ATP6V0B

ATP6V0B
Identifiers
Aliases	ATP6V0B, ATP6F, HATPL, VMA16, ATPase H+ transporting V0 subunit b
External IDs	OMIM: 603717 MGI: 1890510 HomoloGene: 2986 GeneCards: ATP6V0B
Gene location (Human) Chr. Chromosome 1 (human) Band 1p34.1 Start 43,974,487 bp End 43,978,295 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 D1 Start 117,741,523 bp End 117,744,530 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior pituitary monocyte prefrontal cortex body of pancreas blood periodontal fiber right adrenal gland left adrenal gland islet of Langerhans cingulate gyrus Top expressed in facial motor nucleus superior frontal gyrus entorhinal cortex anterior horn of spinal cord cerebellar cortex barrel cortex Region I of hippocampus proper retinal pigment epithelium yolk sac lacrimal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function proton transmembrane transporter activity proton-transporting ATPase activity, rotational mechanism transporter activity Cellular component vacuole vacuolar membrane membrane vacuolar proton-transporting V-type ATPase, V0 domain proton-transporting V-type ATPase, V0 domain phagocytic vesicle membrane endosome membrane proton-transporting two-sector ATPase complex, proton-transporting domain integral component of membrane Biological process regulation of macroautophagy vacuolar acidification ion transmembrane transport insulin receptor signaling pathway ion transport transferrin transport proton transmembrane transport phagosome acidification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 533 114143 Ensembl ENSG00000117410 ENSMUSG00000033379 UniProt Q99437 Q91V37 RefSeq (mRNA) NM_004047 NM_001039457 NM_001294333 NM_033617 RefSeq (protein) NP_001034546 NP_001281262 NP_004038 NP_291095 Location (UCSC) Chr 1: 43.97 – 43.98 Mb Chr 4: 117.74 – 117.74 Mb PubMed search
Wikidata
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V-type proton ATPase 21 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0B gene.

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 part of the transmembrane V0 domain, and is the human counterpart of yeast VMA16. Two alternatively spliced transcript variants that encode different proteins have been found for this gene.

External links

• Human ATP6V0B genome location and ATP6V0B 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 (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.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Izumi H, Ise T, Murakami T, et al. (2003). "Structural and functional characterization of two human V-ATPase subunit gene promoters". Biochim. Biophys. Acta. 1628 (2): 97–104. doi:10.1016/S0167-4781(03)00119-2. PMID 12890556.