ATP6V0A4

From Wikipedia, the free encyclopedia

ATPase, H+ transporting, lysosomal V0 subunit a4

Identifiers

ATP6V0A4; VPP2; A4; ATP6N1B; ATP6N2; MGC130016; MGC130017; RDRTA2; RTA1C; RTADR; STV1; VPH1

External IDs

OMIM: 605239 MGI: 2153480 HomoloGene: 39904

Gene ontology
Molecular Function:	• protein binding • hydrogen ion transmembrane transporter activity
Cellular Component:	• membrane • integral to membrane • apical plasma membrane • vacuolar proton-transporting V-type ATPase complex • brush border membrane
Biological Process:	• ossification • ion transport • regulation of pH • excretion • sensory perception of sound • ATP hydrolysis coupled proton transport • proton transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_020632 (mRNA)
NP_065683 (protein)

NM_080467 (mRNA)
NP_536715 (protein)

Location

Chr 7: 138.04 - 138.13 Mb

Chr 6: 37.98 - 38.05 Mb

Pubmed search

[1]

[2]

ATPase, H+ transporting, lysosomal V0 subunit a4, also known as ATP6V0A4, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP6V0A4 ATPase, H+ transporting, lysosomal V0 subunit a4.

[edit] Further reading

Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 ( Pt 3): 697–712. PMID 9210392.
Stevens TH, Forgac M (1998). "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. PMID 10224039.
Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3–5. PMID 10340843.
Wieczorek H, Brown D, Grinstein S, et al. (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. PMID 12788495.
Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453–7. PMID 14597263.
Karet FE, Finberg KE, Nayir A, et al. (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. PMID 10577919.
Smith AN, Skaug J, Choate KA, et al. (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.