VATB1_HUMAN
ID VATB1_HUMAN Reviewed; 513 AA.
AC P15313; Q53FY0; Q6P4H6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=V-type proton ATPase subunit B, kidney isoform;
DE Short=V-ATPase subunit B 1;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B 1;
GN Name=ATP6V1B1; Synonyms=ATP6B1, VATB, VPP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2527371; DOI=10.1073/pnas.86.16.6067;
RA Suedhof T.C., Fried V.A., Stone D.K., Johnston P.A., Xie X.-S.;
RT "Human endomembrane H+ pump strongly resembles the ATP-synthetase of
RT Archaebacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6067-6071(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-30.
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B., Zheng X.H., Zhong F.,
RA Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH SLC9A3R1 AND SLC4A7, DOMAIN, AND MUTAGENESIS OF LEU-513.
RX PubMed=12444018; DOI=10.1152/ajpcell.00225.2002;
RA Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P., Tatishchev S.,
RA Kurtz I.;
RT "The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs
RT involved in their interaction.";
RL Am. J. Physiol. 284:C667-C673(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29993276; DOI=10.1152/ajprenal.00539.2017;
RA Frische S., Chambrey R., Trepiccione F., Zamani R., Marcussen N.,
RA Alexander R.T., Skjoedt K., Svenningsen P., Dimke H.;
RT "H+-ATPase B1 subunit localizes to thick ascending limb and distal
RT convoluted tubule of rodent and human kidney.";
RL Am. J. Physiol. 315:F429-F444(2018).
RN [8]
RP REVIEW.
RX PubMed=32001091; DOI=10.1016/j.tibs.2019.12.007;
RA Vasanthakumar T., Rubinstein J.L.;
RT "Structure and Roles of V-type ATPases.";
RL Trends Biochem. Sci. 45:295-307(2020).
RN [9]
RP VARIANTS DRTA2 PRO-81; TRP-124; ARG-174; PRO-275; GLU-316; ARG-346 AND
RP SER-364, AND TISSUE SPECIFICITY.
RX PubMed=9916796; DOI=10.1038/5022;
RA Karet F.E., Finberg K.E., Nelson R.D., Nayir A., Mocan H., Sanjad S.A.,
RA Rodriguez-Soriano J., Santos F., Cremers C.W.R.J., Di Pietro A.,
RA Hoffbrand B.I., Winiarski J., Bakkaloglu A., Ozen S., Dusunsel R.,
RA Goodyer P., Hulton S.A., Wu D.K., Skvorak A.B., Morton C.C.,
RA Cunningham M.J., Jha V., Lifton R.P.;
RT "Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular
RT acidosis with sensorineural deafness.";
RL Nat. Genet. 21:84-90(1999).
RN [10]
RP VARIANTS DRTA2 PRO-81; VAL-123; CYS-157; PRO-275 AND ARG-346, AND VARIANTS
RP ILE-30 AND LYS-161.
RX PubMed=12414817; DOI=10.1136/jmg.39.11.796;
RA Stover E.H., Borthwick K.J., Bavalia C., Eady N., Fritz D.M., Rungroj N.,
RA Giersch A.B.S., Morton C.C., Axon P.R., Akil I., Al-Sabban E.A.,
RA Baguley D.M., Bianca S., Bakkaloglu A., Bircan Z., Chauveau D.,
RA Clermont M.-J., Guala A., Hulton S.A., Kroes H., Li Volti G., Mir S.,
RA Mocan H., Nayir A., Ozen S., Rodriguez Soriano J., Sanjad S.A., Tasic V.,
RA Taylor C.M., Topaloglu R., Smith A.N., Karet F.E.;
RT "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal
RT tubular acidosis with new evidence for hearing loss.";
RL J. Med. Genet. 39:796-803(2002).
RN [11]
RP VARIANT HIS-465, AND VARIANTS DRTA2 PRO-81 AND ARG-346.
