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Database: UniProt
Entry: KAP3_RAT
LinkDB: KAP3_RAT
Original site: KAP3_RAT 
ID   KAP3_RAT                Reviewed;         416 AA.
AC   P12369;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit;
GN   Name=Prkar2b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3401231; DOI=10.1016/0006-291x(88)90197-0;
RA   Sandberg M., Levy F.O., Oeyen O., Hansson V., Jahnsen T.;
RT   "Molecular cloning, cDNA structure and deduced amino acid sequence for the
RT   hormone-induced regulatory subunit (RII beta) of cAMP-dependent protein
RT   kinase from rat ovarian granulosa cells.";
RL   Biochem. Biophys. Res. Commun. 154:705-711(1988).
RN   [2]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE OF 16-416.
RC   TISSUE=Ovarian granulosa cell;
RX   PubMed=2427518; DOI=10.1016/s0021-9258(18)67247-3;
RA   Jahnsen T., Hedin L., Kidd V.J., Beattie W.G., Lohmann S.M., Walter U.,
RA   Durica J., Schulz T.Z., Schiltz E., Browner M., Lawrence C.B., Goldman D.,
RA   Ratoosh S.L., Richards J.S.;
RT   "Molecular cloning, cDNA structure, and regulation of the regulatory
RT   subunit of type II cAMP-dependent protein kinase from rat ovarian granulosa
RT   cells.";
RL   J. Biol. Chem. 261:12352-12361(1986).
RN   [3]
RP   ERRATUM OF PUBMED:2427518.
RA   Jahnsen T., Hedin L., Kidd V.J., Beattie W.G., Lohmann S.M., Walter U.,
RA   Durica J., Schulz T.Z., Schiltz E., Browner M., Lawrence C.B., Goldman D.,
RA   Ratoosh S.L., Richards J.S.;
RL   J. Biol. Chem. 263:4041-4041(1988).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=21423175; DOI=10.1038/ncb2209;
RA   Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R.,
RA   Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.;
RT   "Control of PKA stability and signalling by the RING ligase praja2.";
RL   Nat. Cell Biol. 13:412-422(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-112, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 112-416.
RX   PubMed=11342137; DOI=10.1016/s0969-2126(00)00556-6;
RA   Diller T.C., Madhusudan X., Xuong N.H., Taylor S.S.;
RT   "Molecular basis for regulatory subunit diversity in cAMP-dependent protein
RT   kinase: crystal structure of the type II beta regulatory subunit.";
RL   Structure 9:73-82(2001).
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. Type II regulatory chains mediate
CC       membrane association by binding to anchoring proteins, including the
CC       MAP2 kinase.
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two regulatory
CC       chains and two catalytic chains. Activation by cAMP produces two active
CC       catalytic monomers and a regulatory dimer that binds four cAMP
CC       molecules. Interacts with PRKACA and PRKACB. Interacts with the
CC       phosphorylated form of PJA2. Forms a complex composed of PRKAR2B, GSK3B
CC       and GSKIP through GSKIP interaction; facilitates PKA-induced
CC       phosphorylation and regulates GSK3B activity.
CC       {ECO:0000250|UniProtKB:P31323}.
CC   -!- INTERACTION:
CC       P12369; Q5S007: LRRK2; Xeno; NbExp=3; IntAct=EBI-6096160, EBI-5323863;
CC       P12369; P17612: PRKACA; Xeno; NbExp=2; IntAct=EBI-6096160, EBI-476586;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at the
CC       cell membrane. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha,
CC       I-beta, II-alpha, and II-beta. Their expression varies among tissues
CC       and is in some cases constitutive and in others inducible. Brain.
CC       Present in a few pyramidal neurons and mostly in mossy fibers.
CC       Colocalizes with PJA2 in dentate granule cells and at postsynaptic
CC       sites of primary hippocampal neurons. {ECO:0000269|PubMed:21423175}.
CC   -!- PTM: Phosphorylated by the activated catalytic chain.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; M12492; AAA42047.1; -; mRNA.
DR   PIR; A28893; OKRTR2.
DR   RefSeq; NP_001025191.1; NM_001030020.1.
DR   PDB; 1CX4; X-ray; 2.45 A; A=112-416.
DR   PDB; 3IDB; X-ray; 1.62 A; B=108-268.
DR   PDB; 3IDC; X-ray; 2.70 A; B=102-265.
