INM1_YEAST
ID INM1_YEAST Reviewed; 295 AA.
AC P38710; D3DKZ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inositol monophosphatase 1;
DE Short=IMP 1;
DE Short=IMPase 1;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 1;
GN Name=INM1; Synonyms=IMP1; OrderedLocusNames=YHR046C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10096091; DOI=10.1046/j.1365-2958.1999.01267.x;
RA Lopez F., Leube M., Gil-Mascarell R., Navarro-Avino J.P., Serrano R.;
RT "The yeast inositol monophosphatase is a lithium- and sodium-sensitive
RT enzyme encoded by a non-essential gene pair.";
RL Mol. Microbiol. 31:1255-1264(1999).
RN [4]
RP FUNCTION.
RX PubMed=12593845; DOI=10.1016/s0006-291x(03)00051-2;
RA Navarro-Avino J.P., Belles J.M., Serrano R.;
RT "Yeast inositol mono- and trisphosphate levels are modulated by inositol
RT monophosphatase activity and nutrients.";
RL Biochem. Biophys. Res. Commun. 302:41-45(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides.
CC {ECO:0000250, ECO:0000269|PubMed:10096091,
CC ECO:0000269|PubMed:12593845}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) and Na(+).
CC {ECO:0000269|PubMed:10096091}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for inositol 1-phosphate {ECO:0000269|PubMed:10096091};
CC Vmax=20 umol/min/mg enzyme for inositol 1-phosphate
CC {ECO:0000269|PubMed:10096091};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U00062; AAB68918.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06738.1; -; Genomic_DNA.
DR PIR; S46749; S46749.
DR RefSeq; NP_011912.1; NM_001179176.1.
DR AlphaFoldDB; P38710; -.
DR SMR; P38710; -.
DR BioGRID; 36478; 134.
DR DIP; DIP-6506N; -.
DR IntAct; P38710; 1.
DR MINT; P38710; -.
DR STRING; 4932.YHR046C; -.
DR MaxQB; P38710; -.
DR PaxDb; P38710; -.
DR PRIDE; P38710; -.
DR EnsemblFungi; YHR046C_mRNA; YHR046C; YHR046C.
DR GeneID; 856442; -.
DR KEGG; sce:YHR046C; -.
DR SGD; S000001088; INM1.
DR VEuPathDB; FungiDB:YHR046C; -.
DR eggNOG; KOG2951; Eukaryota.
DR GeneTree; ENSGT00940000169763; -.
DR HOGENOM; CLU_044118_1_2_1; -.
DR InParanoid; P38710; -.
DR OMA; FSCVEDK; -.
DR BioCyc; YEAST:YHR046C-MON; -.
DR Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; P38710; -.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:P38710; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38710; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:SGD.
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:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
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; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
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; Nucleus;
KW Reference proteome.
FT CHAIN 1..295
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142585"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 295 AA; 32823 MW; 1DF052114912C6CB CRC64;
MTIDLASIEK FLCELATEKV GPIIKSKSGT QKDYDLKTGS RSVDIVTAID KQVEKLIWES
VKTQYPTFKF IGEESYVKGE TVITDDPTFI IDPIDGTTNF VHDFPFSCTS LGLTVNKEPV
VGVIYNPHIN LLVSASKGNG MRVNNKDYDY KSKLESMGSL ILNKSVVALQ PGSAREGKNF
QTKMATYEKL LSCDYGFVHG FRNLGSSAMT MAYIAMGYLD SYWDGGCYSW DVCAGWCILK
EVGGRVVGAN PGEWSIDVDN RTYLAVRGTI NNESDEQTKY ITDFWNCVDG HLKYD
