IMPA1_BOVIN
ID IMPA1_BOVIN Reviewed; 277 AA.
AC P20456; Q17QE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 165.
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=IMPA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1690719; DOI=10.1016/s0021-9258(19)39271-3;
RA Diehl R.E., Whiting P., Potter J., Gee N., Ragan C.I., Linemeyer D.,
RA Schoepfer R., Bennett C., Dixon R.A.F.;
RT "Cloning and expression of bovine brain inositol monophosphatase.";
RL J. Biol. Chem. 265:5946-5949(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RX PubMed=15858264; DOI=10.1107/s0907444905004038;
RA Gill R., Mohammed F., Badyal R., Coates L., Erskine P., Thompson D.,
RA Cooper J., Gore M., Wood S.;
RT "High-resolution structure of myo-inositol monophosphatase, the putative
RT target of lithium therapy.";
RL Acta Crystallogr. D 61:545-555(2005).
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, glucose-1-phosphate, glucose-6-
CC phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as
CC substrates (By similarity). Is equally active with myo-inositol
CC 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, ECO:0000303|PubMed:15858264};
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:15858264,
CC ECO:0000269|PubMed:9462881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {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; J05394; AAA30589.1; -; mRNA.
DR EMBL; BC118411; AAI18412.1; -; mRNA.
DR PIR; A35223; A35223.
DR RefSeq; NP_776786.1; NM_174361.4.
DR RefSeq; XP_005215709.1; XM_005215652.3.
DR RefSeq; XP_015330016.1; XM_015474530.1.
DR PDB; 2BJI; X-ray; 1.30 A; A/B=1-277.
DR PDBsum; 2BJI; -.
DR AlphaFoldDB; P20456; -.
DR SMR; P20456; -.
DR STRING; 9913.ENSBTAP00000015548; -.
DR BindingDB; P20456; -.
DR ChEMBL; CHEMBL4505; -.
DR PaxDb; P20456; -.
DR PRIDE; P20456; -.
DR Ensembl; ENSBTAT00000015548; ENSBTAP00000015548; ENSBTAG00000011709.
DR GeneID; 281865; -.
DR KEGG; bta:281865; -.
DR CTD; 3612; -.
DR VEuPathDB; HostDB:ENSBTAG00000011709; -.
DR VGNC; VGNC:30184; IMPA1.
DR eggNOG; KOG2951; Eukaryota.
DR GeneTree; ENSGT00940000154634; -.
DR HOGENOM; CLU_044118_1_0_1; -.
DR InParanoid; P20456; -.
DR OMA; RVDGYWE; -.
DR OrthoDB; 915621at2759; -.
DR TreeFam; TF313194; -.
DR BRENDA; 3.1.3.25; 908.
DR Reactome; R-BTA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; P20456; -.
DR UniPathway; UPA00823; UER00788.
DR EvolutionaryTrace; P20456; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000011709; Expressed in mesenteric lymph node and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
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; IEA:Ensembl.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Lithium;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..277
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142512"
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:15858264"
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:0000269|PubMed:15858264"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15858264"
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:0000269|PubMed:15858264"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15858264"
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:15858264"
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 HELIX 4..28
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2BJI"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2BJI"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:2BJI"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2BJI"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:2BJI"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2BJI"
SQ SEQUENCE 277 AA; 30056 MW; 773DDB0291AC5977 CRC64;
MADPWQECMD YAVTLAGQAG EVVREALKNE MNIMVKSSPA DLVTATDQKV EKMLITSIKE
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH GFPFVAVSIG FVVNKKMEFG
IVYSCLEDKM YTGRKGKGAF CNGQKLQVSH QEDITKSLLV TELGSSRTPE TVRIILSNIE
RLLCLPIHGI RGVGTAALNM CLVAAGAADA YYEMGIHCWD VAGAGIIVTE AGGVLLDVTG
GPFDLMSRRV IASSNKTLAE RIAKEIQIIP LQRDDED
