ATP6V1B2

ATP6V1B2
Identifiers
Aliases	ATP6V1B2, ATP6B1B2, ATP6B2, HO57, VATB, VPP3, Vma2, ATPase H+ transporting V1 subunit B2, DOOD, ZLS2
External IDs	MGI: 109618 HomoloGene: 1279 GeneCards: ATP6V1B2
Gene ontology Molecular function • proton-transporting ATPase activity, rotational mechanism • protein binding • hydrogen ion transmembrane transporter activity • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances • hydrolase activity • ATP binding Cellular component • cytoplasm • integral component of membrane • proton-transporting V-type ATPase, V1 domain • cytosol • intracellular membrane-bounded organelle • membrane • melanosome • ruffle • myelin sheath • plasma membrane • microvillus • lysosomal membrane • extracellular exosome • endomembrane system Biological process • insulin receptor signaling pathway • transferrin transport • ion transport • proton transport • ion transmembrane transport • ATP metabolic process • transport • ATP hydrolysis coupled proton transport • regulation of macroautophagy • phagosome acidification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	526	11966
Ensembl	ENSG00000147416	ENSMUSG00000006273
UniProt	P21281	P62814
RefSeq (mRNA)	NM_001693	NM_007509
RefSeq (protein)	NP_001684.2	NP_031535.2
Location (UCSC)	Chr 8: 20.2 – 20.23 Mb	Chr 8: 69.09 – 69.11 Mb
PubMed search	[1]	[2]
Wikidata

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V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.^[3][4][5]

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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.^[5]

In melanocytic cells ATP6V1B2 gene expression may be regulated by MITF.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Bernasconi P, Rausch T, Struve I, Morgan L, Taiz L (Nov 1990). "An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase". J Biol Chem. 265 (29): 17428–31. PMID 2145275.
4. Smith AN, Lovering RC, Futai M, Takeda J, Brown D, Karet FE (Oct 2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Mol Cell. 12 (4): 801–3. doi:10.1016/S1097-2765(03)00397-6. PMID 14580332.
5. "Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2".
6. Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.

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. 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.
• Nelson RD, Guo XL, Masood K, et al. (1992). "Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells.". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3541–5. doi:10.1073/pnas.89.8.3541. PMC 48904. PMID 1373501.
• Lee BS, Underhill DM, Crane MK, Gluck SL (1995). "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells.". J. Biol. Chem. 270 (13): 7320–9. doi:10.1074/jbc.270.13.7320. PMID 7706273.
• 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 (1): 191–8. doi:10.1042/bj3030191. PMC 1137575. PMID 7945239.