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P12369

- KAP3_RAT

UniProt

P12369 - KAP3_RAT

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Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene

Prkar2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei221 – 2211cAMP 1
Binding sitei230 – 2301cAMP 1
Binding sitei350 – 3501cAMP 2
Binding sitei359 – 3591cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 273122cAMP 1Add
BLAST
Nucleotide bindingi274 – 416143cAMP 2Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: RGD
  2. cAMP-dependent protein kinase regulator activity Source: RGD
  3. protein domain specific binding Source: RGD
  4. protein kinase A catalytic subunit binding Source: RGD

GO - Biological processi

  1. regulation of protein kinase activity Source: RGD
  2. response to antipsychotic drug Source: RGD
  3. response to clozapine Source: RGD
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_231505. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene namesi
Name:Prkar2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3394. Prkar2b.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity
Note: Colocalizes with PJA2 in the cytoplasm and at the cell membrane.By similarity

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: RGD
  2. cytoplasm Source: RGD
  3. dendritic shaft Source: ParkinsonsUK-UCL
  4. dendritic spine Source: ParkinsonsUK-UCL
  5. membrane raft Source: RGD
  6. mitochondrial inner membrane Source: RGD
  7. perinuclear region of cytoplasm Source: RGD
  8. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 416415cAMP-dependent protein kinase type II-beta regulatory subunitPRO_0000205392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCurated
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei112 – 1121Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by the activated catalytic chain.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP12369.
PRIDEiP12369.

PTM databases

PhosphoSiteiP12369.

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. Brain. Present in a few pyramidal neurons and mostly in mossy fibers. Colocalizes with PJA2 in dentate granule cells and at postsynaptic sites of primary hippocampal neurons.1 Publication

Gene expression databases

GenevestigatoriP12369.

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 the phosphorylated form of PJA2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-6096160,EBI-5323863From a different organism.
PRKACAP176122EBI-6096160,EBI-476586From a different organism.

Protein-protein interaction databases

BioGridi246811. 1 interaction.
IntActiP12369. 2 interactions.
STRINGi10116.ENSRNOP00000012415.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi137 – 14711Combined sources
Helixi151 – 1544Combined sources
Helixi158 – 16710Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi188 – 20316Combined sources
Beta strandi206 – 21510Combined sources
Helixi221 – 2244Combined sources
Beta strandi231 – 24616Combined sources
Helixi247 – 25913Combined sources
Helixi273 – 2753Combined sources
Beta strandi276 – 2783Combined sources
Helixi280 – 28910Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi310 – 32415Combined sources
Beta strandi336 – 3427Combined sources
Beta strandi347 – 3493Combined sources
Helixi351 – 3555Combined sources
Beta strandi360 – 37516Combined sources
Helixi376 – 3827Combined sources
Helixi384 – 3863Combined sources
Helixi387 – 40519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CX4X-ray2.45A112-416[»]
3IDBX-ray1.62B108-268[»]
3IDCX-ray2.70B102-265[»]
4JVAX-ray2.50A112-416[»]
ProteinModelPortaliP12369.
SMRiP12369. Positions 3-41, 130-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12369.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 151150Dimerization and phosphorylationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP12369.
KOiK04739.
OrthoDBiEOG76T9RR.
PhylomeDBiP12369.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
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.

P12369-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR
60 70 80 90 100
FGHEGRTWGD AGAAAGGGTP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN
110 120 130 140 150
APVINRFTRR ASVCAEAYNP DEEEDDAESR IIHPKTDDQR NRLQEACKDI
160 170 180 190 200
LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI DQGDDGDNFY VIDRGTFDIY
210 220 230 240 250
VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG ALWGLDRVTF
260 270 280 290 300
RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ
310 320 330 340 350
IIAQGDSADS FFIVESGEVR ITMKRKGKSD IEENGAVEIA RCLRGQYFGE
360 370 380 390 400
LALVTNKPRA ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ
410
LVALFGTNMD IVEPTA
Length:416
Mass (Da):46,123
Last modified:January 23, 2007 - v3
Checksum:i8BC984E325FA3612
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12492 mRNA. Translation: AAA42047.1.
PIRiA28893. OKRTR2.
RefSeqiNP_001025191.1. NM_001030020.1.
UniGeneiRn.164375.
Rn.4075.

Genome annotation databases

GeneIDi24679.
KEGGirno:24679.
UCSCiRGD:3394. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12492 mRNA. Translation: AAA42047.1 .
PIRi A28893. OKRTR2.
RefSeqi NP_001025191.1. NM_001030020.1.
UniGenei Rn.164375.
Rn.4075.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CX4 X-ray 2.45 A 112-416 [» ]
3IDB X-ray 1.62 B 108-268 [» ]
3IDC X-ray 2.70 B 102-265 [» ]
4JVA X-ray 2.50 A 112-416 [» ]
ProteinModelPortali P12369.
SMRi P12369. Positions 3-41, 130-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246811. 1 interaction.
IntActi P12369. 2 interactions.
STRINGi 10116.ENSRNOP00000012415.

PTM databases

PhosphoSitei P12369.

Proteomic databases

PaxDbi P12369.
PRIDEi P12369.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24679.
KEGGi rno:24679.
UCSCi RGD:3394. rat.

Organism-specific databases

CTDi 5577.
RGDi 3394. Prkar2b.

Phylogenomic databases

eggNOGi COG0664.
HOGENOMi HOG000196668.
HOVERGENi HBG002025.
InParanoidi P12369.
KOi K04739.
OrthoDBi EOG76T9RR.
PhylomeDBi P12369.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_231505. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Miscellaneous databases

EvolutionaryTracei P12369.
NextBioi 604075.
PROi P12369.

Gene expression databases

Genevestigatori P12369.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi 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 ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, cDNA structure and deduced amino acid sequence for the hormone-induced regulatory subunit (RII beta) of cAMP-dependent protein kinase from rat ovarian granulosa cells."
    Sandberg M., Levy F.O., Oeyen O., Hansson V., Jahnsen T.
    Biochem. Biophys. Res. Commun. 154:705-711(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning, cDNA structure, and regulation of the regulatory subunit of type II cAMP-dependent protein kinase from rat ovarian granulosa cells."
    Jahnsen T., Hedin L., Kidd V.J., Beattie W.G., Lohmann S.M., Walter U., Durica J., Schulz T.Z., Schiltz E., Browner M., Lawrence C.B., Goldman D., Ratoosh S.L., Richards J.S.
    J. Biol. Chem. 261:12352-12361(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 16-416.
    Tissue: Ovarian granulosa cell.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: TISSUE SPECIFICITY.
  5. "Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit."
    Diller T.C., Madhusudan X., Xuong N.H., Taylor S.S.
    Structure 9:73-82(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 112-416.

Entry informationi

Entry nameiKAP3_RAT
AccessioniPrimary (citable) accession number: P12369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3