that encode different isoforms of the a subunit. Alternatively spliced transcript variants encoding the same protein have been described. Mutations in this gene are associated with renal tubular acidosis associated with preserved hearing.

Interactions

ATP6V0A4 has been shown to interact with PFKM.

External links

• Human ATP6V0A4 genome location and ATP6V0A4 gene details page in the UCSC Genome Browser.

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (3): 697–712. doi:10.1042/bj3240697. PMC 1218484. PMID 9210392.
• Stevens TH, Forgac M (1997). "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. doi:10.1152/physrev.1999.79.2.361. PMID 10221984. S2CID 1477911.
• 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, Ehrenfeld J, Harvey WR (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. S2CID 23505139.
• Brown D, Breton S (2000). "H(+)V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways". J. Exp. Biol. 203 (Pt 1): 137–45. doi:10.1242/jeb.203.1.137. PMID 10600682.
• 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 (2003). "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. S2CID 17519696.