ID VATB2_BOVIN Reviewed; 511 AA. AC P31408; A4FUX5; Q28058; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 3. DT 03-AUG-2022, entry version 177. 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=Vacuolar proton pump subunit B 2; GN Name=ATP6V1B2; Synonyms=ATP6B2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; 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], PROTEIN SEQUENCE OF 30-58, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=1371275; DOI=10.1016/s0021-9258(19)50581-6; RA Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M.; RT "Differential expression of the 'B' subunit of the vacuolar H(+)-ATPase in RT bovine tissues."; RL J. Biol. Chem. 267:3696-3706(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1835703; DOI=10.1016/0014-5793(91)81158-5; RA Pan Y.X., Xu J., Strasser J.E., Howell M., Dean G.E.; RT "Structure and expression of subunit A from the bovine chromaffin cell RT vacuolar ATPase."; RL FEBS Lett. 293:89-92(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hippocampus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH ADP, RP FUNCTION, IDENTIFICATION IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY. RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9; RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.; RT "Cryo-EM structures of intact V-ATPase from bovine brain."; RL Nat. Commun. 11:3921-3921(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:32764564). 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:32764564). 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:32764564}. 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:32764564). 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:32764564). 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:32764564). CC {ECO:0000269|PubMed:32764564}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:P21281}. Melanosome CC {ECO:0000250|UniProtKB:P21281}. Cytoplasm CC {ECO:0000250|UniProtKB:P62814}. Cytoplasmic vesicle, clathrin-coated CC vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane CC protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic CC vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane CC protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level) CC (PubMed:1371275, PubMed:32764564). Expressed in all tissues tested, but CC highest in brain and in adrenal medulla (PubMed:1371275, CC PubMed:32764564). {ECO:0000269|PubMed:1371275, CC ECO:0000269|PubMed:32764564}. 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; M88690; AAA30400.1; -; mRNA. DR EMBL; M83131; AAA30391.1; -; mRNA. DR EMBL; X58385; CAA41275.1; -; mRNA. DR EMBL; BC123404; AAI23405.1; -; mRNA. DR PIR; S32614; S32614. DR RefSeq; NP_001001146.1; NM_001001146.1. DR RefSeq; NP_788844.2; NM_176671.3. DR PDB; 6XBW; EM; 3.37 A; D/E/F=1-511. DR PDB; 6XBY; EM; 3.79 A; D/E/F=1-511. DR PDB; 7KHR; EM; 3.62 A; D/E/F=1-511. DR PDBsum; 6XBW; -. DR PDBsum; 6XBY; -. DR PDBsum; 7KHR; -. DR AlphaFoldDB; P31408; -. DR SMR; P31408; -. DR CORUM; P31408; -. DR STRING; 9913.ENSBTAP00000024812; -. DR ChEMBL; CHEMBL4798; -. DR PaxDb; P31408; -. DR PeptideAtlas; P31408; -. DR PRIDE; P31408; -. DR Ensembl; ENSBTAT00000024812; ENSBTAP00000024812; ENSBTAG00000018646. DR GeneID; 338082; -. DR KEGG; bta:338082; -. DR CTD; 526; -. DR VEuPathDB; HostDB:ENSBTAG00000018646; -. DR VGNC; VGNC:26318; ATP6V1B2. DR eggNOG; KOG1351; Eukaryota. DR GeneTree; ENSGT00940000155068; -. DR HOGENOM; CLU_022916_3_0_1; -. DR InParanoid; P31408; -. DR OMA; GFKIKPR; -. DR OrthoDB; 541116at2759; -. DR TreeFam; TF300313; -. DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes. DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1. DR Proteomes; UP000009136; Chromosome 8. DR Bgee; ENSBTAG00000018646; Expressed in occipital lobe and 101 other tissues. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISS: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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro. DR GO; GO:0045851; P:pH reduction; IC:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB. 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 Direct protein sequencing; 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_0000144625" FT BINDING 400 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:32764564, FT ECO:0000312|PDB:6XBW, ECO:0007744|PDB:6XBY" FT CONFLICT 24 FT /note="Missing (in Ref. 1; AAA30400)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="S -> T (in Ref. 2; AAA30391)" FT /evidence="ECO:0000305" FT CONFLICT 161..162 FT /note="QC -> HF (in Ref. 1; AAA30400)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="E -> Q (in Ref. 3; CAA41275)" FT /evidence="ECO:0000305" FT CONFLICT 460 FT /note="R -> K (in Ref. 1; AAA30400)" FT /evidence="ECO:0000305" FT CONFLICT 464 FT /note="A -> T (in Ref. 1; AAA30400)" FT /evidence="ECO:0000305" FT CONFLICT 510..511 FT /note="KH -> NS (in Ref. 2; AAA30391)" FT /evidence="ECO:0000305" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 68..75 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 81..90 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 93..100 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 199..204 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 227..233 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 238..248 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 263..266 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 273..284 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 302..313 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 327..335 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 339..343 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 347..355 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 357..359 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 364..368 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 381..385 FT /evidence="ECO:0007829|PDB:6XBW" FT STRAND 392..399 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 402..405 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 408..411 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 415..438 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 446..461 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 473..482 FT /evidence="ECO:0007829|PDB:6XBW" FT TURN 483..486 FT /evidence="ECO:0007829|PDB:6XBW" FT HELIX 497..503 FT /evidence="ECO:0007829|PDB:6XBW" SQ SEQUENCE 511 AA; 56577 MW; E8DC915692F25E99 CRC64; MALRAMRGIV NGAAPELPVP TSGPLAGSRE 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 RTVYETLDIG WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H //