P00514 (KAP0_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

PRKAR1A

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

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Subunit structure	The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity By similarity. Interacts with the phosphorylated form of PJA2 By similarity. Interacts with CBFA2T3 By similarity. Interacts with PRKX; regulates this cAMP-dependent protein kinase 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	The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear.
Sequence similarities	Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of protein 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 380

379

cAMP-dependent protein kinase type I-alpha regulatory subunit

PRO_0000205376

Regions

Nucleotide binding

136 – 253

118

cAMP 1

Nucleotide binding

254 – 380

127

cAMP 2

Region

2 – 135

134

Dimerization and phosphorylation

Motif

95 – 99

5

Pseudophosphorylation motif

Sites

Binding site

201

1

cAMP 1

Binding site

210

1

cAMP 1

Binding site

325

1

cAMP 2

Binding site

334

1

cAMP 2

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

76

1

Phosphoserine By similarity

Modified residue

82

1

Phosphoserine By similarity

Modified residue

100

1

Phosphoserine By similarity

Disulfide bond

17

Interchain (with C-37) Ref.7

Disulfide bond

38

Interchain (with C-16) Ref.7

Experimental info

Sequence conflict

230

1

Y → N in AAA30708. Ref.4

Secondary structure

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380

Helix Strand Turn

Details...

Beta strand

106 – 108

3

Helix

121 – 132

12

Helix

135 – 138

4

Helix

142 – 151

10

Beta strand

153 – 157

5

Beta strand

162 – 164

3

Beta strand

172 – 179

8

Beta strand

181 – 185

5

Beta strand

188 – 193

6

Helix

201 – 206

6

Beta strand

211 – 218

8

Beta strand

220 – 226

7

Helix

227 – 233

7

Helix

235 – 250

16

Helix

253 – 257

5

Helix

260 – 269

10

Beta strand

271 – 275

5

Beta strand

280 – 282

3

Beta strand

284 – 286

3

Beta strand

290 – 303

14

Beta strand

305 – 309

5

Beta strand

312 – 317

6

Helix

325 – 330

6

Beta strand

335 – 350

16

Helix

351 – 357

7

Helix

359 – 361

3

Helix

362 – 367

6

Helix

368 – 371

4

Sequences

	Sequence		Length	Mass (Da)
	P00514 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: B086A291809422F4	FASTA	380	42,893
	10 20 30 40 50 60 MASGTTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR EYFEKLEKEE 70 80 90 100 110 120 AKQIQNLQKA GSRADSREDE ISPPPPNPVV KGRRRRGAIS AEVYTEEDAA SYVRKVIPKD 130 140 150 160 170 180 YKTMAALAKA IEKNVLFSHL DDNERSDIFD AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE 190 200 210 220 230 240 MDVYVNNEWA TSVGEGGSFG ELALIYGTPR AATVKAKTNV KLWGIDRDSY RRILMGSTLR 250 260 270 280 290 300 KRKMYEEFLS KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA 310 320 330 340 350 360 VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD RPRFERVLGP 370 380 CSDILKRNIQ QYNSFVSLSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Basal ganglia.
[3]	"Amino acid sequence of the regulatory subunit of bovine type I adenosine cyclic 3',5'-phosphate dependent protein kinase." Titani K., Sasagawa T., Ericsson L.H., Kumar S., Smith S.B., Krebs E.G., Walsh K.A. Biochemistry 23:4193-4199(1984) [PubMed: 6487597] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-380.
[4]	"Isolation of a cDNA clone for the type I regulatory subunit of bovine cAMP-dependent protein kinase." Lee D.C., Carmichael D.F., Krebs E.G., McKnight G.S. Proc. Natl. Acad. Sci. U.S.A. 80:3608-3612(1983) [PubMed: 6190178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-232.
[5]	"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.
[6]	"Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains." Su Y., Dostmann W.R., Herberg F.W., Durick K., Xuong N.H., ten Eyck L., Taylor S.S., Varughese K.I. Science 269:807-813(1995) [PubMed: 7638597] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-380.
[7]	"Antiparallel alignment of the two protomers of the regulatory subunit dimer of cAMP-dependent protein kinase I." Bubis J., Vedvick T.S., Taylor S.S. J. Biol. Chem. 262:14961-14966(1987) [PubMed: 3667618] [Abstract] Cited for: DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BT030573 mRNA. Translation: ABQ13013.1.
BC118242 mRNA. Translation: AAI18243.1.
K00833 mRNA. Translation: AAA30708.1.

IPI

IPI00714984.

PIR

OKBO1R. A00617.
I45957.

RefSeq

NP_001069826.1. NM_001076358.1.

UniGene

Bt.10903.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APK	model	-	A	2-380	[»]
1BPK	model	-	A	2-380	[»]
1NE4	X-ray	2.40	A	95-376	[»]
1NE6	X-ray	2.30	A	95-376	[»]
1PVK	model	-	A	114-245	[»]
1RGS	X-ray	2.80	A	93-380	[»]
1RL3	X-ray	2.70	A/B	93-379	[»]
2EZW	NMR	-	A/B	13-61	[»]
2QCS	X-ray	2.20	B	91-380	[»]
3FHI	X-ray	2.00	B	92-245	[»]
3IIA	X-ray	2.70	A	92-245	[»]
3IM3	X-ray	2.00	A	13-62	[»]
3IM4	X-ray	2.28	A/B	13-62	[»]
3PLQ	X-ray	2.30	A	92-245	[»]
3PNA	X-ray	1.50	A/B	92-245	[»]
3PVB	X-ray	3.30	B	85-244	[»]

ProteinModelPortal

P00514.

SMR

P00514. Positions 13-62, 110-377.

DisProt

DP00245.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36644N.

IntAct

P00514. 1 interaction.

MINT

MINT-1778627.

STRING

P00514.

Proteomic databases

PRIDE

P00514.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.

GeneID

615074.

KEGG

bta:615074.

Organism-specific databases

CTD

5573.

Phylogenomic databases

eggNOG

maNOG08260.

GeneTree

ENSGT00530000062947.

HOVERGEN

HBG002025.

InParanoid

P00514.

OMA

FDAMFPC.

OrthoDB

EOG4JQ3XP.

PhylomeDB

P00514.

Family and domain databases

InterPro

IPR002373. 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]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.

KO

K04739.

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]

SUPFAM

SSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit.
SSF51206. cNMP_binding. 2 hits.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

KAP0_BOVIN

Accession

Primary (citable) accession number: P00514
Secondary accession number(s): A5D9F4, Q17QP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 17, 2007
Last modified:	November 16, 2011
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program