ID VAB2_BOVIN STANDARD; PRT; 511 AA. AC P31408; Q28058; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Vacuolar ATP synthase subunit B, brain isoform (EC 3.6.3.14) (V-ATPase DE B2 subunit) (Vacuolar proton pump B isoform 2) (Endomembrane proton DE pump 58 kDa subunit). GN ATP6V1B2 OR ATP6B2. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=92228822; PubMed=1373501; RA Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., RA 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 SEQUENCE FROM N.A., AND 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 RT H(+)-ATPase in bovine tissues."; RL J. Biol. Chem. 267:3696-3706(1992). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=92070583; PubMed=1835703; 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 RT cell vacuolar ATPase."; RL FEBS Lett. 293:89-92(1991). CC -!- FUNCTION: NONCATALYTIC 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 -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). 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. 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; -. DR EMBL; M83131; AAA30391.1; -. DR EMBL; X58385; CAA41275.1; -. DR PIR; S32614; S32614. DR InterPro; IPR000793; ATPase_a/bC. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR005723; V_ATPase_V1_B. 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. KW Hydrolase; ATP synthesis; Hydrogen ion transport; Multigene family. FT CONFLICT 24 24 MISSING (IN REF. 1). FT CONFLICT 83 83 S -> T (IN REF. 2). FT CONFLICT 161 162 QC -> HF (IN REF. 1). FT CONFLICT 250 250 Q -> E (IN REF. 1 AND 2). FT CONFLICT 460 460 R -> K (IN REF. 1). FT CONFLICT 464 464 A -> T (IN REF. 1). FT CONFLICT 510 511 KH -> NS (IN REF. 2). SQ SEQUENCE 511 AA; 56575 MW; E8D70F9692F54459 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 ARFFKSDFEQ 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 //