cAMP-dependent protein kinase type II-alpha regulatory subunit

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Reviewed, UniProtKB/Swiss-Prot P00515 (KAP2_BOVIN)

Last modified November 3, 2009. Version 90. History...

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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 names

Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene names

Name:

PRKAR2A

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
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 PDPK 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.

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Ontologies

Keywords
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 401

400

cAMP-dependent protein kinase type II-alpha regulatory subunit

PRO_0000205384

Regions

Nucleotide binding

136 – 257

122

cAMP 1

Nucleotide binding

258 – 401

144

cAMP 2

Region

2 – 135

134

Dimerization and phosphorylation

Sites

Binding site

205

cAMP 1

Binding site

214

cAMP 1

Binding site

335

cAMP 2

Binding site

344

cAMP 2

Amino acid modifications

Modified residue

N-acetylserine

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by PKA By similarity

Modified residue

212

Phosphothreonine; by PDPK Ref.2

Secondary structure

401

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00515-1 [UniParc].

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

401

45,094

        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

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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.

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Cross-references

Sequence databases

IPI

IPI00693176.

PIR

OKBO2R. A00618.

RefSeq

XP_001790337.1.

UniGene

Bt.95129

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2APK	model	-	A	2-401	[»]
2BPK	model	-	A	2-401	[»]

SMR

P00515. Positions 114-397.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:546N.

STRING

P00515.

Genome annotation databases

Ensembl

ENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205; Bos taurus. [Genome view]

GeneID

100139910.

KEGG

bta:100139910.

Organism-specific databases

CTD

100139910.

Phylogenomic databases

HOVERGEN

P00515.

OMA

DQQRCRL.

Family and domain databases

InterPro

IPR003117. cAMP-dep_prot_kin_reg_I/II_a/b.
IPR002373. cAMP/cGMP_kin.
IPR000595. cNMP_bd.
IPR018488. cNMP_bd_CS.
IPR012198. PK_regulatory.
IPR014710. RmlC-like_jellyroll.
[Graphical view]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.

Pfam

PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]

PIRSF

PIRSF000548. PK_regulatory. 1 hit.

PRINTS

PR00103. CAMPKINASE.

SMART

SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]

PROSITE

PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

KAP2_BOVIN

Accession

Primary (citable) accession number: P00515

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 17, 2007
Last modified:	November 3, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (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