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P61926 (IPKA_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase inhibitor alpha

Short name=PKI-alpha
Alternative name(s):
cAMP-dependent protein kinase inhibitor, muscle/brain isoform
Gene names
Name:PKIA
Synonyms:PRKACN1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length76 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.

Miscellaneous

The inhibitory site contains regions very similar to the hinge regions (sites that directly interact with the enzyme active site) and "pseudosubstrate site" of the regulatory chains; but, unlike these chains, PKI does not contain cAMP-binding sites. The arginine residues within the inhibitory site are essential for inhibition and recognition of the enzyme active site.

Sequence similarities

Belongs to the PKI family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 7675cAMP-dependent protein kinase inhibitor alpha
PRO_0000154535

Sites

Site161Important for inhibition
Site191Important for inhibition
Site201Important for inhibition

Amino acid modifications

Modified residue21Blocked amino end (Thr)
Modified residue21N-acetylthreonine By similarity

Secondary structure

..... 76
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61926 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BDCE072810435951

FASTA767,989
        10         20         30         40         50         60 
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRSS 

        70 
TEQSGEAQGE AAKSES 

« Hide

References

[1]"Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle."
Scott J.D., Fischer E.H., Takio K., Demaille J.G., Krebs E.G.
Proc. Natl. Acad. Sci. U.S.A. 82:5732-5736(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-76.
Tissue: Skeletal muscle.
[2]"Identification of an inhibitory region of the heat-stable protein inhibitor of the cAMP-dependent protein kinase."
Scott J.D., Fischer E.H., Demaille J.G., Krebs E.G.
Proc. Natl. Acad. Sci. U.S.A. 82:4379-4383(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITORY SITE.
[3]"Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase."
Knighton D.R., Zheng J., ten Eyck L.F., Xuong N.-H., Taylor S.S., Sowadski J.M.
Science 253:414-420(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 6-25 IN COMPLEX WITH PRKACA.
[4]"Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine."
Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.
Biochemistry 36:4438-4448(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-25 IN COMPLEX WITH PRKACA.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIROKRBCI. A01340.
RefSeqXP_002710694.1. XM_002710648.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDKX-ray2.00I/J6-25[»]
1CTPX-ray2.90I6-25[»]
1FMOX-ray2.20I6-25[»]
1JBPX-ray2.20S6-25[»]
1Q8WX-ray2.20B6-25[»]
1SMHX-ray2.04B6-25[»]
1STCX-ray2.30I6-25[»]
1SVEX-ray2.49B6-25[»]
1SVGX-ray2.02B6-25[»]
2ERZX-ray2.20I6-25[»]
2F7ZX-ray3.00I6-25[»]
2GFCX-ray1.87I6-25[»]
2GNHX-ray2.05I6-25[»]
2GNLX-ray2.60I6-25[»]
3DNDX-ray2.26I6-25[»]
3DNEX-ray2.00I6-25[»]
DisProtDP00015.
ProteinModelPortalP61926.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP61926.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100343293.

Phylogenomic databases

eggNOGNOG45574.
HOGENOMHOG000059641.
HOVERGENHBG101093.
OMAEGDAQRN.
OrthoDBEOG7JHM8S.
TreeFamTF330809.

Family and domain databases

InterProIPR004171. cAMP_dep_PKI.
[Graphical view]
PfamPF02827. PKI. 1 hit.
[Graphical view]
PIRSFPIRSF001667. PKI. 1 hit.
ProDomPD010366. cAMP_dep_PKI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP61926.
NextBio21582.

Entry information

Entry nameIPKA_RABIT
AccessionPrimary (citable) accession number: P61926
Secondary accession number(s): P04541
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references