ID VATB2_HUMAN Reviewed; 511 AA. AC P21281; B2R5Z3; D3DSQ5; Q14544; Q15859; Q96IR0; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 27-MAR-2024, entry version 224. DE RecName: Full=V-type proton ATPase subunit B, brain isoform; DE Short=V-ATPase subunit B 2; DE AltName: Full=Endomembrane proton pump 58 kDa subunit; DE AltName: Full=HO57; DE AltName: Full=Vacuolar proton pump subunit B 2; GN Name=ATP6V1B2; Synonyms=ATP6B2, 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=1373501; DOI=10.1073/pnas.89.8.3541; RA Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S.; RT "Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase RT 56-kilodalton subunit in renal intercalated cells."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7945239; DOI=10.1042/bj3030191; RA van Hille B., Richener H., Schmid P., Puettner I., Green J.R., Bilbe G.; RT "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two RT human subunit B isoforms."; RL Biochem. J. 303:191-198(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; 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 [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.C., Zheng X.H., RA Zhong F., 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=Brain, and Eye; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45. RX PubMed=7706273; DOI=10.1074/jbc.270.13.7320; RA Lee B.S., Underhill D.M., Crane M.K., Gluck S.L.; RT "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in RT differentiating THP-1 cells."; RL J. Biol. Chem. 270:7320-7329(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-511. RC TISSUE=Brain; RX PubMed=2145275; DOI=10.1016/s0021-9258(18)38179-1; RA Bernasconi P., Rausch T., Struve I., Morgan L., Taiz L.; RT "An mRNA from human brain encodes an isoform of the B subunit of the RT vacuolar H(+)-ATPase."; RL J. Biol. Chem. 265:17428-17431(1990). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., RA Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP INVOLVEMENT IN DDOD. RX PubMed=24913193; DOI=10.1038/cr.2014.77; RA Yuan Y., Zhang J., Chang Q., Zeng J., Xin F., Wang J., Zhu Q., Wu J., RA Lu J., Guo W., Yan X., Jiang H., Zhou B., Li Q., Gao X., Yuan H., Yang S., RA Han D., Mao Z., Chen P., Lin X., Dai P.; RT "De novo mutation in ATP6V1B2 impairs lysosome acidification and causes RT dominant deafness-onychodystrophy syndrome."; RL Cell Res. 24:1370-1373(2014). RN [12] RP INVOLVEMENT IN ZLS2, AND VARIANT ZLS2 PRO-485. RX PubMed=25915598; DOI=10.1038/ng.3282; RA Kortuem F., Caputo V., Bauer C.K., Stella L., Ciolfi A., Alawi M., RA Bocchinfuso G., Flex E., Paolacci S., Dentici M.L., Grammatico P., RA Korenke G.C., Leuzzi V., Mowat D., Nair L.D., Nguyen T.T., Thierry P., RA White S.M., Dallapiccola B., Pizzuti A., Campeau P.M., Tartaglia M., RA Kutsche K.; RT "Mutations in KCNH1 and ATP6V1B2 cause Zimmermann-Laband syndrome."; RL Nat. Genet. 47:661-667(2015). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] 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 [15] 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 [16] {ECO:0007744|PDB:6WLZ, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH ADP, RP FUNCTION, AND IDENTIFICATION IN THE V-ATPASE COMPLEX. RX PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029; RA Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.; RT "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its RT Assembly."; RL Mol. Cell 80:501-511.e3(2020). 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:33065002). 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). In renal intercalated cells, can partially CC compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) CC into the urine under base-line conditions but not in conditions of acid CC load (By similarity). {ECO:0000250|UniProtKB:P62814, CC ECO:0000269|PubMed:33065002, 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 (PubMed:33065002). The V1 complex consists of three CC catalytic AB heterodimers that form a heterohexamer, three peripheral CC stalks each consisting of EG heterodimers, one central rotor including CC subunits D and F, and the regulatory subunits C and H CC (PubMed:33065002). The proton translocation complex V0 consists of the CC proton transport subunit a, a ring of proteolipid subunits c9c'', CC rotary subunit d, subunits e and f, and the accessory subunits CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). CC {ECO:0000269|PubMed:33065002}. CC -!