BPNT1_BOVIN
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 03-AUG-2022, entry version 106.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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) to
CC 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-trisphosphate
CC (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2,
CC Ins(1,3,4,5)P4 or InsP6 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; BT030746; ABS45062.1; -; mRNA.
DR EMBL; BC102110; AAI02111.1; -; mRNA.
DR RefSeq; NP_001029711.1; NM_001034539.2.
DR AlphaFoldDB; Q3ZCK3; -.
DR SMR; Q3ZCK3; -.
DR STRING; 9913.ENSBTAP00000005311; -.
DR PaxDb; Q3ZCK3; -.
DR PeptideAtlas; Q3ZCK3; -.
DR PRIDE; Q3ZCK3; -.
DR Ensembl; ENSBTAT00000005311; ENSBTAP00000005311; ENSBTAG00000004064.
DR GeneID; 521254; -.
DR KEGG; bta:521254; -.
DR CTD; 10380; -.
DR VEuPathDB; HostDB:ENSBTAG00000004064; -.
DR eggNOG; KOG3099; Eukaryota.
DR GeneTree; ENSGT00940000157359; -.
DR HOGENOM; CLU_034742_2_0_1; -.
DR InParanoid; Q3ZCK3; -.
DR OrthoDB; 1096950at2759; -.
DR TreeFam; TF314300; -.
DR Reactome; R-BTA-156584; Cytosolic sulfonation of small molecules.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000004064; Expressed in rumen papilla and 103 other tissues.
DR ExpressionAtlas; Q3ZCK3; baseline and differential.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95861"
FT CHAIN 2..308
FT /note="3'(2'),5'-bisphosphate nucleotidase 1"
FT /id="PRO_0000282934"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195..198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95861"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95861"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95861"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0S1"
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
