[1]	PROTEIN SEQUENCE OF 2-401. TISSUE=Heart muscle; DOI=10.1073/pnas.79.8.2544; PubMed=6283532 [NCBI, ExPASy, EBI, Israel, Japan] Takio K., Smith S.B., Krebs E.G., Walsh K.A., Titani K.; "Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle."; Proc. Natl. Acad. Sci. U.S.A. 79:2544-2548(1982).
[2]	PROTEIN SEQUENCE OF 155-166, AND PHOSPHORYLATION AT THR-212. DOI=10.1016/0003-9861(91)90460-Z; PubMed=1654846 [NCBI, ExPASy, EBI, Israel, Japan] Braun R.K., Vulliet P.R., Carbonaro-Hall D.A., Hall F.L.; "Phosphorylation of RII subunit and attenuation of cAMP-dependent protein kinase activity by proline-directed protein kinase."; Arch. Biochem. Biophys. 289:187-191(1991).
[3]	3D-STRUCTURE MODELING. DOI=10.1021/bi00376a003; PubMed=3030405 [NCBI, ExPASy, EBI, Israel, Japan] Weber I.T., Steitz T.A., Bubis J., Taylor S.S.; "Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase."; Biochemistry 26:343-351(1987).

Comments

SUBUNIT: 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.
PTM: A second phosphorylation site has not been located.
PTM: Phosphorylation of Thr-212 by PDPK seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits.
SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family.
SIMILARITY: Contains 2 cyclic nucleotide-binding domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

IPI00693176; -.

A00618; OKBO2R.

XP_001790337.1; -.

3D structure databases

PDB

2APK; Model; -; A=2-401.	[ExPASy / RCSB / EBI]
2BPK; Model; -; A=2-401.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

2APK; -.
2BPK; -.

P00515; 114-397.

Protein-protein interaction databases

DIP

DIP:546N; -.

Ontologies

GO:0005952;	Cellular component: cAMP-dependent protein kinase complex (inferred from electronic annotation from InterPro).
GO:0030552;	Molecular function: cAMP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008603;	Molecular function: cAMP-dependent protein kinase regulator activity (inferred from electronic annotation from InterPro).
GO:0001932;	Biological process: regulation of protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007165;	Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.

Pfam

PF00027; cNMP_binding; 2.
PF02197; RIIa; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000548; PK_regulatory; 1.

PRINTS

PR00103; CAMPKINASE.

SMART

SM00100; cNMP; 2.
SM00394; RIIa; 1.
SMART graphical view of domain structure.

PROSITE

PS00888; CNMP_BINDING_1; 2.
PS00889; CNMP_BINDING_2; 2.
PS50042; CNMP_BINDING_3; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000014205; Bos taurus. [Contig view]

GeneID

100139910; -.

KEGG

bta:100139910; -.

Phylogenomic databases

HOVERGEN

P00515; -.

OMA

P00515; DQQRCRL.

Other

ProtoNet

P00515.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; cAMP; cAMP-binding; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 401`	`400`	`cAMP-dependent protein kinase type II-alpha regulatory subunit.`	`PRO_0000205384`
`NP_BIND`	`136 257`	`122`	`cAMP 1.`
`NP_BIND`	`258 401`	`144`	`cAMP 2.`
`REGION`	`2 135`	`134`	`Dimerization and phosphorylation.`
`BINDING`	`205 205`		`cAMP 1.`
`BINDING`	`214 214`		`cAMP 1.`
`BINDING`	`335 335`		`cAMP 2.`
`BINDING`	`344 344`		`cAMP 2.`
`MOD_RES`	`2 2`		`N-acetylserine.`
`MOD_RES`	`75 75`		`Phosphoserine (By similarity).`
`MOD_RES`	`77 77`		`Phosphoserine (By similarity).`
`MOD_RES`	`96 96`		`Phosphoserine; by PKA (By similarity).`
`MOD_RES`	`212 212`		`Phosphothreonine; by PDPK.`
`HELIX`	`144 149`	`6`
`STRAND`	`154 156`	`3`
`STRAND`	`176 184`	`9`
`STRAND`	`187 189`	`3`
`STRAND`	`192 200`	`9`
`STRAND`	`207 210`	`4`
`STRAND`	`214 217`	`4`
`STRAND`	`223 225`	`3`
`HELIX`	`230 236`	`7`
`TURN`	`237 239`	`3`
`HELIX`	`242 263`	`22`

Sequence information

Length: 401 AA [This is the length of the unprocessed precursor]

Molecular weight: 45094 Da [This is the MW of the unprocessed precursor]

CRC64: 8FEA32E5B39A545A [This is a checksum on the sequence]

        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

P00515 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools