V-type proton ATPase subunit B, kidney isoform is an
enzyme that in humans is encoded by the ATP6V1B1gene.[5][6][7]
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.[7]
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.
PMID9442887.
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.
PMID8125298.
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.
PMID8597961.
S2CID10616789.
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.
PMID9373149.
V-type proton ATPase subunit B, kidney isoform is an
enzyme that in humans is encoded by the ATP6V1B1gene.[5][6][7]
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.[7]
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.
PMID9442887.
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.
PMID8125298.
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.
PMID8597961.
S2CID10616789.
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.
PMID9373149.