IMPA2_RAT
ID IMPA2_RAT Reviewed; 290 AA.
AC Q8CIN7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Inositol monophosphatase 2;
DE Short=IMP 2;
DE Short=IMPase 2;
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:O14732};
DE AltName: Full=Inositol-1(or 4)-monophosphatase 2;
DE AltName: Full=Myo-inositol monophosphatase A2;
GN Name=Impa2;
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;
RA Parthasarathy L., Seelan R., Parthasarathy R.;
RT "Molecular cloning and sequencing of rat Impa2.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Can use myo-inositol monophosphates, scylloinositol 1,4-
CC diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as
CC substrates. Has been implicated as the pharmacological target for
CC lithium Li(+) action in brain (By similarity).
CC {ECO:0000250|UniProtKB:O14732}.
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:O14732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O14732};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O14732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14732}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY160191; AAN47010.1; -; mRNA.
DR EMBL; BC083544; AAH83544.1; -; mRNA.
DR RefSeq; NP_757378.1; NM_172224.1.
DR AlphaFoldDB; Q8CIN7; -.
DR SMR; Q8CIN7; -.
DR STRING; 10116.ENSRNOP00000025147; -.
DR PaxDb; Q8CIN7; -.
DR PRIDE; Q8CIN7; -.
DR GeneID; 282636; -.
DR KEGG; rno:282636; -.
DR UCSC; RGD:628692; rat.
DR CTD; 3613; -.
DR RGD; 628692; Impa2.
DR VEuPathDB; HostDB:ENSRNOG00000018516; -.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_1_0_1; -.
DR InParanoid; Q8CIN7; -.
DR OMA; VHQELEF; -.
DR OrthoDB; 915621at2759; -.
DR PhylomeDB; Q8CIN7; -.
DR TreeFam; TF313194; -.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q8CIN7; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018516; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; Q8CIN7; baseline and differential.
DR Genevisible; Q8CIN7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; ISO: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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0010226; P:response to lithium ion; ISO:RGD.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..290
FT /note="Inositol monophosphatase 2"
FT /id="PRO_0000142522"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 105..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 31796 MW; 6DF985B2BD99F266 CRC64;
MKPNSEEEEE LVQGVGPWDE CFEVAVQLAL RAGQIIRKAL TEEKHVSTKT SAADLVTETD
HRVEDLIVSE LRKRFPSHRF IAEEATASGA KCVLTHSPTW IIDPIDGTCN FVHRFPTVAV
SIGFAVHQEL EFGVIHHCTE ERLYTGRRGQ GAFCNGQRLQ VSRETDLAKA LVLTEIGPKR
DPDTLKVFLS NMERLLHAKA HGVRVIGSST LALCYLASGA ADAYYQFGLH CWDLAAATVI
IREAGGIVID TSGGPLDLMS CRVVAAGTRE MAVLIAQALQ TINYGRDDEK