DR   PDB; 4JVA; X-ray; 2.50 A; A=112-416.
DR   PDB; 6WJF; EM; 7.50 A; C/D=1-416.
DR   PDB; 6WJG; EM; 6.20 A; C/D=1-416.
DR   PDBsum; 1CX4; -.
DR   PDBsum; 3IDB; -.
DR   PDBsum; 3IDC; -.
DR   PDBsum; 4JVA; -.
DR   PDBsum; 6WJF; -.
DR   PDBsum; 6WJG; -.
DR   AlphaFoldDB; P12369; -.
DR   EMDB; EMD-21692; -.
DR   EMDB; EMD-21693; -.
DR   SMR; P12369; -.
DR   BioGRID; 246811; 2.
DR   CORUM; P12369; -.
DR   DIP; DIP-61323N; -.
DR   IntAct; P12369; 3.
DR   STRING; 10116.ENSRNOP00000012415; -.
DR   GuidetoPHARMACOLOGY; 1475; -.
DR   iPTMnet; P12369; -.
DR   PhosphoSitePlus; P12369; -.
DR   jPOST; P12369; -.
DR   PaxDb; 10116-ENSRNOP00000012415; -.
DR   Ensembl; ENSRNOT00000012415.7; ENSRNOP00000012415.6; ENSRNOG00000009079.7.
DR   Ensembl; ENSRNOT00055009585; ENSRNOP00055007396; ENSRNOG00055005922.
DR   Ensembl; ENSRNOT00060015782; ENSRNOP00060012312; ENSRNOG00060009345.
DR   Ensembl; ENSRNOT00065018006; ENSRNOP00065013730; ENSRNOG00065011126.
DR   GeneID; 24679; -.
DR   KEGG; rno:24679; -.
DR   UCSC; RGD:3394; rat.
DR   AGR; RGD:3394; -.
DR   CTD; 5577; -.
DR   RGD; 3394; Prkar2b.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000158160; -.
DR   HOGENOM; CLU_018310_2_0_1; -.
DR   InParanoid; P12369; -.
DR   OMA; GEQGDTF; -.
DR   OrthoDB; 55978at2759; -.
DR   PhylomeDB; P12369; -.
DR   TreeFam; TF314920; -.
DR   Reactome; R-RNO-163615; PKA activation.
DR   Reactome; R-RNO-164378; PKA activation in glucagon signalling.
DR   Reactome; R-RNO-180024; DARPP-32 events.
DR   Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-RNO-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR   Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR   Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR   Reactome; R-RNO-9634597; GPER1 signaling.
DR   Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR   EvolutionaryTrace; P12369; -.
DR   PRO; PR:P12369; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000009079; Expressed in ovary and 19 other cell types or tissues.
DR   ExpressionAtlas; P12369; baseline and differential.
DR   Genevisible; P12369; RN.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0097546; C:ciliary base; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043198; C:dendritic shaft; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0030552; F:cAMP binding; IDA:RGD.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:RGD.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0007612; P:learning; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEP:RGD.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12104; DD_RIIbeta_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF156; CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; cAMP-binding; Cell membrane; Cytoplasm; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..416
FT                   /note="cAMP-dependent protein kinase type II-beta
FT                   regulatory subunit"
FT                   /id="PRO_0000205392"
FT   REGION          2..151
FT                   /note="Dimerization and phosphorylation"
FT   REGION          53..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         152..273
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         221
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         230
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         274..416
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         350
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         359
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   MOD_RES         69
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P31323"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100,
FT                   ECO:0007744|PubMed:22673903"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   HELIX           158..167
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   STRAND          188..203
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   STRAND          206..215
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   STRAND          231..246
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   HELIX           247..259
FT                   /evidence="ECO:0007829|PDB:3IDB"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          276..278
FT                   /evidence="ECO:0007829|PDB:4JVA"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          310..324
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          336..342
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   HELIX           351..355
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   STRAND          360..375
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   HELIX           376..382
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:1CX4"
FT   HELIX           387..405
FT                   /evidence="ECO:0007829|PDB:1CX4"
SQ   SEQUENCE   416 AA;  46123 MW;  8BC984E325FA3612 CRC64;
     MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD
     AGAAAGGGTP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP
     DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI
     DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG
     ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ
     IIAQGDSADS FFIVESGEVR ITMKRKGKSD IEENGAVEIA RCLRGQYFGE LALVTNKPRA
     ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA
//
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