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P00515 (KAP2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. 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:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene names
Name:PRKAR2A
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 length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase By similarity.

Subunit structure

The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4 and CBFA2T3 By similarity. Interacts with the phosphorylated form of PJA2 By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Note: Co-localizes with PJA2 in the cytoplasm and the cell membrane By similarity.

Tissue specificity

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Post-translational modification

A second phosphorylation site has not been located.

Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 401400cAMP-dependent protein kinase type II-alpha regulatory subunit
PRO_0000205384

Regions

Nucleotide binding136 – 257122cAMP 1
Nucleotide binding258 – 401144cAMP 2
Region2 – 135134Dimerization and phosphorylation

Sites

Binding site2051cAMP 1
Binding site2141cAMP 1
Binding site3351cAMP 2
Binding site3441cAMP 2

Amino acid modifications

Modified residue21N-acetylserine
Modified residue751Phosphoserine By similarity
Modified residue771Phosphoserine By similarity
Modified residue961Phosphoserine; by PKA By similarity
Modified residue2121Phosphothreonine; by PDPK1 Ref.2

Secondary structure

1 ...................... 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00515 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 8FEA32E5B39A545A

FASTA40145,094
        10         20         30         40         50         60 
MSHIQIPPGL TELLQGYTVE VLRQRPPDLV DFAVDYFTRL REARSRASTP PAAPPSGSQD 

        70         80         90        100        110        120 
FDPGAGLVAD AVADSESEDE EDLDVPIPGR FDRRVSVCAE TYNPDEEEED TDPRVIHPKT 

       130        140        150        160        170        180 
DQQRCRLQEA CKDILLFKNL DPEQLSQVLD AMFERTVKVD EHVIDQGDDG DNFYVIERGT 

       190        200        210        220        230        240 
YDILVTKDNQ TRSVGQYDNH GSFGELALMY NTPRAATIVA TSEGSLWGLD RVTFRRIIVK 

       250        260        270        280        290        300 
NNAKKRKMFE SFIESVPLLK SLEVSERMKI VDVIGEKVYK DGERIITQGE KADSFYIIES 

       310        320        330        340        350        360 
GEVSILIKSK TKVNKDGENQ EVEIARCHKG QYFGELALVT NKPRAASAYA VGDVKCLVMD 

       370        380        390        400 
VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSSMDLIDPG Q

« Hide

References

[1]"Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle."
Takio K., Smith S.B., Krebs E.G., Walsh K.A., Titani K.
Proc. Natl. Acad. Sci. U.S.A. 79:2544-2548(1982) [PubMed: 6283532] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-401.
Tissue: Heart muscle.
[2]"Phosphorylation of RII subunit and attenuation of cAMP-dependent protein kinase activity by proline-directed protein kinase."
Braun R.K., Vulliet P.R., Carbonaro-Hall D.A., Hall F.L.
Arch. Biochem. Biophys. 289:187-191(1991) [PubMed: 1654846] [Abstract]
Cited for: PROTEIN SEQUENCE OF 155-166, PHOSPHORYLATION AT THR-212.
[3]"Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase."
Weber I.T., Steitz T.A., Bubis J., Taylor S.S.
Biochemistry 26:343-351(1987) [PubMed: 3030405] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

IPIIPI00693176.
PIROKBO2R. A00618.
RefSeqNP_001178296.1. NM_001191367.1.
XP_002697092.1. XM_002697046.1.
UniGeneBt.104132.
Bt.95129.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2APKmodel-A2-401[»]
2BPKmodel-A2-401[»]
ProteinModelPortalP00515.
SMRP00515. Positions 1-44, 93-393.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-546N.
MINTMINT-1772188.
STRINGP00515.

Proteomic databases

PRIDEP00515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205.
GeneID100139910.
KEGGbta:100139910.

Organism-specific databases

CTD5576.

Phylogenomic databases

eggNOGmaNOG15816.
GeneTreeENSGT00530000062947.
HOVERGENHBG002025.
InParanoidP00515.
OMADQQRCRL.
OrthoDBEOG4RV2RN.
PhylomeDBP00515.

Family and domain databases

InterProIPR002373. cAMP/cGMP_kin.
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
KOK04739.
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMSSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit.
SSF51206. cNMP_binding. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAP2_BOVIN
AccessionPrimary (citable) accession number: P00515
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 17, 2007
Last modified: January 25, 2012
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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