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P97697 (IMPA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inositol monophosphatase 1

Short name=IMP 1
Short name=IMPase 1
EC=3.1.3.25
Alternative name(s):
Inositol-1(or 4)-monophosphatase 1
Lithium-sensitive myo-inositol monophosphatase A1
Gene names
Name:Impa1
Synonyms:Imp
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Can use myo-inositol monophosphates, 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.

Catalytic activity

Myo-inositol phosphate + H2O = myo-inositol + phosphate.

Cofactor

Magnesium By similarity.

Enzyme regulation

Inhibited by Li+ By similarity.

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Inositol monophosphatase 1
PRO_0000142517

Regions

Region92 – 954Substrate binding By similarity
Region194 – 1963Substrate binding By similarity

Sites

Metal binding701Magnesium 1 By similarity
Metal binding901Magnesium 1 By similarity
Metal binding901Magnesium 2 By similarity
Metal binding921Magnesium 1; via carbonyl oxygen By similarity
Metal binding931Magnesium 2 By similarity
Metal binding2201Magnesium 2 By similarity
Binding site701Substrate By similarity
Binding site2131Substrate By similarity
Binding site2201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P97697 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 01A7FFB795D2AAED

FASTA27730,511
        10         20         30         40         50         60 
MADPWQECMD YAVILARQAG EMIREALKNK MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE 

        70         80         90        100        110        120 
KYPYHSFIGE ESVASGEKTV FTEQPTWIID PIDGTTNFVH RFPFVAVSIG FVVNKEMEFG 

       130        140        150        160        170        180 
VVYSCVEDKM YTGRKGKGAF CNGQKLRVSQ QEDITKSLLV TELGSSRKPE TLRIVLSNME 

       190        200        210        220        230        240 
RLCSIPIHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD MAGAGIIVIE AGGVLLDVTG 

       250        260        270 
GPFDLMSRRI IAASNIALAE RIAKELEIIP LQRDDES 

« Hide

References

[1]"Molecular characterization of coding and untranslated regions of rat cortex lithium-sensitive myo-inositol monophosphatase cDNA."
Parthasarathy L., Parthasarathy R., Vadnal R.
Gene 191:81-87(1997) [PubMed: 9210592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]Parthasarathy L., Parthasarathy R., Vadnal R.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 157-167, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U84038 mRNA. Translation: AAB63338.2.
IPIIPI00206712.
RefSeqNP_114446.1. NM_032057.1.
UniGeneRn.3975.

3D structure databases

ProteinModelPortalP97697.
SMRP97697. Positions 3-276.
ModBaseSearch...

Protein-protein interaction databases

STRINGP97697.

Proteomic databases

PRIDEP97697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83523.
KEGGrno:83523.
UCSCNM_032057. rat.

Organism-specific databases

CTD3612.
RGD69254. Impa1.

Phylogenomic databases

GeneTreeENSGT00390000014699.
HOVERGENHBG052123.
InParanoidP97697.
OrthoDBEOG42FSJ2.
PhylomeDBP97697.

Gene expression databases

ArrayExpressP97697.
GenevestigatorP97697.
GermOnlineENSRNOG00000010482. Rattus norvegicus.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
KOK01092.
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616003.

Entry information

Entry nameIMPA1_RAT
AccessionPrimary (citable) accession number: P97697
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 1, 2004
Last modified: November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families