IMPA1_RAT
ID IMPA1_RAT Reviewed; 277 AA.
AC P97697;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Inositol monophosphatase 1;
DE Short=IMP 1;
DE Short=IMPase 1;
DE EC=3.1.3.25 {ECO:0000269|PubMed:9462881};
DE AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000303|PubMed:9462881};
DE EC=3.1.3.94 {ECO:0000269|PubMed:9462881};
DE AltName: Full=Inositol-1(or 4)-monophosphatase 1;
DE AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
GN Name=Impa1; Synonyms=Imp;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9210592; DOI=10.1016/s0378-1119(97)00045-0;
RA Parthasarathy L., Parthasarathy R., Vadnal R.;
RT "Molecular characterization of coding and untranslated regions of rat
RT cortex lithium-sensitive myo-inositol monophosphatase cDNA.";
RL Gene 191:81-87(1997).
RN [2]
RP SEQUENCE REVISION.
RA Parthasarathy L., Parthasarathy R., Vadnal R.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 157-167, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=1377913; DOI=10.1042/bj2840749;
RA McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R.,
RA Bailey F.J., Maigetter R., Ragan C.I.;
RT "cDNA cloning of human and rat brain myo-inositol monophosphatase.
RT Expression and characterization of the human recombinant enzyme.";
RL Biochem. J. 284:749-754(1992).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=9462881; DOI=10.1016/s0006-8993(97)01042-1;
RA Parthasarathy R., Parthasarathy L., Vadnal R.;
RT "Brain inositol monophosphatase identified as a galactose 1-phosphatase.";
RL Brain Res. 778:99-106(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides and has
CC been implicated as the pharmacological target for lithium action in
CC brain. Has broad substrate specificity and can use myo-inositol 1,3-
CC diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate,
CC glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-
CC glycerophosphate, and 2'-AMP as substrates (By similarity). Is equally
CC active with myo-inositol monophosphate and D-galactose 1-phosphate.
CC {ECO:0000250|UniProtKB:P29218, ECO:0000269|PubMed:9462881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:9462881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate;
CC Xref=Rhea:RHEA:29315, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58336; EC=3.1.3.94;
CC Evidence={ECO:0000269|PubMed:9462881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9462881};
CC -!- ACTIVITY REGULATION: Activity with myo-inositol monophosphate and D-
CC galactose 1-phosphate is inhibited by Li(+), Ca(2+) and Mn(2+), but
CC also by Mg(2+) at concentrations above 3 mM.
CC {ECO:0000269|PubMed:9462881}.
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9462881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1377913}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U84038; AAB63338.2; -; mRNA.
DR RefSeq; NP_114446.1; NM_032057.1.
DR AlphaFoldDB; P97697; -.
DR SMR; P97697; -.
DR BioGRID; 249742; 1.
DR MINT; P97697; -.
DR STRING; 10116.ENSRNOP00000014274; -.
DR ChEMBL; CHEMBL1293238; -.
DR iPTMnet; P97697; -.
DR PhosphoSitePlus; P97697; -.
DR SwissPalm; P97697; -.
DR jPOST; P97697; -.
DR PaxDb; P97697; -.
DR PRIDE; P97697; -.
DR GeneID; 83523; -.
DR KEGG; rno:83523; -.
DR UCSC; RGD:69254; rat.
DR CTD; 3612; -.
DR RGD; 69254; Impa1.
DR eggNOG; KOG2951; Eukaryota.
DR InParanoid; P97697; -.
DR OrthoDB; 915621at2759; -.
DR PhylomeDB; P97697; -.
DR BRENDA; 3.1.3.25; 5301.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; P97697; -.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:P97697; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:RGD.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052834; F:inositol monophosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0031403; F:lithium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:RGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:RGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR00378; LIIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Lithium; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..277
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142517"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
SQ SEQUENCE 277 AA; 30511 MW; 01A7FFB795D2AAED CRC64;
MADPWQECMD YAVILARQAG EMIREALKNK MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE
KYPYHSFIGE ESVASGEKTV FTEQPTWIID PIDGTTNFVH RFPFVAVSIG FVVNKEMEFG
VVYSCVEDKM YTGRKGKGAF CNGQKLRVSQ QEDITKSLLV TELGSSRKPE TLRIVLSNME
RLCSIPIHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD MAGAGIIVIE AGGVLLDVTG
GPFDLMSRRI IAASNIALAE RIAKELEIIP LQRDDES
