IMP2_SOLLC
ID IMP2_SOLLC Reviewed; 265 AA.
AC P54927; Q84MJ6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Inositol monophosphatase 2;
DE Short=IMP 2;
DE Short=IMPase 2;
DE Short=LeIMP2;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 2;
GN Name=IMP2; Synonyms=IMP-2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP INDUCTION BY LITHIUM, AND TISSUE SPECIFICITY.
RC STRAIN=cv. VFNT Cherry;
RX PubMed=8718627; DOI=10.2307/3870160;
RA Gillaspy G.E., Keddie J.S., Oda K., Gruissem W.;
RT "Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a
RT multigene family.";
RL Plant Cell 7:2175-2185(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP INOSITOL AND LITHIUM.
RX PubMed=14729261; DOI=10.1016/j.gene.2003.09.048;
RA Styer J.C., Keddie J., Spence J., Gillaspy G.E.;
RT "Genomic organization and regulation of the LeIMP-1 and LeIMP-2 genes
RT encoding myo-inositol monophosphatase in tomato.";
RL Gene 326:35-41(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides.
CC {ECO:0000269|PubMed:8718627}.
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:8718627};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8718627};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- TISSUE SPECIFICITY: Low expression in roots, stems, leaves, flowers and
CC young and mature green fruits. Expressed in the stem/leaf junctions,
CC below the shoot apex and on the abaxial side of the petiole of the
CC first expanded leaflets. {ECO:0000269|PubMed:14729261,
CC ECO:0000269|PubMed:8718627}.
CC -!- INDUCTION: Down-regulated by Li(+) and inositol.
CC {ECO:0000269|PubMed:14729261, ECO:0000269|PubMed:8718627}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U39443; AAB19029.1; -; mRNA.
DR EMBL; AY227667; AAP15455.1; -; Genomic_DNA.
DR EMBL; AEKE02011759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T07800; T07800.
DR RefSeq; NP_001233843.1; NM_001246914.1.
DR AlphaFoldDB; P54927; -.
DR SMR; P54927; -.
DR STRING; 4081.Solyc03g044890.1.1; -.
DR PaxDb; P54927; -.
DR PRIDE; P54927; -.
DR EnsemblPlants; Solyc03g044890.1.1; Solyc03g044890.1.1.1; Solyc03g044890.1.
DR GeneID; 544014; -.
DR Gramene; Solyc03g044890.1.1; Solyc03g044890.1.1.1; Solyc03g044890.1.
DR KEGG; sly:544014; -.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_1_0_1; -.
DR InParanoid; P54927; -.
DR OMA; HAWDCLA; -.
DR OrthoDB; 915621at2759; -.
DR PhylomeDB; P54927; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000004994; Chromosome 3.
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:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006021; P:inositol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
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 Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..265
FT /note="Inositol monophosphatase 2"
FT /id="PRO_0000142524"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 6..7
FT /note="DV -> EC (in Ref. 2; AAP15455)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="L -> S (in Ref. 2; AAP15455)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="DV -> EC (in Ref. 2; AAP15455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 28705 MW; 5369735F30FC884B CRC64;
MEEFVDVAIE AAKKAGEIIR HGFYKSKHIE HKGVVDLVTE TDKACEVLIF NHLKQCFPSH
KFIGEETTAA ASGNFELTDE PTWIVDPLDG TTNFVHGFPF VCVSIGLTIE KKPVVGVVYN
PIIDELFTAI YGRGAFLNGK SIRVSSESQL VKALVATEVG TNRDKAIVDA TTGRINRVIF
KVRSLRMSGS CALNLCGVAC GRLDLFYEIE FGGPWDVAAG ALIVIEAGGL VLDPSGSEFD
LTARRVAATN AHLKDAFINA LNESE