RX PubMed=12579397; DOI=10.1007/s00467-002-1018-8;
RA Ruf R., Rensing C., Topaloglu R., Guay-Woodford L., Klein C., Vollmer M.,
RA Otto E., Beekmann F., Haller M., Wiedensohler A., Leumann E., Antignac C.,
RA Rizzoni G., Filler G., Brandis M., Weber J.L., Hildebrandt F.;
RT "Confirmation of the ATP6B1 gene as responsible for distal renal tubular
RT acidosis.";
RL Pediatr. Nephrol. 18:105-109(2003).
RN [12]
RP CHARACTERIZATION OF VARIANTS DRTA2 PRO-81; TRP-124; ARG-174; PRO-275;
RP GLU-316; ARG-346 AND SER-364, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16769747; DOI=10.1681/asn.2005121277;
RA Yang Q., Li G., Singh S.K., Alexander E.A., Schwartz J.H.;
RT "Vacuolar H+ -ATPase B1 subunit mutations that cause inherited distal renal
RT tubular acidosis affect proton pump assembly and trafficking in inner
RT medullary collecting duct cells.";
RL J. Am. Soc. Nephrol. 17:1858-1866(2006).
RN [13]
RP VARIANT DRTA2 31-ARG--LEU-513 DEL.
RX PubMed=19478356;
RA Sethi S.K., Singh N., Gil H., Bagga A.;
RT "Genetic studies in a family with distal renal tubular acidosis and
RT sensorineural deafness.";
RL Indian Pediatr. 46:425-427(2009).
RN [14]
RP VARIANT HIS-465.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (PubMed:16769747). V-ATPase is responsible
CC for acidifying and maintaining the pH of intracellular compartments and
CC in some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment
CC (PubMed:32001091). Essential for the proper assembly and activity of V-
CC ATPase (PubMed:16769747). In renal intercalated cells, mediates
CC secretion of protons (H+) into the urine thereby ensuring correct
CC urinary acidification (PubMed:16769747). Required for optimal olfactory
CC function by mediating the acidification of the nasal olfactory
CC epithelium (By similarity). {ECO:0000250|UniProtKB:Q91YH6,
CC ECO:0000269|PubMed:16769747, ECO:0000303|PubMed:32001091}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Forms a complex with SLC9A3R1 and SCL4A7
CC (PubMed:12444018). {ECO:0000250|UniProtKB:P21281,
CC ECO:0000269|PubMed:12444018}.
CC -!- INTERACTION:
CC P15313; P54253: ATXN1; NbExp=6; IntAct=EBI-2891281, EBI-930964;
CC P15313; P46379-2: BAG6; NbExp=3; IntAct=EBI-2891281, EBI-10988864;
CC P15313; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2891281, EBI-12593112;
CC P15313; O14645: DNALI1; NbExp=3; IntAct=EBI-2891281, EBI-395638;
CC P15313; P04792: HSPB1; NbExp=3; IntAct=EBI-2891281, EBI-352682;
CC P15313; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2891281, EBI-10975473;
CC P15313; O14901: KLF11; NbExp=3; IntAct=EBI-2891281, EBI-948266;
CC P15313; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2891281, EBI-396669;
CC P15313; Q13148: TARDBP; NbExp=6; IntAct=EBI-2891281, EBI-372899;
CC P15313; P02766: TTR; NbExp=3; IntAct=EBI-2891281, EBI-711909;
CC P15313; O76024: WFS1; NbExp=3; IntAct=EBI-2891281, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:29993276}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:Q91YH6}.
CC -!- TISSUE SPECIFICITY: Kidney; localizes to early distal nephron,
CC encompassing thick ascending limbs and distal convoluted tubules (at
CC protein level) (PubMed:29993276, PubMed:16769747). Expressed in the
CC cochlea and endolymphatic sac (PubMed:9916796).
CC {ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:29993276,
CC ECO:0000269|PubMed:9916796}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with SLC9A3R1 and
CC SCL4A7. {ECO:0000269|PubMed:12444018}.
