IMPA2_MOUSE
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 03-AUG-2022, entry version 147.
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 STRING; 10090.ENSMUSP00000025403; -.
DR PhosphoSitePlus; Q91UZ5; -.
DR EPD; Q91UZ5; -.
DR MaxQB; Q91UZ5; -.
DR PaxDb; Q91UZ5; -.
DR PRIDE; Q91UZ5; -.
DR ProteomicsDB; 269312; -.
DR Antibodypedia; 21936; 94 antibodies from 22 providers.
DR DNASU; 114663; -.
DR Ensembl; ENSMUST00000025403; ENSMUSP00000025403; ENSMUSG00000024525.
DR GeneID; 114663; -.
DR KEGG; mmu:114663; -.
DR UCSC; uc008fly.1; mouse.
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; VHQELEF; -.
DR OrthoDB; 915621at2759; -.
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 74 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 206 other tissues.
DR ExpressionAtlas; Q91UZ5; baseline and differential.
DR Genevisible; Q91UZ5; MM.
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:0046855; P:inositol phosphate dephosphorylation; ISO:MGI.
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 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 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
