ATP6V0A4

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
Gene location (Human)
Chr.	Chromosome 7 (human)
End	138,799,560 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	38,101,521 bp
RNA expression pattern
	Top expressed in
	kidney; ; renal medulla; ; kidney tubule; ; parotid gland; ; skin of abdomen; ; cavity of mouth; ; minor salivary gland; ; metanephric glomerulus; ; thymus; ; bronchial epithelial cell;
	Top expressed in
	lip; ; kidney; ; morula; ; proximal tubule; ; esophagus; ; blastocyst; ; yolk sac; ; secondary oocyte; ; pharynx; ; larynx;
	More reference expression data
	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; sensory perception of sound; vacuolar acidification; ion transmembrane transport; ATP synthesis coupled proton transport; regulation of pH; phagosome acidification; transport; proton transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	50617
	140494
	ENSG00000105929
	ENSMUSG00000038600
	Q9HBG4
	Q920R6
	NM_020632; NM_130840; NM_130841
	NM_080467
	NP_065683; NP_570855; NP_570856
	NP_536715
	Wikidata
View/Edit Human	View/Edit Mouse

V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.^[5]^[6]^[7]

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.^[7]

Interactions

ATP6V0A4 has been shown to interact with PFKM.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000105929 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038600 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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. S2CID 19880326.
1 2 "Entrez Gene: ATP6V0A4 ATPase, H+ transporting, lysosomal V0 subunit a4".
↑ 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.

External links

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

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000105929 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038600 - 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.

[pmid10577919-5] 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.

[pmid10973252-6] 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. S2CID 19880326.

[entrez-7] 1 2 "Entrez Gene: ATP6V0A4 ATPase, H+ transporting, lysosomal V0 subunit a4".

[pmid12649290-8] 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.

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[2]

[3]

[4]

[5]

[6]

[7]

[8]

Function

Interactions

References

External links

Further reading