ID BPNT1_BOVIN Reviewed; 308 AA. AC Q3ZCK3; A7E3X5; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 30. DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1; DE EC=3.1.3.7; DE AltName: Full=Bisphosphate 3'-nucleotidase 1; GN Name=BPNT1; 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 [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) CC to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine CC 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards CC inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- CC trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, CC Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6 (By similarity). CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O = CC adenosine 5'-phosphate + phosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- ENZYME REGULATION: Uncompetitive inhibition by micromolar CC concentrations of lithium. Competitive inhibition by inositol 1,4- CC bisphosphate (By similarity). CC -!- SIMILARITY: Belongs to the inositol monophosphatase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT030746; ABS45062.1; -; mRNA. DR EMBL; BC102110; AAI02111.1; -; mRNA. DR IPI; IPI00687550; -. DR RefSeq; NP_001029711.1; -. DR UniGene; Bt.49571; -. DR SMR; Q3ZCK3; 7-308. DR Ensembl; ENSBTAG00000004064; Bos taurus. DR GeneID; 521254; -. DR KEGG; bta:521254; -. DR HOVERGEN; Q3ZCK3; -. DR OMA; Q3ZCK3; GFQLKEA. DR BRENDA; 3.1.3.7; 251. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:EC. DR GO; GO:0004437; F:inositol or phosphatidylinositol phosphatas...; IEA:InterPro. DR GO; GO:0031403; F:lithium ion binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR InterPro; IPR000760; Inositol_P. DR PANTHER; PTHR20854; Inositol_P; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00378; INOSPHPHTASE. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Hydrolase; Lithium; Magnesium; Metal-binding. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 308 3'(2'),5'-bisphosphate nucleotidase 1. FT /FTId=PRO_0000282934. FT REGION 195 198 Substrate binding (By similarity). FT METAL 74 74 Magnesium 1 (By similarity). FT METAL 117 117 Magnesium 1 (By similarity). FT METAL 117 117 Magnesium 2 (By similarity). FT METAL 119 119 Magnesium 1; via carbonyl oxygen (By FT similarity). FT METAL 120 120 Magnesium 2 (By similarity). FT METAL 247 247 Magnesium 2 (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 308 AA; 33328 MW; 8A9184010B4B893C CRC64; MASSPTVLMR LVASAYSIAQ KAGTIVRRVI AEGDLGIIEK TCATDLQTKA DRLVQVSICS SLARKFPKLT IIGEEDLPPE DVDQELIEDG QWEEILKQPC PSQYSAIKEE DLVVWVDPLD GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI NQPYYNYQAG PDAVLGRTIW GVLGLGAFGF QLKEAPAGKH IITTTRSHNS QLVTDCITAM NPDDVLRVGG AGNKIIQLIE GKASAYVFAS PGCKKWDTCA PEVILHAVGG KLTDIHGNAL QYNKEVKHMN SAGVLATLRN YDYYASRVPQ SVKNALVP //