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P20456 (IMPA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:IMPA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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.

Enzyme regulation

Inhibited by Li+.

Pathway

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the inositol monophosphatase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandLithium
Magnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioninositol monophosphate 1-phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Inositol monophosphatase 1
PRO_0000142512

Regions

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

Sites

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

Secondary structure

1 ............................................. 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20456 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 773DDB0291AC5977

FASTA27730,056
        10         20         30         40         50         60 
MADPWQECMD YAVTLAGQAG EVVREALKNE MNIMVKSSPA DLVTATDQKV EKMLITSIKE 

        70         80         90        100        110        120 
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH GFPFVAVSIG FVVNKKMEFG 

       130        140        150        160        170        180 
IVYSCLEDKM YTGRKGKGAF CNGQKLQVSH QEDITKSLLV TELGSSRTPE TVRIILSNIE 

       190        200        210        220        230        240 
RLLCLPIHGI RGVGTAALNM CLVAAGAADA YYEMGIHCWD VAGAGIIVTE AGGVLLDVTG 

       250        260        270 
GPFDLMSRRV IASSNKTLAE RIAKEIQIIP LQRDDED

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of bovine brain inositol monophosphatase."
Diehl R.E., Whiting P., Potter J., Gee N., Ragan C.I., Linemeyer D., Schoepfer R., Bennett C., Dixon R.A.F.
J. Biol. Chem. 265:5946-5949(1990) [PubMed: 1690719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons.
[3]"High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy."
Gill R., Mohammed F., Badyal R., Coates L., Erskine P., Thompson D., Cooper J., Gore M., Wood S.
Acta Crystallogr. D 61:545-555(2005) [PubMed: 15858264] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05394 mRNA. Translation: AAA30589.1.
BC118411 mRNA. Translation: AAI18412.1.
IPIIPI00692819.
PIRA35223.
RefSeqNP_776786.1. NM_174361.3.
UniGeneBt.424.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJIX-ray1.30A/B1-277[»]
ProteinModelPortalP20456.
SMRP20456. Positions 3-276.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20456.

Proteomic databases

PRIDEP20456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000015548; ENSBTAP00000015548; ENSBTAG00000011709.
GeneID281865.
KEGGbta:281865.

Organism-specific databases

CTD3612.

Phylogenomic databases

eggNOGmaNOG06324.
GeneTreeENSGT00390000014699.
HOVERGENHBG052123.
InParanoidP20456.
OMAATDQKIE.
OrthoDBEOG42FSJ2.
PhylomeDBP20456.

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...

Entry information

Entry nameIMPA1_BOVIN
AccessionPrimary (citable) accession number: P20456
Secondary accession number(s): Q17QE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 101 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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