- INTERACTION: CC P21281; P14136: GFAP; NbExp=3; IntAct=EBI-4290814, EBI-744302; CC P21281; P42858: HTT; NbExp=3; IntAct=EBI-4290814, EBI-466029; CC P21281; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-4290814, EBI-1055254; CC P21281; P07196: NEFL; NbExp=3; IntAct=EBI-4290814, EBI-475646; CC P21281; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-4290814, EBI-396669; CC P21281; P15884: TCF4; NbExp=3; IntAct=EBI-4290814, EBI-533224; CC P21281; O76024: WFS1; NbExp=3; IntAct=EBI-4290814, EBI-720609; CC P21281; PRO_0000449620 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-4290814, EBI-25475859; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:29993276}. Melanosome CC {ECO:0000269|PubMed:12643545}. Cytoplasm CC {ECO:0000250|UniProtKB:P62814}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated CC vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane CC protein {ECO:0000305}. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC {ECO:0000269|PubMed:12643545}. CC -!- TISSUE SPECIFICITY: Kidney; localizes to early distal nephron, CC encompassing thick ascending limbs and distal convoluted tubules (at CC protein level). {ECO:0000269|PubMed:29993276}. CC -!- DISEASE: Zimmermann-Laband syndrome 2 (ZLS2) [MIM:616455]: A form of CC Zimmermann-Laband syndrome, a rare developmental disorder characterized CC by facial dysmorphism with bulbous nose and thick floppy ears, gingival CC enlargement, hypoplasia or aplasia of terminal phalanges and nails, CC hypertrichosis, joint hyperextensibility, and hepatosplenomegaly. Some CC patients manifest intellectual disability with or without epilepsy. CC ZLS2 inheritance is autosomal dominant. {ECO:0000269|PubMed:25915598}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Deafness, congenital, with onychodystrophy, autosomal dominant CC (DDOD) [MIM:124480]: An autosomal dominant syndrome characterized CC mainly by congenital sensorineural hearing loss accompanied by CC dystrophic or absent nails. Coniform teeth, selective tooth agenesis, CC and hands and feet abnormalities are present in some patients. CC {ECO:0000269|PubMed:24913193}. 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 --------------------------------------------------------------------------- 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; M60346; AAA35610.1; -; mRNA. DR EMBL; L35249; AAA58661.1; -; mRNA. DR EMBL; AK312372; BAG35290.1; -; mRNA. DR EMBL; CH471080; EAW63758.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63759.1; -; Genomic_DNA. DR EMBL; BC003100; AAH03100.1; -; mRNA. DR EMBL; BC007309; AAH07309.1; -; mRNA. DR EMBL; BC030640; AAH30640.1; -; mRNA. DR EMBL; Z37165; CAA85522.1; -; Genomic_DNA. DR EMBL; X62949; CAA44721.1; -; mRNA. DR CCDS; CCDS6014.1; -. DR PIR; B44138; B44138. DR PIR; I39208; I39208. DR RefSeq; NP_001684.2; NM_001693.3. DR PDB; 6WLZ; EM; 2.90 A; D/E/F=1-511. DR PDB; 6WM2; EM; 3.10 A; D/E/F=1-511. DR PDB; 6WM3; EM; 3.40 A; D/E/F=1-511. DR PDB; 6WM4; EM; 3.60 A; D/E/F=1-511. DR PDB; 7U4T; EM; 3.60 A; D/E/F=1-511. DR PDB; 7UNF; EM; 4.08 A; O/P/Q=1-511. DR PDBsum; 6WLZ; -. DR PDBsum; 6WM2; -. DR PDBsum; 6WM3; -. DR PDBsum; 6WM4; -. DR PDBsum; 7U4T; -. DR PDBsum; 7UNF; -. DR AlphaFoldDB; P21281; -. DR EMDB; EMD-21845; -. DR EMDB; EMD-21847; -. DR EMDB; EMD-21848; -. DR EMDB; EMD-21849; -. DR EMDB; EMD-26334; -. DR EMDB; EMD-26623; -. DR SMR; P21281; -. DR BioGRID; 107009; 238. DR CORUM; P21281; -. DR DIP; DIP-47433N; -. DR IntAct; P21281; 62. DR MINT; P21281; -. DR STRING; 9606.ENSP00000276390; -. DR BindingDB; P21281; -. DR ChEMBL; CHEMBL5641; -. DR DrugBank; DB07347; 4-(2-Aminoethyl)Benzenesulfonyl Fluoride. DR DrugBank; DB05260; Gallium nitrate. DR DrugBank; DB01133; Tiludronic acid. DR DrugCentral; P21281; -. DR GuidetoPHARMACOLOGY; 812; -. DR TCDB; 3.A.2.2.4; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR GlyGen; P21281; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P21281; -. DR MetOSite; P21281; -. DR PhosphoSitePlus; P21281; -. DR SwissPalm; P21281; -. DR BioMuta; ATP6V1B2; -. DR DMDM; 12643271; -. DR REPRODUCTION-2DPAGE; IPI00007812; -. DR EPD; P21281; -. DR jPOST; P21281; -. DR MassIVE; P21281; -. DR MaxQB; P21281; -. DR PaxDb; 9606-ENSP00000276390; -. DR PeptideAtlas; P21281; -. DR ProteomicsDB; 53856; -. DR Pumba; P21281; -. DR Antibodypedia; 9185; 284 antibodies from 31 providers. DR DNASU; 526; -. DR Ensembl; ENST00000276390.7; ENSP00000276390.2; ENSG00000147416.11. DR GeneID; 526; -. DR KEGG; hsa:526; -. DR MANE-Select; ENST00000276390.7; ENSP00000276390.2; NM_001693.4; NP_001684.2. DR UCSC; uc003wzp.4; human. DR AGR; HGNC:854; -. DR CTD; 526; -. DR DisGeNET; 526; -. DR GeneCards; ATP6V1B2; -. DR HGNC; HGNC:854; ATP6V1B2. DR HPA; ENSG00000147416; Low tissue specificity. DR MalaCards; ATP6V1B2; -. DR MIM; 124480; phenotype. DR MIM; 606939; gene. DR MIM; 616455; phenotype. DR neXtProt; NX_P21281; -. DR OpenTargets; ENSG00000147416; -. DR Orphanet; 79499; Autosomal dominant deafness-onychodystrophy syndrome. DR Orphanet; 79500; DOORS syndrome. DR Orphanet; 3473; Zimmermann-Laband syndrome. DR PharmGKB; PA25155; -. DR VEuPathDB; HostDB:ENSG00000147416; -. DR eggNOG; KOG1351; Eukaryota. DR GeneTree; ENSGT00940000155068; -. DR HOGENOM; CLU_022916_3_0_1; -. DR InParanoid; P21281; -. DR OMA; GFKIKPR; -. DR OrthoDB; 5473721at2759; -. DR PhylomeDB; P21281; -. DR TreeFam; TF300313; -. DR BioCyc; MetaCyc:HS07429-MONOMER; -. DR PathwayCommons; P21281; -. 