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Database: UniProt
Entry: P21281
LinkDB: P21281
Original site: P21281 
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}.
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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   Genevisible; P21281; HS.
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.
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
//
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