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Reviewed, UniProtKB/Swiss-Prot P17105 (IP3KA_RAT)

Last modified November 3, 2009. Version 70. 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

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Names and origin

Protein namesRecommended name:
    Inositol-trisphosphate 3-kinase A
    EC=2.7.1.127
Alternative name(s):
    Inositol 1,4,5-trisphosphate 3-kinase A
    IP3 3-kinase A
      Short name=IP3K A
Gene names
Name: Itpka
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.

Enzyme regulation

IP3K is activated by calmodulin.

Sequence similarities

Belongs to the inositol phosphokinase (IPK) family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Inositol-trisphosphate 3-kinase A
PRO_0000066867

Regions

Nucleotide binding247 – 2493ATP
Region285 – 2939Calmodulin-binding
Region310 – 3178Substrate binding By similarity

Sites

Binding site1951ATP By similarity
Binding site2071ATP
Binding site2601ATP
Binding site2621Substrate By similarity
Binding site2831Substrate By similarity
Binding site3341ATP By similarity
Binding site4141ATP
Binding site4171Substrate By similarity

Secondary structure

1 ......................................... 459
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P17105-1 [UniParc].

Last modified November 1, 1991. Version 3.
Checksum: 8093DADC0FADC290

FASTA45950,871
        10         20         30         40         50         60 
MTLPGHPTGM ARPRGAGPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA AGEPRARGAK 

        70         80         90        100        110        120 
RRGGQVPNGL PRAAPAPVIP QLTVTSEEDV APASPGPPDR EGNWLPAAGS HLQQPRRLST 

       130        140        150        160        170        180 
SSLSSTGSSS LLEDSEDDLL SDSESRSRGN VQLETSEDVG QKSHWQKIRT MVNLPVMSPF 

       190        200        210        220        230        240 
KKRYSWVQLA GHTGSFKAAG TSGLILKRSS EPEHYCLVRL MADVLRGCVP AFHGVVERDG 

       250        260        270        280        290        300 
ESYLQLQDLL DGFDGPCVLD CKMGVRTYLE EELTKARERP KLRKDMYKKM LAVDPEAPTE 

       310        320        330        340        350        360 
EEHAQRAVTK PRYMQWREGI SSSTTLGFRI EGIKKADGSC STDFKTTRSR EQVTRVFEEF 

       370        380        390        400        410        420 
MQGDAEVLKR YLNRLQQIRD TLEISDFFRR HEVIGSSLLF VHDHCHRAGV WLIDFGKTTP 

       430        440        450 
LPDGQILDHR RPWEEGNRED GYLLGLDNLI GILANLAER

« Hide

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References

[1]"Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase."
Takazawa K., Vandekerckhove J., Dumont J.E., Erneux C.
Biochem. J. 272:107-112(1990) [PubMed: 2176078] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase."
Choi K.Y., Kim H.K., Lee S.Y., Moon K.H., Sim S.S., Kim J.W., Chung H.K., Rhee S.G.
Science 248:64-66(1990) [PubMed: 2157285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[3]"Active site labelling of inositol 1,4,5-trisphosphate 3-kinase A by phenylglyoxal."
Communi D., Lecocq R., Vanweyenberg V., Erneux C.
Biochem. J. 310:109-115(1995) [PubMed: 7646431] [Abstract]
Cited for: PROTEIN SEQUENCE OF 315-326, ACTIVE SITE.
[4]"Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase."
Miller G.J., Hurley J.H.
Mol. Cell 15:703-711(2004) [PubMed: 15350215] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 185-459 IN COMPLEX WITH ADP.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X56917 mRNA. Translation: CAA40248.1.
M29787 mRNA. Translation: AAA41457.1. Different initiation.
IPIIPI00213554.
PIRS13064.
RefSeqNP_112307.1.
UniGeneRn.9877

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TZDX-ray2.20A/B185-459[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP17105.

PTM databases

PhosphoSiteP17105.

Genome annotation databases

EnsemblENSRNOT00000007247; ENSRNOP00000007247; ENSRNOG00000005284; Rattus norvegicus. [Genome view]
GeneID81677.
KEGGrno:81677.
UCSCM29787. rat.

Organism-specific databases

CTD81677.
RGD619950. Itpka.

Phylogenomic databases

HOVERGENP17105.
OMAYSWVQLA.

Enzyme and pathway databases

BRENDA2.7.1.127. 248.

Gene expression databases

ArrayExpressP17105.
GenevestigatorP17105.
GermOnlineENSRNOG00000005284. Rattus norvegicus.

Family and domain databases

InterProIPR005522. IPK.
[Graphical view]
PANTHERPTHR12400. IPK. 1 hit.
PfamPF03770. IPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615284.

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Entry information

Entry nameIP3KA_RAT
AccessionPrimary (citable) accession number: P17105
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: November 3, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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