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P00514 (KAP0_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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 I-alpha regulatory subunit
Gene names
Name:PRKAR1A
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length380 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.

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. Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane By similarity. Interacts with AICDA By similarity.

Subcellular location

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380cAMP-dependent protein kinase type I-alpha regulatory subunit
PRO_0000423216
Initiator methionine11Removed; alternate Ref.3
Chain2 – 380379cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
PRO_0000205376

Regions

Nucleotide binding136 – 253118cAMP 1
Nucleotide binding254 – 380127cAMP 2
Region2 – 135134Dimerization and phosphorylation
Motif95 – 995Pseudophosphorylation motif

Sites

Binding site2011cAMP 1
Binding site2101cAMP 1
Binding site3251cAMP 2
Binding site3341cAMP 2

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylalanine; in cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
Modified residue821Phosphoserine By similarity
Modified residue1001Phosphoserine By similarity
Disulfide bond17Interchain (with C-37) Ref.7
Disulfide bond38Interchain (with C-16) Ref.7

Experimental info

Sequence conflict2301Y → N in AAA30708. Ref.4

Secondary structure

................................................................ 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00514 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: B086A291809422F4

FASTA38042,893
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
PIROKBO1R. A00617.
I45957.
RefSeqNP_001069826.1. NM_001076358.1.
UniGeneBt.10903.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1APKmodel-A2-380[»]
1BPKmodel-A2-380[»]
1NE4X-ray2.40A95-377[»]
1NE6X-ray2.30A95-377[»]
1PVKmodel-A114-245[»]
1RGSX-ray2.80A93-380[»]
1RL3X-ray2.70A/B93-380[»]
2EZWNMR-A/B13-62[»]
2QCSX-ray2.20B91-380[»]
3FHIX-ray2.00B92-245[»]
3IIAX-ray2.70A92-245[»]
3IM3X-ray2.00A13-62[»]
3IM4X-ray2.28A/B13-62[»]
3PLQX-ray2.30A92-245[»]
3PNAX-ray1.50A/B92-245[»]
3PVBX-ray3.30B85-244[»]
4JV4X-ray2.95A93-377[»]
4MX3X-ray3.88A/B2-380[»]
DisProtDP00245.
ProteinModelPortalP00514.
SMRP00514. Positions 13-62, 110-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36644N.
IntActP00514. 2 interactions.
MINTMINT-1778627.
STRING9913.ENSBTAP00000011371.

Chemistry

BindingDBP00514.

Proteomic databases

PRIDEP00514.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.
GeneID615074.
KEGGbta:615074.

Organism-specific databases

CTD5573.

Phylogenomic databases

eggNOGCOG0664.
GeneTreeENSGT00530000062947.
HOGENOMHOG000196669.
HOVERGENHBG002025.
InParanoidP00514.
KOK04739.
OMAXVIPKDY.
OrthoDBEOG72JWG6.
TreeFamTF314920.

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

EvolutionaryTraceP00514.
NextBio20899431.

Entry information

Entry nameKAP0_BOVIN
AccessionPrimary (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: July 9, 2014
This is version 138 of the entry and version 2 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