IMPA1_PONAB
ID IMPA1_PONAB Reviewed; 277 AA.
AC Q5R4X0; Q5R6Q6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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; Synonyms=IMPA;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P29218};
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:0000250|UniProtKB:P29218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; CR860429; CAH92554.1; -; mRNA.
DR EMBL; CR861120; CAH93196.1; -; mRNA.
DR RefSeq; NP_001127563.1; NM_001134091.1.
DR AlphaFoldDB; Q5R4X0; -.
DR SMR; Q5R4X0; -.
DR STRING; 9601.ENSPPYP00000021324; -.
DR GeneID; 100174641; -.
DR KEGG; pon:100174641; -.
DR CTD; 3612; -.
DR InParanoid; Q5R4X0; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142516"
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"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT CONFLICT 109
FT /note="I -> V (in Ref. 1; CAH92554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30171 MW; 664C1303B0801221 CRC64;
MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG
VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRIVLSNME
KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG
GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED
