BPNT1_RAT
ID BPNT1_RAT Reviewed; 308 AA.
AC Q9Z1N4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7 {ECO:0000269|PubMed:10347153};
DE AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE AltName: Full=PAP-inositol 1,4-phosphatase;
DE Short=PIP;
DE AltName: Full=scHAL2 analogous 3;
GN Name=Bpnt1; Synonyms=Sal3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10347153; DOI=10.1074/jbc.274.23.16034;
RA Lopez-Coronado J.M., Belles J.M., Lesage F., Serrano R., Rodriguez P.L.;
RT "A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity,
RT 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-
RT phosphatase.";
RL J. Biol. Chem. 274:16034-16039(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 28-40; 145-167; 202-217; 225-232; 262-274 AND 278-297,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 5-308 IN COMPLEX WITH MAGNESIUM
RP AND AMP.
RX PubMed=11812139; DOI=10.1006/jmbi.2001.5271;
RA Patel S., Yenush L., Rodriguez P.L., Serrano R., Blundell T.L.;
RT "Crystal structure of an enzyme displaying both inositol-polyphosphate-1-
RT phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a
RT novel target of lithium therapy.";
RL J. Mol. Biol. 315:677-685(2002).
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. {ECO:0000269|PubMed:10347153}.
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 Evidence={ECO:0000269|PubMed:10347153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC Evidence={ECO:0000305|PubMed:10347153};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10347153};
CC -!- ACTIVITY REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate. Inhibited by calcium ions. {ECO:0000269|PubMed:10347153}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.8 umol/min/mg enzyme with adenosine 3',5'-bisphosphate as
CC substrate {ECO:0000269|PubMed:10347153};
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung,
CC liver, skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:10347153}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AJ000347; CAA04022.1; -; mRNA.
DR EMBL; BC085692; AAH85692.1; -; mRNA.
DR RefSeq; NP_741987.1; NM_171990.2.
DR RefSeq; XP_006250493.1; XM_006250431.3.
DR PDB; 1JP4; X-ray; 1.69 A; A=1-308.
DR PDBsum; 1JP4; -.
DR AlphaFoldDB; Q9Z1N4; -.
DR SMR; Q9Z1N4; -.
DR STRING; 10116.ENSRNOP00000003249; -.
DR iPTMnet; Q9Z1N4; -.
DR PhosphoSitePlus; Q9Z1N4; -.
DR SwissPalm; Q9Z1N4; -.
DR jPOST; Q9Z1N4; -.
DR PaxDb; Q9Z1N4; -.
DR PRIDE; Q9Z1N4; -.
DR GeneID; 64473; -.
DR KEGG; rno:64473; -.
DR UCSC; RGD:621833; rat.
DR CTD; 10380; -.
DR RGD; 621833; Bpnt1.
DR VEuPathDB; HostDB:ENSRNOG00000002378; -.
DR eggNOG; KOG3099; Eukaryota.
DR HOGENOM; CLU_034742_2_0_1; -.
DR InParanoid; Q9Z1N4; -.
DR PhylomeDB; Q9Z1N4; -.
DR BRENDA; 3.1.3.57; 5301.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; Q9Z1N4; -.
DR EvolutionaryTrace; Q9Z1N4; -.
DR PRO; PR:Q9Z1N4; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002378; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; Q9Z1N4; baseline and differential.
DR Genevisible; Q9Z1N4; RN.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:RGD.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IDA:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
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 PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Hydrolase; Lithium;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..308
FT /note="3'(2'),5'-bisphosphate nucleotidase 1"
FT /id="PRO_0000142529"
FT REGION 220..224
FT /note="Substrate"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11812139"
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:0000269|PubMed:11812139"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11812139"
FT BINDING 119..122
FT /ligand="substrate"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11812139"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11812139"
FT BINDING 195..198
FT /ligand="substrate"
FT BINDING 242
FT /ligand="substrate"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11812139"
FT BINDING 247
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
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"
FT HELIX 7..32
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:1JP4"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1JP4"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1JP4"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:1JP4"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:1JP4"
SQ SEQUENCE 308 AA; 33174 MW; 478C375057E88EC9 CRC64;
MASSHNVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRMVQMSICS
SLSRKFPKLT IIGEEDLPPG EVDQELIEDG QSEEILKQPC PSQYSAIKEE DLVVWVDPVD
GTKEYTEGLL DNVTVLIGIA YEGKAIAGII NQPYYNYQAG PDAVLGRTIW GVLGLGAFGF
QLKEAPAGKH IITTTRSHSN KLVTDCIAAM NPDNVLRVGG AGNKIIQLIE GKASAYVFAS
PGCKKWDTCA PEVILHAVGG KLTDIHGNPL QYDKEVKHMN SAGVLAALRN YEYYASRVPE
SVKSALIP
