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 30-NOV-2010, entry version 103. 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=92228822; 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(+)- RT ATPase 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 MEDLINE=92156101; PubMed=1371275; RA Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M.; RT "Differential expression of the 'B' subunit of the vacuolar H(+)- RT ATPase in bovine tissues."; RL J. Biol. Chem. 267:3696-3706(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92070583; 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 CC of intracellular compartments in eukaryotic cells. CC -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a CC peripheral catalytic V1 complex (main components: subunits A, B, CC C, D, E, and F) attached to an integral membrane V0 proton pore CC complex (main component: the proteolipid protein). CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane CC protein. Melanosome (By similarity). Note=Endomembrane. CC -!- TISSUE SPECIFICITY: In all tissues tested, but highest in brain CC and in adrenal medulla. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. 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 IPI; IPI00688522; -. DR PIR; S32614; S32614. DR RefSeq; NP_001001146.1; NM_001001146.1. DR RefSeq; NP_788844.2; NM_176671.3. DR UniGene; Bt.4086; -. DR ProteinModelPortal; P31408; -. DR SMR; P31408; 55-507. DR STRING; P31408; -. DR Ensembl; ENSBTAT00000024812; ENSBTAP00000024812; ENSBTAG00000018646. DR GeneID; 338082; -. DR KEGG; bta:338082; -. DR CTD; 338082; -. DR eggNOG; maNOG09631; -. DR HOVERGEN; HBG002176; -. DR InParanoid; P31408; -. DR PhylomeDB; P31408; -. DR BioCyc; CATTLE:338082-MONOMER; -. DR BRENDA; 3.6.3.14; 251. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. 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:0046933; F:hydrogen ion transporting ATP synthase acti...; IEA:InterPro. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotati...; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR000194; ATPase_a/bsu_nucl-bd. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N. DR InterPro; IPR005723; ATPase_V1-cplx_bsu. DR InterPro; IPR022879; V-ATPase_su_B/beta. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 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; Phosphoprotein; Transport. FT CHAIN 1 511 V-type proton ATPase subunit B, brain FT isoform. FT /FTId=PRO_0000144625. FT MOD_RES 404 404 Phosphoserine (By similarity). FT MOD_RES 498 498 Phosphoserine (By similarity). FT CONFLICT 24 24 Missing (in Ref. 1; AAA30400). FT CONFLICT 83 83 S -> T (in Ref. 2; AAA30391). FT CONFLICT 161 162 QC -> HF (in Ref. 1; AAA30400). FT CONFLICT 250 250 E -> Q (in Ref. 3; CAA41275). FT CONFLICT 460 460 R -> K (in Ref. 1; AAA30400). FT CONFLICT 464 464 A -> T (in Ref. 1; AAA30400). FT CONFLICT 510 511 KH -> NS (in Ref. 2; AAA30391). 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 //