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; P21281; -. DR BioGRID-ORCS; 526; 843 hits in 1187 CRISPR screens. DR ChiTaRS; ATP6V1B2; human. DR GeneWiki; ATP6V1B2; -. DR GenomeRNAi; 526; -. DR Pharos; P21281; Tchem. DR PRO; PR:P21281; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P21281; Protein. DR Bgee; ENSG00000147416; Expressed in pons and 206 other cell types or tissues. DR ExpressionAtlas; P21281; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0001726; C:ruffle; IEA:Ensembl. 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:0015078; F:proton transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro. DR GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc. DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL. DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl. DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central. 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:SF5; V-TYPE PROTON ATPASE SUBUNIT B, BRAIN ISOFORM; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. DR Genevisible; P21281; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle; KW Deafness; Disease variant; Hydrogen ion transport; Ion transport; Membrane; KW Nucleotide-binding; Reference proteome; Synapse; Transport. FT CHAIN 1..511 FT /note="V-type proton ATPase subunit B, brain isoform" FT /id="PRO_0000144626" FT BINDING 400 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:33065002, FT ECO:0000312|PDB:6WLZ, ECO:0007744|PDB:6WM2, FT ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4" FT VARIANT 485 FT /note="R -> P (in ZLS2; dbSNP:rs730882177)" FT /evidence="ECO:0000269|PubMed:25915598" FT /id="VAR_073962" FT CONFLICT 28 FT /note="A -> S (in Ref. 1; CAA44721)" FT /evidence="ECO:0000305" FT CONFLICT 29 FT /note="R -> Q (in Ref. 5; AAH30640)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="Q -> R (in Ref. 5; AAH30640)" FT /evidence="ECO:0000305" FT CONFLICT 342 FT /note="E -> G (in Ref. 5; AAH30640)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="Q -> L (in Ref. 2; AAA58661)" FT /evidence="ECO:0000305" FT CONFLICT 424..425 FT /note="AC -> RA (in Ref. 7; AAA35610)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="M -> V (in Ref. 7; AAA35610)" FT /evidence="ECO:0000305" FT CONFLICT 510..511 FT /note="KH -> ND (in Ref. 7; AAA35610)" FT /evidence="ECO:0000305" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 81..90 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 93..98 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:6WLZ" FT TURN 126..129 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 148..152 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:6WM3" FT HELIX 199..209 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 217..223 FT /evidence="ECO:0007829|PDB:6WM3" FT STRAND 228..236 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 238..250 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 274..287 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 300..312 FT /evidence="ECO:0007829|PDB:6WLZ" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 327..335 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 347..355 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 357..359 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 364..370 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:6WLZ" FT TURN 403..405 FT /evidence="ECO:0007829|PDB:6WLZ" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 415..438 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 450..461 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 473..484 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 489..491 FT /evidence="ECO:0007829|PDB:6WM3" FT HELIX 497..503 FT /evidence="ECO:0007829|PDB:6WLZ" SQ SEQUENCE 511 AA; 56501 MW; E01E85BBA36E5DED CRC64; MALRAMRGIV NGAAPELPVP TGGPAVGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFER NFIAQGPYEN RTVFETLDIG WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H //