ID   MINP1_RAT               Reviewed;         481 AA.
AC   O35217;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 3.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000305|PubMed:9359836};
DE            EC=3.1.3.62 {ECO:0000269|PubMed:1653239, ECO:0000269|PubMed:9359836};
DE   AltName: Full=2,3-bisphosphoglycerate 3-phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE            Short=2,3-BPG phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE            EC=3.1.3.80 {ECO:0000250|UniProtKB:Q9UNW1};
DE   AltName: Full=Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase {ECO:0000303|PubMed:1653239};
DE            Short=Ins(1,3,4,5)P(4) 3-phosphatase {ECO:0000303|PubMed:1653239};
DE   Flags: Precursor;
GN   Name=Minpp1 {ECO:0000312|RGD:3089};
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], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN
RP   SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=9359836; DOI=10.1042/bj3280075;
RA   Craxton A., Caffrey J.J., Burkhart W., Safrany S.T., Shears S.B.;
RT   "Molecular cloning and expression of a rat hepatic multiple inositol
RT   polyphosphate phosphatase.";
RL   Biochem. J. 328:75-81(1997).
RN   [2]
RP   IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=1653239; DOI=10.1016/s0021-9258(18)55328-x;
RA   Nogimori K., Hughes P.J., Glennon M.C., Hodgson M.E., Putney J.W. Jr.,
RA   Shears S.B.;
RT   "Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
RT   activity from rat liver and the evaluation of its substrate specificity.";
RL   J. Biol. Chem. 266:16499-16506(1991).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8384201; DOI=10.1016/s0021-9258(18)53233-6;
RA   Ali N., Craxton A., Shears S.B.;
RT   "Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside
RT   endoplasmic reticulum.";
RL   J. Biol. Chem. 268:6161-6167(1993).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=9923613; DOI=10.1016/s0014-5793(98)01636-6;
RA   Caffrey J.J., Hidaka K., Matsuda M., Hirata M., Shears S.B.;
RT   "The human and rat forms of multiple inositol polyphosphate phosphatase:
RT   functional homology with a histidine acid phosphatase up-regulated during
RT   endochondral ossification.";
RL   FEBS Lett. 442:99-104(1999).
CC   -!- FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes
CC       1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-
CC       inositol hexakisphosphate (InsP6) to a range of less phosphorylated
CC       inositol phosphates. This regulates the availability of these various
CC       small molecule second messengers and metal chelators which control many
CC       aspects of cell physiology (PubMed:9359836, PubMed:1653239). Has a weak
CC       in vitro activity towards 1D-myo-inositol 1,4,5-trisphosphate which is
CC       unlikely to be physiologically relevant. By regulating intracellular
CC       inositol polyphosphates pools, which act as metal chelators, it may
CC       control the availability of intracellular calcium and iron, which are
CC       important for proper neuronal development and homeostasis. May have a
CC       dual substrate specificity, and function as a 2,3-bisphosphoglycerate
CC       3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-
CC       phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of
CC       the Rapoport-Luebering glycolytic bypass and is a regulator of systemic
CC       oxygen homeostasis as the major allosteric effector of hemoglobin (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UNW1, ECO:0000269|PubMed:1653239,
CC       ECO:0000269|PubMed:9359836}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:58130; EC=3.1.3.62;
CC         Evidence={ECO:0000269|PubMed:1653239};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000269|PubMed:1653239};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:195535; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC         ChEBI:CHEBI:195537; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol
CC         1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537,
CC         ChEBI:CHEBI:195539; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-
CC         phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539;
CC         EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,3,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:20960,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130,
CC         ChEBI:CHEBI:58747; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20961;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,3,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77111,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58747,
CC         ChEBI:CHEBI:195534; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77112;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,3-trisphosphate + phosphate; Xref=Rhea:RHEA:77123,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195534,
CC         ChEBI:CHEBI:195536; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77124;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol
CC         2,3-bisphosphate + phosphate; Xref=Rhea:RHEA:77127,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195536,
CC         ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77128;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-
CC         phosphate + phosphate; Xref=Rhea:RHEA:77139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195538;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77140;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627,
CC         ChEBI:CHEBI:57733; Evidence={ECO:0000269|PubMed:1653239,
CC         ECO:0000269|PubMed:9359836};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144;
CC         Evidence={ECO:0000269|PubMed:1653239, ECO:0000269|PubMed:9359836};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77147,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627,
CC         ChEBI:CHEBI:203600; Evidence={ECO:0000269|PubMed:9359836};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77148;
CC         Evidence={ECO:0000269|PubMed:9359836};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate +
CC         phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 nM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
CC         {ECO:0000269|PubMed:1653239};
CC         KM=0.3 nM for 1D-myo-inositol hexakisphosphate
CC         {ECO:0000269|PubMed:1653239};
CC         Vmax=211 nmol/min/mg enzyme with 1D-myo-inositol
CC         1,3,4,5,6-pentakisphosphate as substrate
CC         {ECO:0000269|PubMed:1653239};
CC         Vmax=12 nmol/min/mg enzyme with 1D-myo-inositol hexakisphosphate as
CC         substrate {ECO:0000269|PubMed:1653239};
CC       pH dependence:
CC         Optimum pH is 5-9 with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate or
CC         1D-myo-inositol hexakisphosphate as substrate in absence of
CC         magnesium. Optimum pH is 7.4 with 1D-myo-inositol hexakisphosphate as
CC         substrate in presence of 1 mM magnesium.
