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P12368 (KAP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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 type II-alpha regulatory subunit
Gene names
Name:Prkar2a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

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. Interacts with MYRIP; his interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release. Ref.4

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Note: Colocalizes 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

Phosphorylated by the activated catalytic chain.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein heterooligomerization

Inferred from direct assay PubMed 17081990. Source: RGD

regulation of protein kinase activity

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

response to clozapine

Inferred from expression pattern PubMed 11907174. Source: RGD

   Cellular_componentT-tubule

Inferred from direct assay PubMed 14569017. Source: RGD

cAMP-dependent protein kinase complex

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

cytoplasm

Inferred from direct assay PubMed 18550536. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 18550536. Source: RGD

protein complex

Inferred from direct assay PubMed 17081990. Source: RGD

   Molecular_functioncAMP binding

Inferred from direct assay PubMed 11907174. Source: RGD

cAMP-dependent protein kinase regulator activity

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

protein binding

Inferred from physical interaction PubMed 21177871. Source: RGD

protein domain specific binding

Inferred from mutant phenotype PubMed 16306226. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 17081990. Source: RGD

protein kinase A catalytic subunit binding

Inferred by curator PubMed 16816331. Source: RGD

small molecule binding

Inferred from direct assay PubMed 21177871. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 401400cAMP-dependent protein kinase type II-alpha regulatory subunit
PRO_0000205388

Regions

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

Sites

Binding site2051cAMP 1 By similarity
Binding site2141cAMP 1 By similarity
Binding site3351cAMP 2 By similarity
Binding site3441cAMP 2 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue481Phosphoserine By similarity
Modified residue751Phosphoserine By similarity
Modified residue771Phosphoserine By similarity
Modified residue971Phosphoserine Ref.3
Modified residue2121Phosphothreonine; by PDPK1 By similarity

Experimental info

Sequence conflict741E → Q in AAA41856. Ref.2
Sequence conflict901S → A in AAA41856. Ref.2
Sequence conflict1251Y → C in AAA41856. Ref.2
Sequence conflict154 – 1552EK → KR in AAA41856. Ref.2
Sequence conflict1981D → A in AAA41856. Ref.2

Secondary structure

..... 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12368 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 026FEBFCFACA9C7D

FASTA40145,540
        10         20         30         40         50         60 
MSHIQIPPGL TELLQGYTVE VLRQQPPDLV DFAVEYFTRL REARRQESDS FIAPPTTFHA 

        70         80         90        100        110        120 
QESSGVPVIE EDGESESDSD DEDLEVPIPS KFTRRVSVCA ETFNPDEEED NDPRVVHPKT 

       130        140        150        160        170        180 
DEQRYRLQEA CKDILLFKNL DQEQLSQVLD AMFEKIVKTD EHVIDQGDDG DNFYVIERGT 

       190        200        210        220        230        240 
YDILVTKDNQ TRSVGQYDNR GSFGELALMY NTPRAATIVA TSDGSLWGLD RVTFRRIIVK 

       250        260        270        280        290        300 
NNAKKRKMFE SFIESVPLFK SLEMSERMKI VDVIGEKIYK DGERIITQGE KADSFYIIES 

       310        320        330        340        350        360 
GEVSILIRSK TKTNKNGGNQ EVEIAHCHKG QYFGELALVT NKPRAASAYA VGDVKCLVMD 

       370        380        390        400 
VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSNLDLLDPG Q 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence and complete coding region of cAMP-dependent protein kinase type II regulatory subunit from a rat testicular germ cell cDNA library."
Ziemba A.J., Collard M.W.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain."
Scott J.D., Glaccum M.B., Zoller M.J., Uhler M.D., Helfman D.M., McKnight G.S., Krebs E.G.
Proc. Natl. Acad. Sci. U.S.A. 84:5192-5196(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-401.
Tissue: Skeletal muscle.
[3]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"MyRIP anchors protein kinase A to the exocyst complex."
Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.
J. Biol. Chem. 282:33155-33167(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYRIP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF533978 mRNA. Translation: AAM97689.1.
J02934 mRNA. Translation: AAA41856.1.
PIROKRT2R. A28325.
RefSeqNP_062137.1. NM_019264.2.
UniGeneRn.9742.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-A/B1-45[»]
2H9RNMR-A/B1-45[»]
2HWNX-ray1.60A/B/C/D1-45[»]
3TMHX-ray3.80B/C/F/G1-45[»]
ProteinModelPortalP12368.
SMRP12368. Positions 1-45, 93-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-555N.
IntActP12368. 4 interactions.
MINTMINT-4564663.
STRING10116.ENSRNOP00000027552.

PTM databases

PhosphoSiteP12368.

Proteomic databases

PaxDbP12368.
PRIDEP12368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29699.
KEGGrno:29699.
UCSCRGD:3393. rat.

Organism-specific databases

CTD5576.
RGD3393. Prkar2a.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000196668.
HOVERGENHBG002025.
InParanoidP12368.
KOK04739.
PhylomeDBP12368.

Enzyme and pathway databases

ReactomeREACT_205051. Metabolism.

Gene expression databases

GenevestigatorP12368.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
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]
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. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12368.
NextBio610099.
PROP12368.

Entry information

Entry nameKAP2_RAT
AccessionPrimary (citable) accession number: P12368
Secondary accession number(s): Q8K1M2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 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