ATP6V1A

V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene.^[5][6]

ATP6V1A
Identifiers
Aliases	ATP6V1A, ATP6A1, ATP6V1A1, HO68, VA68, VPP2, Vma1, ATPase H+ transporting V1 subunit A, ARCL2D, IECEE3, DEE93
External IDs	OMIM: 607027; MGI: 1201780; HomoloGene: 123934; GeneCards: ATP6V1A; OMA:ATP6V1A - orthologs
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q13.31 Start 113,747,033 bp[1] End 113,812,056 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 B4 Start 43,905,765 bp[2] End 43,960,068 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 23 middle temporal gyrus pons endothelial cell Epithelium of choroid plexus kidney tubule orbitofrontal cortex cerebellar vermis lateral nuclear group of thalamus renal medulla Top expressed in cingulate gyrus ventromedial nucleus CA3 field primary motor cortex dentate gyrus facial motor nucleus medial dorsal nucleus medial vestibular nucleus pontine nuclei anterior amygdaloid area More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding hydrolase activity ATP binding proton-transporting ATPase activity, rotational mechanism Cellular component proton-transporting V-type ATPase, V1 domain cytosol myelin sheath plasma membrane proton-transporting two-sector ATPase complex integral component of plasma membrane microvillus lysosomal membrane apical plasma membrane mitochondrion extracellular exosome cytoplasm vacuolar membrane Biological process insulin receptor signaling pathway transferrin transport ion transport ion transmembrane transport ATP metabolic process regulation of macroautophagy phagosome acidification cellular iron ion homeostasis cellular response to increased oxygen levels transport proton transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 523 11964 Ensembl ENSG00000114573 ENSMUSG00000052459 UniProt P38606 P50516 RefSeq (mRNA) NM_001690 NM_007508 NM_001358203 NM_001358204 RefSeq (protein) NP_001681 NP_031534 NP_001345132 NP_001345133 Location (UCSC) Chr 3: 113.75 – 113.81 Mb Chr 16: 43.91 – 43.96 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle 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. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist.^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000114573 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052459 – 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.
5. van Hille B, Richener H, Evans DB, Green JR, Bilbe G (May 1993). "Identification of two subunit A isoforms of the vacuolar H(+)-ATPase in human osteoclastoma". J Biol Chem. 268 (10): 7075–80. doi:10.1016/S0021-9258(18)53147-1. PMID 8463241.
6. "Entrez Gene: ATP6V1A ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A".

External links

• Human ATP6V1A genome location and ATP6V1A 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 (Pt 3): 697–712. doi:10.1042/bj3240697. PMC 1218484. 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. 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, 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. S2CID 23505139.
• 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 (2004). "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.
• van Hille B, Richener H, Green JR, Bilbe G (1995). "The ubiquitous VA68 isoform of subunit A of the vacuolar H(+)-ATPase is highly expressed in human osteoclasts". Biochem. Biophys. Res. Commun. 214 (3): 1108–13. doi:10.1006/bbrc.1995.2400. PMID 7575517.
• Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Chang SY, Park SG, Kim S, Kang CY (2002). "Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation". J. Biol. Chem. 277 (10): 8388–94. doi:10.1074/jbc.M108792200. PMID 11741979.