CC -!- DISEASE: Renal tubular acidosis, distal, 2, with progressive
CC sensorineural hearing loss (DRTA2) [MIM:267300]: An autosomal recessive
CC disease characterized by the association of renal distal tubular
CC acidosis with sensorineural hearing loss. Distal renal tubular acidosis
CC is characterized by reduced ability to acidify urine, variable
CC hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and
CC nephrolithiasis. It is due to functional failure of alpha-intercalated
CC cells of the cortical collecting duct of the distal nephron, where
CC vectorial proton transport is required for urinary acidification.
CC {ECO:0000269|PubMed:12414817, ECO:0000269|PubMed:12579397,
CC ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:19478356,
CC ECO:0000269|PubMed:9916796}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M25809; AAA36498.1; ALT_INIT; mRNA.
DR EMBL; AK291121; BAF83810.1; -; mRNA.
DR EMBL; AK313194; BAG36011.1; -; mRNA.
DR EMBL; AK223151; BAD96871.1; -; mRNA.
DR EMBL; CH471053; EAW99790.1; -; Genomic_DNA.
DR EMBL; BC063411; AAH63411.1; -; mRNA.
DR CCDS; CCDS1912.1; -.
DR PIR; A33281; A33281.
DR RefSeq; NP_001683.2; NM_001692.3.
DR AlphaFoldDB; P15313; -.
DR SMR; P15313; -.
DR BioGRID; 107008; 112.
DR IntAct; P15313; 37.
DR MINT; P15313; -.
DR STRING; 9606.ENSP00000234396; -.
DR BindingDB; P15313; -.
DR ChEMBL; CHEMBL3217; -.
DR DrugBank; DB01133; Tiludronic acid.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P15313; -.
DR MetOSite; P15313; -.
DR PhosphoSitePlus; P15313; -.
DR BioMuta; ATP6V1B1; -.
DR DMDM; 215274116; -.
DR EPD; P15313; -.
DR jPOST; P15313; -.
DR MassIVE; P15313; -.
DR MaxQB; P15313; -.
DR PaxDb; P15313; -.
DR PeptideAtlas; P15313; -.
DR PRIDE; P15313; -.
DR ProteomicsDB; 53129; -.
DR Antibodypedia; 4020; 380 antibodies from 30 providers.
DR DNASU; 525; -.
DR Ensembl; ENST00000234396.10; ENSP00000234396.4; ENSG00000116039.13.
DR GeneID; 525; -.
DR KEGG; hsa:525; -.
DR MANE-Select; ENST00000234396.10; ENSP00000234396.4; NM_001692.4; NP_001683.2.
DR UCSC; uc002shj.4; human.
DR CTD; 525; -.
DR DisGeNET; 525; -.
DR GeneCards; ATP6V1B1; -.
DR GeneReviews; ATP6V1B1; -.
DR HGNC; HGNC:853; ATP6V1B1.
DR HPA; ENSG00000116039; Group enriched (kidney, salivary gland).
DR MalaCards; ATP6V1B1; -.
DR MIM; 192132; gene.
DR MIM; 267300; phenotype.
DR neXtProt; NX_P15313; -.
DR OpenTargets; ENSG00000116039; -.
DR Orphanet; 402041; Autosomal recessive distal renal tubular acidosis.
DR PharmGKB; PA25154; -.
DR VEuPathDB; HostDB:ENSG00000116039; -.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000161413; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P15313; -.
DR OMA; AVLDYHE; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; P15313; -.
DR TreeFam; TF300313; -.
DR BioCyc; MetaCyc:HS03975-MON; -.
DR PathwayCommons; P15313; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-77387; Insulin receptor recycling.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-983712; Ion channel transport.
DR SignaLink; P15313; -.
DR BioGRID-ORCS; 525; 8 hits in 1063 CRISPR screens.
DR GeneWiki; ATP6V1B1; -.
DR GenomeRNAi; 525; -.
DR Pharos; P15313; Tchem.
DR PRO; PR:P15313; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P15313; protein.
DR Bgee; ENSG00000116039; Expressed in right uterine tube and 95 other tissues.
DR ExpressionAtlas; P15313; baseline and differential.
DR Genevisible; P15313; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IMP:HGNC-UCL.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0015078; F:proton transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0055064; P:chloride ion homeostasis; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IMP:HGNC-UCL.
