ATP6V1B1

ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1
Identifiers
Symbols	ATP6V1B1 ; ATP6B1; RTA1B; VATB; VMA2; VPP3
External IDs	OMIM: 192132 MGI: 103285 HomoloGene: 68198 ChEMBL: 3217 GeneCards: ATP6V1B1 Gene
EC number	3.6.3.14
Gene ontology Molecular function • ATP binding • hydrogen ion transmembrane transporter activity • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances • protein complex binding Cellular component • cytoplasm • cytosol • microvillus • endomembrane system • basolateral plasma membrane • apical plasma membrane • lateral plasma membrane • vacuolar proton-transporting V-type ATPase complex • proton-transporting V-type ATPase, V1 domain • extracellular exosome Biological process • ossification • cellular iron ion homeostasis • regulation of pH • excretion • sensory perception of sound • insulin receptor signaling pathway • ATP hydrolysis coupled proton transport • proton transport • transferrin transport • ion transmembrane transport • inner ear morphogenesis • pH reduction • ATP metabolic process • interaction with host • calcium ion homeostasis • transmembrane transport • phagosome maturation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
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: 83.74 – 83.76 Mb
PubMed search

V-type proton ATPase subunit B, kidney isoform is an enzyme that in humans is encoded by the ATP6V1B1 gene.^[1][2][3]

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.^[3]

References

1. 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.
2. 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. doi:10.1073/pnas.86.16.6067. PMC 297776. PMID 2527371.
3. "Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)".

Further reading

• Schuler GD, Boguski MS, Stewart EA; et al. (1996). "A gene map of the human genome". Science 274 (5287): 540–6. doi:10.1126/science.274.5287.540. PMID 8849440.
• Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (Pt 3): 697–712. 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. PMID 10221984.
• 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.
• 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. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
• 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.
• 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.
• 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.