ATP6V1B2

From Wikipedia, the free encyclopedia

ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2

Identifiers

ATP6V1B2; VATB; VPP3; ATP6B1B2; ATP6B2; HO57; Vma2

External IDs

OMIM: 606939 MGI: 109618 HomoloGene: 1279

Gene ontology
Molecular Function:	• ATP binding • hydrogen-exporting ATPase activity, phosphorylative mechanism • hydrolase activity • metal ion binding • hydrogen ion transporting ATP synthase activity, rotational mechanism • hydrogen ion transporting ATPase activity, rotational mechanism
Cellular Component:	• cytoplasm • proton-transporting two-sector ATPase complex
Biological Process:	• ion transport • ATP synthesis coupled proton transport • energy coupled proton transport, against electrochemical gradient

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001693 (mRNA)
NP_001684 (protein)

NM_007509 (mRNA)
NP_031535 (protein)

Location

Chr 8: 20.1 - 20.12 Mb

Chr 8: 72.02 - 72.04 Mb

Pubmed search

[1]

[2]

ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2, also known as ATP6V1B2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2.

[edit] Further reading

Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 ( Pt 3): 697-712. 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. PMID 10224039.
Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3-5. 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. PMID 12788495.
Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453-7. 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. PMID 1373501.
Bernasconi P, Rausch T, Struve I, et al. (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.
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. 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 ( Pt 1): 191-8. PMID 7945239.