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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

PRKAR2A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei205cAMP 11
Binding sitei214cAMP 11
Binding sitei335cAMP 21
Binding sitei344cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi136 – 257cAMP 1Add BLAST122
Nucleotide bindingi258 – 401cAMP 2Add BLAST144

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene namesi
Name:PRKAR2A
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2111446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00002053842 – 401cAMP-dependent protein kinase type II-alpha regulatory subunitAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei77PhosphoserineBy similarity1
Modified residuei96Phosphoserine; by PKABy similarity1
Modified residuei212Phosphothreonine; by PDPK11 Publication1
Modified residuei347PhosphoserineBy similarity1
Modified residuei392PhosphoserineBy similarity1

Post-translational modificationi

A second phosphorylation site has not been located.1 Publication
Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00515.
PeptideAtlasiP00515.
PRIDEiP00515.

PTM databases

iPTMnetiP00515.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSBTAG00000014205.

Interactioni

Subunit structurei

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; this interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CQ6XGM83EBI-7634955,EBI-8037154From a different organism.

Protein-protein interaction databases

DIPiDIP-546N.
IntActiP00515. 4 interactors.
MINTiMINT-1772188.
STRINGi9913.ENSBTAP00000018886.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2APKmodel-A2-401[»]
2BPKmodel-A2-401[»]
ProteinModelPortaliP00515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 135Dimerization and phosphorylationAdd BLAST134

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP00515.
KOiK04739.
OMAiDNQTRCV.
OrthoDBiEOG091G0F1K.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHIQIPPGL TELLQGYTVE VLRQRPPDLV DFAVDYFTRL REARSRASTP
60 70 80 90 100
PAAPPSGSQD FDPGAGLVAD AVADSESEDE EDLDVPIPGR FDRRVSVCAE
110 120 130 140 150
TYNPDEEEED TDPRVIHPKT DQQRCRLQEA CKDILLFKNL DPEQLSQVLD
160 170 180 190 200
AMFERTVKVD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNH
210 220 230 240 250
GSFGELALMY NTPRAATIVA TSEGSLWGLD RVTFRRIIVK NNAKKRKMFE
260 270 280 290 300
SFIESVPLLK SLEVSERMKI VDVIGEKVYK DGERIITQGE KADSFYIIES
310 320 330 340 350
GEVSILIKSK TKVNKDGENQ EVEIARCHKG QYFGELALVT NKPRAASAYA
360 370 380 390 400
VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSSMDLIDPG

Q
Length:401
Mass (Da):45,094
Last modified:April 17, 2007 - v2
Checksum:i8FEA32E5B39A545A
GO

Sequence databases

PIRiA00618. OKBO2R.
RefSeqiNP_001178296.1. NM_001191367.1.
UniGeneiBt.9222.

Genome annotation databases

EnsembliENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205.
GeneIDi100139910.
KEGGibta:100139910.

Cross-referencesi

Sequence databases

PIRiA00618. OKBO2R.
RefSeqiNP_001178296.1. NM_001191367.1.
UniGeneiBt.9222.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2APKmodel-A2-401[»]
2BPKmodel-A2-401[»]
ProteinModelPortaliP00515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-546N.
IntActiP00515. 4 interactors.
MINTiMINT-1772188.
STRINGi9913.ENSBTAP00000018886.

Chemistry databases

ChEMBLiCHEMBL2111446.

PTM databases

iPTMnetiP00515.

Proteomic databases

PaxDbiP00515.
PeptideAtlasiP00515.
PRIDEiP00515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205.
GeneIDi100139910.
KEGGibta:100139910.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP00515.
KOiK04739.
OMAiDNQTRCV.
OrthoDBiEOG091G0F1K.
TreeFamiTF314920.

Enzyme and pathway databases

ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiP00515.

Gene expression databases

BgeeiENSBTAG00000014205.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAP2_BOVIN
AccessioniPrimary (citable) accession number: P00515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 17, 2007
Last modified: October 5, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.