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Database: UniProt
Entry: P38710
LinkDB: P38710
Original site: P38710 
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   26-NOV-2014, entry version 115.
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;
OC   Saccharomycetes; 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.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, ENZYME 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
RT   inositol 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.,
RA   Dephoure N., 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}.
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ENZYME 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
CC         {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-
CC       inositol from D-glucose 6-phosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2440 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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   ProteinModelPortal; P38710; -.
DR   SMR; P38710; 4-285.
DR   BioGrid; 36478; 32.
DR   DIP; DIP-6506N; -.
DR   MINT; MINT-2734649; -.
DR   STRING; 4932.YHR046C; -.
DR   MaxQB; P38710; -.
DR   PaxDb; P38710; -.
DR   PeptideAtlas; P38710; -.
DR   EnsemblFungi; YHR046C; YHR046C; YHR046C.
DR   GeneID; 856442; -.
DR   KEGG; sce:YHR046C; -.
DR   CYGD; YHR046c; -.
DR   SGD; S000001088; INM1.
DR   eggNOG; COG0483; -.
DR   GeneTree; ENSGT00390000014699; -.
DR   HOGENOM; HOG000282238; -.
DR   InParanoid; P38710; -.
DR   KO; K01092; -.
DR   OMA; WCISLAR; -.
DR   OrthoDB; EOG7RBZKG; -.
DR   BioCyc; YEAST:YHR046C-MONOMER; -.
DR   Reactome; REACT_188936; Synthesis of IP2, IP, and Ins in the cytosol.
DR   UniPathway; UPA00823; UER00788.
DR   NextBio; 982054; -.
DR   Genevestigator; P38710; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR20854; PTHR20854; 1.
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   Complete proteome; Cytoplasm; Hydrolase; Lithium; Magnesium;
KW   Metal-binding; Nucleus; Reference proteome.
FT   CHAIN         1    295       Inositol monophosphatase 1.
FT                                /FTId=PRO_0000142585.
FT   REGION       94     97       Substrate binding. {ECO:0000250}.
FT   METAL        73     73       Magnesium 1. {ECO:0000250}.
FT   METAL        92     92       Magnesium 1. {ECO:0000250}.
FT   METAL        92     92       Magnesium 2. {ECO:0000250}.
FT   METAL        94     94       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        95     95       Magnesium 2. {ECO:0000250}.
FT   METAL       231    231       Magnesium 2. {ECO:0000250}.
FT   BINDING      73     73       Substrate. {ECO:0000250}.
FT   BINDING     231    231       Substrate. {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
//
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