CC         {ECO:0000269|PubMed:1653239};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:8384201}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}.
CC       Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with
CC       the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney and
CC       liver. Expressed in chondrocytes with an elevated expression in
CC       hypertrophic chondrocytes. {ECO:0000269|PubMed:9359836,
CC       ECO:0000269|PubMed:9923613}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UNW1}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC       subfamily. {ECO:0000305}.
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; AF012714; AAC53453.2; -; mRNA.
DR   RefSeq; NP_062136.1; NM_019263.1.
DR   AlphaFoldDB; O35217; -.
DR   SMR; O35217; -.
DR   STRING; 10116.ENSRNOP00000015017; -.
DR   GlyCosmos; O35217; 2 sites, No reported glycans.
DR   GlyGen; O35217; 2 sites.
DR   PhosphoSitePlus; O35217; -.
DR   jPOST; O35217; -.
DR   PaxDb; 10116-ENSRNOP00000015017; -.
DR   GeneID; 29688; -.
DR   KEGG; rno:29688; -.
DR   UCSC; RGD:3089; rat.
DR   AGR; RGD:3089; -.
DR   CTD; 9562; -.
DR   RGD; 3089; Minpp1.
DR   eggNOG; KOG1382; Eukaryota.
DR   InParanoid; O35217; -.
DR   OrthoDB; 1072311at2759; -.
DR   PhylomeDB; O35217; -.
DR   Reactome; R-RNO-1855231; Synthesis of IPs in the ER lumen.
DR   PRO; PR:O35217; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016158; F:3-phytase activity; IEA:RHEA.
DR   GO; GO:0008707; F:4-phytase activity; IEA:RHEA.
DR   GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; ISO:RGD.
DR   GO; GO:0016312; F:inositol bisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052827; F:inositol pentakisphosphate phosphatase activity; ISO:RGD.
DR   GO; GO:0052745; F:inositol phosphate phosphatase activity; ISO:RGD.
DR   GO; GO:0046030; F:inositol trisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030351; F:inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity; IDA:RGD.
DR   GO; GO:0030352; F:inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity; IDA:RGD.
DR   GO; GO:0004446; F:inositol-hexakisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; ISS:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:RGD.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF57; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..481
FT                   /note="Multiple inositol polyphosphate phosphatase 1"
FT                   /id="PRO_0000019585"
FT   MOTIF           478..481
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2L6"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        33
FT                   /note="P -> H (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357
FT                   /note="S -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  54589 MW;  44E7BC000129DB47 CRC64;
     MLRGARSHLS ASVALAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK TRYEDVNPWL
     LGDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR KLRQLQGLLQ TRESVDGGSR
     VAAALDQWPL WYDDWMDGQL VEKGRQDMRQ LALRLAALFP DLFCRENYGR LRLITSSKHR
     CVDSSAAFLQ GLWQHYHPGL PPPDVSDMEC DPPRVNDKLM RFFDHCEKFL TEVERNATAL
     YHVEAFKTGP EMQTVLKKVA ATLQVPVNNL NADLIQVAFF TCSFDLAIQG VHSPWCDVFD
     VDDAKVLEYL NDLKQYWKRS YGYAINSRSS CNLFQDIFLH LDKAVEQKQR SQPVSSSVIL
     QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVHREFRSG HIVPYASNLI FVLYHCEDAQ
     TPQEKFQIQM LLNEKVLPLA HSQKTVALYE DLKNHYQDIL QSCQTSKECN LPKVNITSDE
     L
//