BPNT1_MOUSE
ID BPNT1_MOUSE Reviewed; 308 AA.
AC Q9Z0S1; Q3U8Z5; Q91XB9; Q9D7Y0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7 {ECO:0000269|PubMed:10224133};
DE AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE AltName: Full=PAP-inositol 1,4-phosphatase;
DE Short=PIP;
GN Name=Bpnt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT "Cloning and characterization of a mammalian lithium-sensitive bisphosphate
RT 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL J. Biol. Chem. 274:13619-13628(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-244, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:10224133}.
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:10224133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC Evidence={ECO:0000305|PubMed:10224133};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10224133};
CC -!- ACTIVITY REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate. {ECO:0000269|PubMed:10224133}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=520 nM for adenosine 3',5'-bisphosphate (PAP)
CC {ECO:0000269|PubMed:10224133};
CC Vmax=42 umol/min/mg enzyme with adenosine 3',5'-bisphosphate (PAP) as
CC substrate {ECO:0000269|PubMed:10224133};
CC pH dependence:
CC Optimum pH is approximately 7.5. {ECO:0000269|PubMed:10224133};
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney.
CC {ECO:0000269|PubMed:10224133}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF125043; AAD17330.1; -; mRNA.
DR EMBL; AK008714; BAB25850.1; -; mRNA.
DR EMBL; AK151931; BAE30807.1; -; mRNA.
DR EMBL; AK152009; BAE30872.1; -; mRNA.
DR EMBL; BC011036; AAH11036.1; -; mRNA.
DR CCDS; CCDS15597.1; -.
DR RefSeq; NP_035924.2; NM_011794.3.
DR AlphaFoldDB; Q9Z0S1; -.
DR SMR; Q9Z0S1; -.
DR BioGRID; 204743; 1.
DR STRING; 10090.ENSMUSP00000027916; -.
DR iPTMnet; Q9Z0S1; -.
DR PhosphoSitePlus; Q9Z0S1; -.
DR SwissPalm; Q9Z0S1; -.
DR REPRODUCTION-2DPAGE; Q9Z0S1; -.
DR EPD; Q9Z0S1; -.
DR jPOST; Q9Z0S1; -.
DR MaxQB; Q9Z0S1; -.
DR PaxDb; Q9Z0S1; -.
DR PeptideAtlas; Q9Z0S1; -.
DR PRIDE; Q9Z0S1; -.
DR ProteomicsDB; 281707; -.
DR Antibodypedia; 34625; 226 antibodies from 29 providers.
DR DNASU; 23827; -.
DR Ensembl; ENSMUST00000027916; ENSMUSP00000027916; ENSMUSG00000026617.
DR GeneID; 23827; -.
DR KEGG; mmu:23827; -.
DR UCSC; uc007dzc.1; mouse.
DR CTD; 10380; -.
DR MGI; MGI:1338800; Bpnt1.
DR VEuPathDB; HostDB:ENSMUSG00000026617; -.
DR eggNOG; KOG3099; Eukaryota.
DR GeneTree; ENSGT00940000157359; -.
DR InParanoid; Q9Z0S1; -.
DR OMA; QTEADRC; -.
DR PhylomeDB; Q9Z0S1; -.
DR TreeFam; TF314300; -.
DR BRENDA; 3.1.3.7; 3474.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; Q9Z0S1; -.
DR BioGRID-ORCS; 23827; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Bpnt1; mouse.
DR PRO; PR:Q9Z0S1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9Z0S1; protein.
DR Bgee; ENSMUSG00000026617; Expressed in small intestine Peyer's patch and 245 other tissues.
DR ExpressionAtlas; Q9Z0S1; baseline and differential.
DR Genevisible; Q9Z0S1; MM.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:MGI.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
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 1: Evidence at protein 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_0000142528"
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:0007744|PubMed:23806337"
FT CONFLICT 164
FT /note="A -> V (in Ref. 3; AAH11036)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="H -> R (in Ref. 3; AAH11036)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> A (in Ref. 1; AAD17330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33196 MW; D941FEA4C2E59E9D CRC64;
MASSHTVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRLVQMSICS
SLARKFPKLT IIGEEDLPPG EVDQELIEDG QWEEILKQPC PSQYSAIKEE DLVVWVDPLD
GTKEYTEGLL DNVTVLIGIA YEGKAIAGII NQPYYNYQAG PDAALGRTIW GVLGLGAFGF
QLKEAPAGKH IITTTRSHSN QLVTDCISAM NPDTVLRVGG AGNKIIQLIE GKASAYVFAS
PGCKKWDTCA PEVILHAVGG KLTDIHGNAL QYNKEVKHMN SAGVLAALRN YEYYASHVPE
SVKNALIP
