ID IMPA2_MOUSE Reviewed; 290 AA. AC Q91UZ5; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 156. 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 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 STRAIN=129/J; RX PubMed=11418250; DOI=10.1016/s0378-1119(01)00502-9; RA Shamir A., Sjoeholt G., Ebstein R.P., Agam G., Steen V.M.; RT "Characterization of two genes, Impa1 and Impa2 encoding mouse myo-inositol RT monophosphatases."; RL Gene 271:285-291(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; 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). 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, and Spleen; 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). 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 -!- TISSUE SPECIFICITY: Mostly expressed in brain, small intestine, heart, CC kidney, and spleen (at protein level). {ECO:0000269|PubMed:17068342}. 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; AF353730; AAK39516.1; -; mRNA. DR EMBL; BC011093; AAH11093.1; -; mRNA. DR CCDS; CCDS29320.1; -. DR RefSeq; NP_444491.1; NM_053261.2. DR AlphaFoldDB; Q91UZ5; -. DR SMR; Q91UZ5; -. DR BioGRID; 227793; 1. DR STRING; 10090.ENSMUSP00000025403; -. DR PhosphoSitePlus; Q91UZ5; -. DR EPD; Q91UZ5; -. DR MaxQB; Q91UZ5; -. DR PaxDb; 10090-ENSMUSP00000025403; -. DR ProteomicsDB; 269312; -. DR Pumba; Q91UZ5; -. DR Antibodypedia; 21936; 101 antibodies from 22 providers. DR DNASU; 114663; -. DR Ensembl; ENSMUST00000025403.8; ENSMUSP00000025403.7; ENSMUSG00000024525.8. DR GeneID; 114663; -. DR KEGG; mmu:114663; -. DR UCSC; uc008fly.1; mouse. DR AGR; MGI:2149728; -. DR CTD; 3613; -. DR MGI; MGI:2149728; Impa2. DR VEuPathDB; HostDB:ENSMUSG00000024525; -. DR eggNOG; KOG2951; Eukaryota. DR GeneTree; ENSGT00940000160536; -. DR HOGENOM; CLU_044118_1_0_1; -. DR InParanoid; Q91UZ5; -. DR OMA; DKSHTWI; -. DR OrthoDB; 3685586at2759; -. DR PhylomeDB; Q91UZ5; -. DR TreeFam; TF313194; -. 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 BioGRID-ORCS; 114663; 5 hits in 79 CRISPR screens. DR ChiTaRS; Impa2; mouse. DR PRO; PR:Q91UZ5; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; Q91UZ5; Protein. DR Bgee; ENSMUSG00000024525; Expressed in granulocyte and 209 other cell types or tissues. DR ExpressionAtlas; Q91UZ5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0010226; P:response to lithium ion; ISO:MGI. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. 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:SF29; INOSITOL MONOPHOSPHATASE 2; 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. DR Genevisible; Q91UZ5; MM. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1..290 FT /note="Inositol monophosphatase 2" FT /id="PRO_0000142521" 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; 31716 MW; F27FDC7EB1D5A436 CRC64; MKPSSEEEGE LVQGVGPWDE CFEVAVQLAL RAGQIIRKAL TEEKRVSTKT SAADLVTETD HRVEDLIVSE LRKRFPSHRF IAEEATASGA KCVLTHSPTW IIDPIDGTCN FVHRFPTVAV SIGFAVHQEL EFGVIHHCTE ERLYTGRRGQ GAFCNGQRLQ VSRETDLAKA LVLTEIGPKR DPDTLKVFLS NMERLLHAKA HGVRVIGSST LALCYLASGA ADAYYQFGLH CWDLAAATVI IREAGGIVID TSGGPLDLMS CRVVAAGTRE MAVLIAQALQ TINYGRDDEK //