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 29-SEP-2021, entry version 174. 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], AND PROTEIN SEQUENCE OF 30-58. RC TISSUE=Brain; RX PubMed=1371275; 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] RP SUBUNIT. 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 (By similarity). V-ATPase is responsible for CC acidifying and maintaining the pH of intracellular compartments and in CC some cell types, is targeted to the plasma membrane, where it is CC responsible for acidifying the extracellular environment (By CC similarity). In renal intercalated cells, can partially compensate the CC lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine CC under base-line conditions but not in conditions of acid load (By CC similarity). {ECO:0000250|UniProtKB:P21281, CC ECO:0000250|UniProtKB:P62814}. 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, and subunits e and Ac45 (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}. CC -!- TISSUE SPECIFICITY: In all tissues tested, but highest in brain and in CC adrenal medulla. 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 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 96 other tissues. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro. DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro. 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; Cell membrane; Cytoplasm; Direct protein sequencing; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1..511 FT /note="V-type proton ATPase subunit B, brain isoform" FT /id="PRO_0000144625" 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 //