VATB2_HUMAN
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 03-AUG-2022, entry version 215.
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 PDBsum; 6WLZ; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; P21281; -.
DR SMR; P21281; -.
DR BioGRID; 107009; 205.
DR CORUM; P21281; -.
DR DIP; DIP-47433N; -.
DR IntAct; P21281; 60.
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 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; P21281; -.
DR PeptideAtlas; P21281; -.
DR PRIDE; P21281; -.
DR ProteomicsDB; 53856; -.
DR Antibodypedia; 9185; 256 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 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; 541116at2759; -.
DR PhylomeDB; P21281; -.
DR TreeFam; TF300313; -.
DR BioCyc; MetaCyc:HS07429-MON; -.
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; 805 hits in 1094 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 204 other tissues.
DR ExpressionAtlas; P21281; baseline and differential.
DR Genevisible; P21281; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016021; C:integral component of 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:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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:0007035; P:vacuolar acidification; IBA:GO_Central.
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 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
