ID   IMPA1_MOUSE             Reviewed;         277 AA.
AC   O55023;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-NOV-2023, entry version 154.
DE   RecName: Full=Inositol monophosphatase 1;
DE            Short=IMP 1;
DE            Short=IMPase 1;
DE            EC=3.1.3.25 {ECO:0000250|UniProtKB:P29218};
DE   AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000250|UniProtKB:P29218};
DE            EC=3.1.3.94 {ECO:0000250|UniProtKB:P29218};
DE   AltName: Full=Inositol-1(or 4)-monophosphatase 1;
DE   AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
GN   Name=Impa1;
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].
RC   TISSUE=Brain;
RA   Parthasarathy L., Parthasarathy R., Vadnal R.E.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INDUCTION.
RX   PubMed=12877981; DOI=10.1016/s0169-328x(03)00120-7;
RA   Shamir A., Shaltiel G., Greenberg M.L., Belmaker R.H., Agam G.;
RT   "The effect of lithium on expression of genes for inositol biosynthetic
RT   enzymes in mouse hippocampus; a comparison with the yeast model.";
RL   Brain Res. Mol. Brain Res. 115:104-110(2003).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17068342; DOI=10.1074/jbc.m604474200;
RA   Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y., Furuichi T.,
RA   Chung S.-K., Yoshikawa T.;
RT   "Spatial expression patterns and biochemical properties distinguish a
RT   second myo-inositol monophosphatase IMPA2 from IMPA1.";
RL   J. Biol. Chem. 282:637-646(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP   PHOSPHATE, SUBUNIT, AND COFACTOR.
RX   PubMed=23027737; DOI=10.1107/s1744309112035191;
RA   Singh N., Halliday A.C., Knight M., Lack N.A., Lowe E., Churchill G.C.;
RT   "Cloning, expression, purification, crystallization and X-ray analysis of
RT   inositol monophosphatase from Mus musculus and Homo sapiens.";
RL   Acta Crystallogr. F 68:1149-1152(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
CC       monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-
CC       diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate,
CC       glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-
CC       glycerophosphate, and 2'-AMP as substrates.
CC       {ECO:0000250|UniProtKB:P29218}.
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:0000250|UniProtKB:P29218};
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:0000250|UniProtKB:P29218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000303|PubMed:23027737};
CC   -!- ACTIVITY REGULATION: Inhibited by Li(+), Ca(2+) and Mn(2+), but also by
CC       Mg(2+) at concentrations above 3 mM. {ECO:0000250|UniProtKB:P29218}.
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23027737}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in brain, small intestine, testis,
CC       kidney, and spleen (at protein level). {ECO:0000269|PubMed:17068342}.
CC   -!- INDUCTION: By lithium Li(+) in hippocamp.
CC       {ECO:0000269|PubMed:12877981}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF042730; AAB97469.1; -; mRNA.
DR   CCDS; CCDS17240.1; -.
DR   PDB; 4AS5; X-ray; 2.43 A; A/B/C/D=1-277.
DR   PDBsum; 4AS5; -.
DR   AlphaFoldDB; O55023; -.
DR   SMR; O55023; -.
DR   IntAct; O55023; 2.
DR   STRING; 10090.ENSMUSP00000068174; -.
DR   GlyGen; O55023; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O55023; -.
DR   PhosphoSitePlus; O55023; -.
DR   SwissPalm; O55023; -.
DR   EPD; O55023; -.
DR   jPOST; O55023; -.
DR   MaxQB; O55023; -.
DR   PaxDb; 10090-ENSMUSP00000068174; -.
DR   PeptideAtlas; O55023; -.
DR   ProteomicsDB; 269480; -.
DR   Pumba; O55023; -.
DR   AGR; MGI:1933158; -.
DR   MGI; MGI:1933158; Impa1.
DR   eggNOG; KOG2951; Eukaryota.
DR   InParanoid; O55023; -.
DR   PhylomeDB; O55023; -.
DR   BRENDA; 3.1.3.25; 3474.
DR   Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   UniPathway; UPA00823; UER00788.
DR   ChiTaRS; Impa1; mouse.
DR   PRO; PR:O55023; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O55023; Protein.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; ISO:MGI.
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; ISS:UniProtKB.
DR   GO; GO:0031403; F:lithium ion binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:MGI.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; ISO:MGI.
DR   CDD; cd01639; IMPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF26; INOSITOL MONOPHOSPHATASE 1; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR00378; LIIMPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..277
FT                   /note="Inositol monophosphatase 1"
FT                   /id="PRO_0000142514"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:23027737"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         90..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:23027737"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:23027737"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:23027737"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:23027737"
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:0000269|PubMed:23027737"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P29218"
FT   HELIX           4..26
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           45..61
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           95..100
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   TURN            125..128
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           169..183
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          207..215
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           218..230
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   STRAND          247..254
FT                   /evidence="ECO:0007829|PDB:4AS5"
FT   HELIX           256..265
FT                   /evidence="ECO:0007829|PDB:4AS5"
SQ   SEQUENCE   277 AA;  30436 MW;  EDBDB7BD24748E9D CRC64;
     MADPWQECMD YAVILARQAG EMIREALKNE MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE
     KYPCHSFIGE ESVAAGEKTV FTESPTWFID PIDGTTNFVH RFPFVAVSIG FLVNKEMEFG
     IVYSCVEDKM YTGRKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRKPE TLRIVLSNME
     KLCSIPIHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD MAGAGIIVTE AGGVLMDVTG
     GPFDLMSRRI IAANSITLAK RIAKEIEIIP LQRDDES
//