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ATP6V1B1
Identifiers
Aliases	ATP6V1B1, ATP6B1, RTA1B, VATB, VMA2, VPP3, ATPase H+ transporting V1 subunit B1, DRTA2
External IDs	OMIM: 192132; MGI: 103285; HomoloGene: 68198; GeneCards: ATP6V1B1; OMA:ATP6V1B1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p13.3 Start 70,935,900 bp End 70,965,431 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 C3|6 35.94 cM Start 83,719,972 bp End 83,735,837 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube testicle human kidney skin of leg minor salivary glands skin of abdomen olfactory zone of nasal mucosa canal of the cervix body of pancreas stromal cell of endometrium Top expressed in right kidney inner renal medulla human kidney connecting tubule nose olfactory system upper respiratory tract olfactory epithelium trigeminal nerve hair More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein-containing complex binding proton transmembrane transporter activity hydrolase activity ATP binding Cellular component cytoplasm proton-transporting V-type ATPase, V1 domain cytosol lateral plasma membrane membrane microvillus basolateral plasma membrane apical plasma membrane vacuolar proton-transporting V-type ATPase complex extracellular exosome endomembrane system synaptic vesicle extrinsic component of synaptic vesicle membrane Biological process insulin receptor signaling pathway excretion calcium ion homeostasis transferrin transport pH reduction ossification ion transport hearing ion transmembrane transport ATP metabolic process inner ear morphogenesis regulation of macroautophagy regulation of pH phagosome acidification transport proton transmembrane transport renal water homeostasis renal sodium ion transport prostaglandin metabolic process regulation of gene expression adult behavior renal sodium excretion olfactory behavior chloride ion homeostasis potassium ion homeostasis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 525 110935 Ensembl ENSG00000116039 ENSMUSG00000006269 UniProt P15313 Q91YH6 RefSeq (mRNA) NM_001692 NM_134157 RefSeq (protein) NP_001683 NP_598918 Location (UCSC) Chr 2: 70.94 – 70.97 Mb Chr 6: 83.72 – 83.74 Mb PubMed search
Wikidata
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V-type proton ATPase subunit B, kidney isoform is an enzyme that in humans is encoded by the ATP6V1B1 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 one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000116039 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000006269 – 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. Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, Rodriguez-Soriano J, Santos F, Cremers CW, Di Pietro A, Hoffbrand BI, Winiarski J, Bakkaloglu A, Ozen S, Dusunsel R, Goodyer P, Hulton SA, Wu DK, Skvorak AB, Morton CC, Cunningham MJ, Jha V, Lifton RP (Feb 1999). "Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness". Nat Genet. 21 (1): 84–90. doi:10.1038/5022. PMID 9916796. S2CID 34262548.
6. Sudhof TC, Fried VA, Stone DK, Johnston PA, Xie XS (Sep 1989). "Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria". Proc Natl Acad Sci U S A. 86 (16): 6067–71. Bibcode:1989PNAS...86.6067S. doi:10.1073/pnas.86.16.6067. PMC 297776. PMID 2527371.
7. ^ "Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)".

External links

• Human ATP6V1B1 genome location and ATP6V1B1 gene details page in the UCSC Genome Browser.

Further reading

• Schuler GD, Boguski MS, Stewart EA, et al. (1996). "A gene map of the human genome". Science. 274 (5287): 540–6. Bibcode:1996Sci...274..540S. doi:10.1126/science.274.5287.540. PMID 8849440. S2CID 22619.
• 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, Schmid P, et al. (1994). "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms". Biochem. J. 303 (Pt 1): 191–8. doi:10.1042/bj3030191. PMC 1137575. PMID 7945239.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Breton S, Smith PJ, Lui B, Brown D (1996). "Acidification of the male reproductive tract by a proton pumping (H+)-ATPase". Nat. Med. 2 (4): 470–2. doi:10.1038/nm0496-470. PMID 8597961. S2CID 10616789.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

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