ATP6V0A4

ATPase, H+ transporting, lysosomal V0 subunit a4
Identifiers
Symbols	ATP6V0A4 ; A4; ATP6N1B; ATP6N2; RDRTA2; RTA1C; RTADR; STV1; VPH1; VPP2
External IDs	OMIM: 605239 MGI: 2153480 HomoloGene: 39904 GeneCards: ATP6V0A4 Gene
EC number	3.6.3.14
Gene ontology Molecular function • protein binding • proton-transporting ATPase activity, rotational mechanism • ATPase binding Cellular component • vacuolar proton-transporting V-type ATPase, V0 domain • lysosomal membrane • endosome • plasma membrane • endosome membrane • integral component of membrane • apical plasma membrane • vacuolar proton-transporting V-type ATPase complex • phagocytic vesicle membrane • brush border membrane • apical part of cell • extracellular exosome Biological process • ossification • cellular iron ion homeostasis • regulation of pH • vacuolar acidification • excretion • sensory perception of sound • insulin receptor signaling pathway • ATP synthesis coupled proton transport • ATP hydrolysis coupled proton transport • 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	50617	140494
Ensembl	ENSG00000105929	ENSMUSG00000038600
UniProt	Q9HBG4	Q920R6
RefSeq (mRNA)	NM_020632	NM_080467
RefSeq (protein)	NP_065683	NP_536715
Location (UCSC)	Chr 7: 138.71 – 138.8 Mb	Chr 6: 38.05 – 38.12 Mb
PubMed search

V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.^[1][2][3]

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.^[3]

Interactions

ATP6V0A4 has been shown to interact with PFKM.^[4]

References

1. Karet FE, Finberg KE, Nayir A, Bakkaloglu A, Ozen S, Hulton SA, Sanjad SA, Al-Sabban EA, Medina JF, Lifton RP (Jan 2000). "Localization of a gene for autosomal recessive distal renal tubular acidosis with normal hearing (rdRTA2) to 7q33-34". Am. J. Hum. Genet. 65 (6): 1656–65. doi:10.1086/302679. PMC 1288376. PMID 10577919. Check date values in: |year= / |date= mismatch (help)
2. Smith AN, Skaug J, Choate KA, Nayir A, Bakkaloglu A, Ozen S, Hulton SA, Sanjad SA, Al-Sabban EA, Lifton RP, Scherer SW, Karet FE (Oct 2000). "Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing". Nat. Genet. 26 (1): 71–5. doi:10.1038/79208. PMID 10973252.
3. "Entrez Gene: ATP6V0A4 ATPase, H+ transporting, lysosomal V0 subunit a4".
4. Su Y, Zhou A, Al-Lamki RS, Karet FE (May 2003). "The a-subunit of the V-type H+-ATPase interacts with phosphofructokinase-1 in humans". J. Biol. Chem. 278 (22): 20013–8. doi:10.1074/jbc.M210077200. PMID 12649290.

Further reading

• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (3): 697–712. 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. PMID 10221984.
• 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.
• 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. 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.
• 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 (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.