MINP1_RAT
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 03-AUG-2022, entry version 124.
DE RecName: Full=Multiple inositol polyphosphate phosphatase 1;
DE EC=3.1.3.62;
DE AltName: Full=2,3-bisphosphoglycerate 3-phosphatase;
DE Short=2,3-BPG phosphatase;
DE EC=3.1.3.80;
DE AltName: Full=Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase;
DE Short=Ins(1,3,4,5)P(4) 3-phosphatase;
DE Flags: Precursor;
GN Name=Minpp1; Synonyms=Mipp1;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP 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 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 [3]
RP FUNCTION, AND 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: Acts as a phosphoinositide 5- and phosphoinositide 6-
CC phosphatase and regulates cellular levels of inositol pentakisphosphate
CC (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-
CC bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation
CC of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate
CC without formation of 3-phosphoglycerate. May play a role in bone
CC development (endochondral ossification). May play a role in the
CC transition of chondrocytes from proliferation to hypertrophy (By
CC similarity). Through the regulation of intracellular inositol
CC polyphosphates, may control intracellular cation homeostasis, including
CC that of calcium and iron, hence affecting free cation availability
CC required for neural cell signaling (By similarity).
CC {ECO:0000250|UniProtKB:F1NPQ2, ECO:0000250|UniProtKB:Q9UNW1,
CC ECO:0000269|PubMed:9923613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol hexakisphosphate + H2O = myo-inositol
CC pentakisphosphate (mixed isomers) + phosphate.; EC=3.1.3.62;
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:0000269|PubMed:9359836};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for Ins(1,3,4,5)P(4) {ECO:0000269|PubMed:9359836};
CC Vmax=302 pmol/min/ug enzyme {ECO:0000269|PubMed:9359836};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:8384201}.
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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000305}.
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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 GlyGen; O35217; 2 sites.
DR jPOST; O35217; -.
DR PaxDb; O35217; -.
DR PRIDE; O35217; -.
DR GeneID; 29688; -.
DR KEGG; rno:29688; -.
DR UCSC; RGD:3089; rat.
DR CTD; 9562; -.
DR RGD; 3089; Minpp1.
DR eggNOG; KOG1382; Eukaryota.
DR InParanoid; O35217; -.
DR OrthoDB; 1046588at2759; -.
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; IEA:UniProtKB-SubCell.
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:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; IBA:GO_Central.
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:0048015; P:phosphatidylinositol-mediated signaling; NAS:RGD.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Reference proteome; 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
