Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5R4X0 (IMPA1_PONAB)

Last modified September 22, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Inositol monophosphatase
    EC=3.1.3.25
Alternative name(s):
    Inositol-1(or 4)-monophosphatase
      Short name=IMPase
      Short name=IMP
    Lithium-sensitive myo-inositol monophosphatase A1
Gene names
Name: IMPA1
Synonyms: IMPA
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

Sequence similarities

Belongs to the inositol monophosphatase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandLithium
Magnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioninositol-1(or 4)-monophosphatase activity

Inferred from electronic annotation. Source: EC

lithium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium 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
PRO_0000142516

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

Experimental info

Sequence conflict1091I → V in CAH92554. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R4X0-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 664C1303B0801221

FASTA27730,171
        10         20         30         40         50         60 
MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE 

        70         80         90        100        110        120 
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG 

       130        140        150        160        170        180 
VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRIVLSNME 

       190        200        210        220        230        240 
KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG 

       250        260        270 
GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

CR860429 mRNA. Translation: CAH92554.1.
CR861120 mRNA. Translation: CAH93196.1.
RefSeqNP_001127563.1.
UniGenePab.18540

3D structure databases

SMRQ5R4X0. Positions 5-276.
ModBaseSearch...

Genome annotation databases

GeneID100174641.

Organism-specific databases

CTD100174641.

Phylogenomic databases

HOVERGENQ5R4X0.

Enzyme and pathway databases

BRENDA3.1.3.25. 269192.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.
ProDomPD023420. Inositol_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMPA1_PONAB
AccessionPrimary (citable) accession number: Q5R4X0
Secondary accession number(s): Q5R6Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 21, 2004
Last modified: September 22, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents