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 12-AUG-2020, entry version 170. 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. CC -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of CC vacuolar ATPase. V-ATPase is responsible for acidifying a variety of CC intracellular compartments in eukaryotic cells. CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F) CC attached to an integral membrane V0 proton pore complex (main CC component: the proteolipid protein). CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. CC Melanosome {ECO:0000250}. Note=Endomembrane. 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 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 VGNC; VGNC:26318; ATP6V1B2. DR eggNOG; KOG1351; Eukaryota. DR GeneTree; ENSGT00940000155068; -. DR HOGENOM; CLU_022916_3_0_1; -. DR InParanoid; P31408; -. DR KO; K02147; -. DR OMA; RTFPEDM; -. DR OrthoDB; 541116at2759; -. DR TreeFam; TF300313; -. DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes. DR Reactome; R-BTA-77387; Insulin receptor recycling. DR Reactome; R-BTA-917977; Transferrin endocytosis and recycling. DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1. DR Reactome; R-BTA-983712; Ion channel transport. DR Proteomes; UP000009136; Chromosome 8. DR Bgee; ENSBTAG00000018646; Expressed in brain and 19 other tissues. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl. 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:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro. DR GO; GO:0001726; C:ruffle; IEA:Ensembl. 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 Direct protein sequencing; Hydrogen ion transport; Hydrolase; KW Ion transport; Membrane; 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" 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 //