DR GO; GO:0045851; P:pH reduction; IMP:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0006885; P:regulation of pH; IMP:HGNC-UCL.
DR GO; GO:0035812; P:renal sodium excretion; IEA:Ensembl.
DR GO; GO:0003096; P:renal sodium ion transport; IEA:Ensembl.
DR GO; GO:0097254; P:renal tubular secretion; IMP:HGNC-UCL.
DR GO; GO:0003091; P:renal water homeostasis; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:UniProtKB.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Deafness; Disease variant;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..513
FT /note="V-type proton ATPase subunit B, kidney isoform"
FT /id="PRO_0000144624"
FT MOTIF 510..513
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:12444018"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT VARIANT 30
FT /note="T -> I (in dbSNP:rs17720303)"
FT /evidence="ECO:0000269|PubMed:12414817, ECO:0000269|Ref.3"
FT /id="VAR_021011"
FT VARIANT 31..513
FT /note="Missing (in DRTA2; dbSNP:rs121964879)"
FT /evidence="ECO:0000269|PubMed:19478356"
FT /id="VAR_085740"
FT VARIANT 81
FT /note="L -> P (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion; dbSNP:rs121964880)"
FT /evidence="ECO:0000269|PubMed:12414817,
FT ECO:0000269|PubMed:12579397, ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007866"
FT VARIANT 123
FT /note="G -> V (in DRTA2; dbSNP:rs1343871627)"
FT /evidence="ECO:0000269|PubMed:12414817"
FT /id="VAR_021012"
FT VARIANT 124
FT /note="R -> W (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion; dbSNP:rs727505222)"
FT /evidence="ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007867"
FT VARIANT 157
FT /note="R -> C (in DRTA2; dbSNP:rs782500780)"
FT /evidence="ECO:0000269|PubMed:12414817"
FT /id="VAR_021013"
FT VARIANT 161
FT /note="E -> K (in dbSNP:rs114234874)"
FT /evidence="ECO:0000269|PubMed:12414817"
FT /id="VAR_021014"
FT VARIANT 174
FT /note="M -> R (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion)"
FT /evidence="ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007868"
FT VARIANT 275
FT /note="T -> P (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion; dbSNP:rs1161604514)"
FT /evidence="ECO:0000269|PubMed:12414817,
FT ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:9916796"
FT /id="VAR_007869"
FT VARIANT 316
FT /note="G -> E (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion; dbSNP:rs1553420413)"
FT /evidence="ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007870"
FT VARIANT 346
FT /note="P -> R (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion; dbSNP:rs781838938)"
FT /evidence="ECO:0000269|PubMed:12414817,
FT ECO:0000269|PubMed:12579397, ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007871"
FT VARIANT 364
FT /note="G -> S (in DRTA2; disruption of V-ATPase assembly
FT resulting in loss of enzyme activity; impaired trafficking
FT of V-ATPase to apical cell membrane; impaired renal proton
FT secretion)"
FT /evidence="ECO:0000269|PubMed:16769747,
FT ECO:0000269|PubMed:9916796"
FT /id="VAR_007872"
FT VARIANT 465
FT /note="R -> H (in dbSNP:rs142905621)"
FT /evidence="ECO:0000269|PubMed:12579397,
FT ECO:0000269|PubMed:27535533"
FT /id="VAR_021015"
FT MUTAGEN 513
FT /note="L->G: Loss of interactions with SLC9A3R1 and
FT SCL4A7."
FT /evidence="ECO:0000269|PubMed:12444018"
FT CONFLICT 467
FT /note="V -> M (in Ref. 1; AAA36498)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="G -> S (in Ref. 1; AAA36498)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="A -> R (in Ref. 1; AAA36498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56833 MW; 5399E2849F3B99AA CRC64;
MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP LVVLDRVKFA
QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID ARKTTCEFTG DILRTPVSED
MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ PINPHSRIYP EEMIQTGISP IDVMNSIARG
QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS
DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP
DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY
AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFINQG PYENRSVFES LDLGWKLLRI
FPKEMLKRIP QAVIDEFYSR EGALQDLAPD TAL
