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Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1)

 IMPA1_RAT               Reviewed;         277 AA.
P97697;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
25-OCT-2017, entry version 138.
RecName: Full=Inositol monophosphatase 1;
Short=IMP 1;
Short=IMPase 1;
EC=3.1.3.25 {ECO:0000269|PubMed:9462881};
AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000303|PubMed:9462881};
EC=3.1.3.94 {ECO:0000269|PubMed:9462881};
AltName: Full=Inositol-1(or 4)-monophosphatase 1;
AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
Name=Impa1; Synonyms=Imp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9210592; DOI=10.1016/S0378-1119(97)00045-0;
Parthasarathy L., Parthasarathy R., Vadnal R.;
"Molecular characterization of coding and untranslated regions of rat
cortex lithium-sensitive myo-inositol monophosphatase cDNA.";
Gene 191:81-87(1997).
[2]
SEQUENCE REVISION.
Parthasarathy L., Parthasarathy R., Vadnal R.;
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 157-167, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
TISSUE SPECIFICITY.
PubMed=1377913; DOI=10.1042/bj2840749;
McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R.,
Bailey F.J., Maigetter R., Ragan C.I.;
"cDNA cloning of human and rat brain myo-inositol monophosphatase.
Expression and characterization of the human recombinant enzyme.";
Biochem. J. 284:749-754(1992).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
SUBUNIT.
PubMed=9462881; DOI=10.1016/S0006-8993(97)01042-1;
Parthasarathy R., Parthasarathy L., Vadnal R.;
"Brain inositol monophosphatase identified as a galactose 1-
phosphatase.";
Brain Res. 778:99-106(1997).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Responsible for the provision of inositol required for
synthesis of phosphatidylinositol and polyphosphoinositides and
has been implicated as the pharmacological target for lithium
action in brain. Has broad substrate specificity and can use myo-
inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-
inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate,
fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as
substrates (By similarity). Is equally active with myo-inositol
monophosphate and D-galactose 1-phosphate.
{ECO:0000250|UniProtKB:P29218, ECO:0000269|PubMed:9462881}.
-!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
+ phosphate. {ECO:0000269|PubMed:9462881}.
-!- CATALYTIC ACTIVITY: Alpha-D-galactose 1-phosphate + H(2)O = D-
galactose + phosphate. {ECO:0000269|PubMed:9462881}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9462881};
-!- ENZYME REGULATION: Activity with myo-inositol monophosphate and D-
galactose 1-phosphate is inhibited by Li(+), Ca(2+) and Mn(2+),
but also by Mg(2+) at concentrations above 3 mM.
{ECO:0000269|PubMed:9462881}.
-!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
inositol from D-glucose 6-phosphate: step 2/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9462881}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1377913}.
-!- SIMILARITY: Belongs to the inositol monophosphatase family.
{ECO:0000305}.
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EMBL; U84038; AAB63338.2; -; mRNA.
RefSeq; NP_114446.1; NM_032057.1.
UniGene; Rn.3975; -.
ProteinModelPortal; P97697; -.
SMR; P97697; -.
BioGrid; 249742; 1.
MINT; MINT-1511588; -.
STRING; 10116.ENSRNOP00000014274; -.
ChEMBL; CHEMBL1293238; -.
iPTMnet; P97697; -.
PhosphoSitePlus; P97697; -.
SwissPalm; P97697; -.
PaxDb; P97697; -.
PRIDE; P97697; -.
GeneID; 83523; -.
KEGG; rno:83523; -.
UCSC; RGD:69254; rat.
CTD; 3612; -.
RGD; 69254; Impa1.
eggNOG; KOG2951; Eukaryota.
eggNOG; COG0483; LUCA.
HOGENOM; HOG000282238; -.
HOVERGEN; HBG052123; -.
InParanoid; P97697; -.
KO; K01092; -.
PhylomeDB; P97697; -.
BRENDA; 3.1.3.25; 5301.
SABIO-RK; P97697; -.
UniPathway; UPA00823; UER00788.
PRO; PR:P97697; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:RGD.
GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052834; F:inositol monophosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0031403; F:lithium ion binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:RGD.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
CDD; cd01639; IMPase; 1.
InterPro; IPR033942; IMPase.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR020552; Inositol_monoPase_Li-sen.
InterPro; IPR000760; Inositol_monophosphatase-like.
InterPro; IPR020550; Inositol_monophosphatase_CS.
PANTHER; PTHR20854; PTHR20854; 1.
Pfam; PF00459; Inositol_P; 1.
PRINTS; PR00377; IMPHPHTASES.
PRINTS; PR00378; LIIMPHPHTASE.
PROSITE; PS00629; IMP_1; 1.
PROSITE; PS00630; IMP_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
Lithium; Magnesium; Metal-binding; Reference proteome.
CHAIN 1 277 Inositol monophosphatase 1.
/FTId=PRO_0000142517.
REGION 92 95 Substrate binding.
{ECO:0000250|UniProtKB:P29218}.
REGION 194 196 Substrate binding.
{ECO:0000250|UniProtKB:P29218}.
METAL 70 70 Magnesium 1; catalytic.
{ECO:0000250|UniProtKB:P29218}.
METAL 90 90 Magnesium 1; catalytic.
{ECO:0000250|UniProtKB:P29218}.
METAL 90 90 Magnesium 2.
{ECO:0000250|UniProtKB:P29218}.
METAL 92 92 Magnesium 1; via carbonyl oxygen;
catalytic.
{ECO:0000250|UniProtKB:P29218}.
METAL 93 93 Magnesium 2.
{ECO:0000250|UniProtKB:P29218}.
METAL 220 220 Magnesium 2.
{ECO:0000250|UniProtKB:P29218}.
BINDING 70 70 Substrate.
{ECO:0000250|UniProtKB:P29218}.
BINDING 213 213 Substrate.
{ECO:0000250|UniProtKB:P29218}.
BINDING 220 220 Substrate.
{ECO:0000250|UniProtKB:P29218}.
SEQUENCE 277 AA; 30511 MW; 01A7FFB795D2AAED CRC64;
MADPWQECMD YAVILARQAG EMIREALKNK MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE
KYPYHSFIGE ESVASGEKTV FTEQPTWIID PIDGTTNFVH RFPFVAVSIG FVVNKEMEFG
VVYSCVEDKM YTGRKGKGAF CNGQKLRVSQ QEDITKSLLV TELGSSRKPE TLRIVLSNME
RLCSIPIHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD MAGAGIIVIE AGGVLLDVTG
GPFDLMSRRI IAASNIALAE RIAKELEIIP LQRDDES


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