ID A0A0A6YW07_MOUSE Unreviewed; 208 AA. AC A0A0A6YW07; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 27-NOV-2024, entry version 58. DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068}; DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068}; GN Name=Impa1 {ECO:0000313|Ensembl:ENSMUSP00000141345.2, GN ECO:0000313|MGI:MGI:1933158}; 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 {ECO:0000313|Ensembl:ENSMUSP00000141345.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000141345.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141345.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RG Mouse Genome Sequencing Consortium; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000141345.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141345.2}; RX PubMed=21750661; RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N., RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D., RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L., RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J., RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P., RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G., RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.; RT "Modernizing reference genome assemblies."; RL PLoS Biol. 9:e1001091-e1001091(2011). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000141345.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141345.2}; RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. 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:0000256|ARBA:ARBA00001033, CC ECO:0000256|RuleBase:RU364068}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRSR:PIRSR600760-2, ECO:0000256|RuleBase:RU364068}; CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol CC from D-glucose 6-phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005152, CC ECO:0000256|RuleBase:RU364068}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}. 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 RefSeq; NP_001297362.1; NM_001310433.1. DR AlphaFoldDB; A0A0A6YW07; -. DR SMR; A0A0A6YW07; -. DR Antibodypedia; 25334; 154 antibodies from 26 providers. DR DNASU; 55980; -. DR Ensembl; ENSMUST00000191670.6; ENSMUSP00000141345.2; ENSMUSG00000027531.17. DR GeneID; 55980; -. DR KEGG; mmu:55980; -. DR AGR; MGI:1933158; -. DR CTD; 3612; -. DR MGI; MGI:1933158; Impa1. DR VEuPathDB; HostDB:ENSMUSG00000027531; -. DR GeneTree; ENSGT00940000154634; -. DR HOGENOM; CLU_044118_7_2_1; -. DR OrthoDB; 3685586at2759; -. DR UniPathway; UPA00823; UER00788. DR BioGRID-ORCS; 55980; 4 hits in 82 CRISPR screens. DR ChiTaRS; Impa1; mouse. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000027531; Expressed in motor neuron and 258 other cell types or tissues. DR ExpressionAtlas; A0A0A6YW07; baseline and differential. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR CDD; cd01639; IMPase; 1. DR FunFam; 3.30.540.10:FF:000004; Inositol-1-monophosphatase; 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 PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1. DR PANTHER; PTHR20854:SF26; INOSITOL MONOPHOSPHATASE 1; 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. PE 1: Evidence at protein level; KW Hydrolase {ECO:0000256|RuleBase:RU364068}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR600760-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600760-2}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0A6YW07, KW ECO:0007829|ProteomicsDB:A0A0A6YW07}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 92 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" SQ SEQUENCE 208 AA; 23649 MW; CC3141F194F77F64 CRC64; MADPWQECMD YAVILARQAG EMIREALKNE MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE KYPCHSFIGE ESVAAGEKTV FTEQPTWVID PIDGTTNFVH RFPFVAVSIG FLVNKEMEFG IVYSCVEDKM YTGRKGKGAF CNGQKLQVSQ QEESGVLEQL LLICALWQRE EQMPIMRWES TAGTWRELAS LSPRQAECSW MSRVDRSI //