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 02-OCT-2024, entry version 232. 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 NHERF1 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 NHERF1 and SCL4A7 (PubMed:12444018). CC {ECO:0000250|UniProtKB:P21281, 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:16769747, PubMed:29993276). 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 NHERF1 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 113. DR IntAct; P15313; 38. 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 jPOST; P15313; -. DR MassIVE; P15313; -. DR PaxDb; 9606-ENSP00000234396; -. DR PeptideAtlas; P15313; -. DR ProteomicsDB; 53129; -. DR Pumba; P15313; -. DR Antibodypedia; 4020; 430 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 AGR; HGNC:853; -. 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; ICELRTP; -. DR OrthoDB; 5473721at2759; -. DR PhylomeDB; P15313; -. DR TreeFam; TF300313; -. DR BioCyc; MetaCyc:HS03975-MONOMER; -. 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 1152 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 97 other cell types or tissues. DR ExpressionAtlas; P15313; baseline and differential. 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:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl. 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 CDD; cd18112; ATP-synt_V_A-type_beta_C; 1. DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1. DR CDD; cd01135; V_A-ATPase_B; 1. DR Gene3D; 3.40.50.12240; -; 1. 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 NCBIfam; TIGR01040; V-ATPase_V1_B; 1. DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1. DR PANTHER; PTHR43389:SF1; V-TYPE PROTON ATPASE SUBUNIT B, KIDNEY ISOFORM; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR Pfam; PF22919; ATP-synt_VA_C; 1. DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Proteomics identification; 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 NHERF1 and 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 //