ID   KAP1_MOUSE              Reviewed;         381 AA.
AC   P12849;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=cAMP-dependent protein kinase type I-beta regulatory subunit;
GN   Name=Prkar1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=3375237; DOI=10.1073/pnas.85.11.3703;
RA   Clegg C.H., Cadd G.G., McKnight G.S.;
RT   "Genetic characterization of a brain-specific form of the type I regulatory
RT   subunit of cAMP-dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3703-3707(1988).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-83 AND THR-85, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-97, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. {ECO:0000250}.
CC   -!- SUBUNIT: The inactive holoenzyme is composed of two regulatory chains
CC       and two catalytic chains. Activation by cAMP releases the two active
CC       catalytic monomers and the regulatory dimer. Interacts with PRKX;
CC       regulates this cAMP-dependent protein kinase (By similarity). Interacts
CC       with smAKAP; this interaction may target PRKAR1B to the plasma membrane
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: 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.
CC   -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC       region of the catalytic chain, resulting in the inhibition of its
CC       activity.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; M20473; AAA39935.1; -; mRNA.
DR   CCDS; CCDS19803.1; -.
DR   PIR; A30205; OKMSR1.
DR   RefSeq; NP_001240819.1; NM_001253890.1.
DR   RefSeq; NP_032949.3; NM_008923.3.
DR   RefSeq; XP_006504723.1; XM_006504660.3.
DR   RefSeq; XP_006504724.1; XM_006504661.3.
DR   RefSeq; XP_006504726.1; XM_006504663.2.
DR   RefSeq; XP_017176208.1; XM_017320719.1.
DR   AlphaFoldDB; P12849; -.
DR   SMR; P12849; -.
DR   BioGRID; 202366; 93.
DR   CORUM; P12849; -.
DR   IntAct; P12849; 6.
DR   MINT; P12849; -.
DR   STRING; 10090.ENSMUSP00000026973; -.
DR   iPTMnet; P12849; -.
DR   PhosphoSitePlus; P12849; -.
DR   jPOST; P12849; -.
DR   MaxQB; P12849; -.
DR   PaxDb; 10090-ENSMUSP00000026973; -.
DR   PeptideAtlas; P12849; -.
DR   ProteomicsDB; 301729; -.
DR   Pumba; P12849; -.
DR   Antibodypedia; 10769; 400 antibodies from 32 providers.
DR   DNASU; 19085; -.
DR   Ensembl; ENSMUST00000026973.14; ENSMUSP00000026973.8; ENSMUSG00000025855.14.
DR   Ensembl; ENSMUST00000110890.8; ENSMUSP00000106515.2; ENSMUSG00000025855.14.
DR   GeneID; 19085; -.
DR   KEGG; mmu:19085; -.
DR   UCSC; uc009afy.2; mouse.
DR   AGR; MGI:97759; -.
DR   CTD; 5575; -.
DR   MGI; MGI:97759; Prkar1b.
DR   VEuPathDB; HostDB:ENSMUSG00000025855; -.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000157513; -.
DR   HOGENOM; CLU_018310_1_1_1; -.
DR   InParanoid; P12849; -.
DR   OMA; QILAWQK; -.
DR   OrthoDB; 55978at2759; -.
DR   PhylomeDB; P12849; -.
DR   TreeFam; TF314920; -.
DR   Reactome; R-MMU-163615; PKA activation.
DR   Reactome; R-MMU-164378; PKA activation in glucagon signalling.
DR   Reactome; R-MMU-180024; DARPP-32 events.
DR   Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-MMU-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR   Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR   Reactome; R-MMU-9634597; GPER1 signaling.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 19085; 0 hits in 80 CRISPR screens.
DR   PRO; PR:P12849; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P12849; Protein.
DR   Bgee; ENSMUSG00000025855; Expressed in substantia nigra and 280 other cell types or tissues.
DR   ExpressionAtlas; P12849; baseline and differential.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR   GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0030552; F:cAMP binding; ISO:MGI.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:MGI.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; ISS:MGI.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR   GO; GO:1903367; P:positive regulation of fear response; ISO:MGI.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12102; DD_RIbeta_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; IPR042818; RIbeta_DD.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-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.
DR   Genevisible; P12849; MM.
PE   1: Evidence at protein level;
KW   cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane; Methylation;
KW   Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..381
FT                   /note="cAMP-dependent protein kinase type I-beta regulatory
FT                   subunit"
FT                   /id="PRO_0000205382"
FT   REGION          1..136
FT                   /note="Dimerization and phosphorylation"
FT   REGION          66..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..100
FT                   /note="Pseudophosphorylation motif"
FT   BINDING         137..254
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         202
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         211
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         255..381
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         326
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         335
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P31321"
FT   MOD_RES         21
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P31321"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         97
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   DISULFID        18
FT                   /note="Interchain (with C-39)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        39
FT                   /note="Interchain (with C-18)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  43224 MW;  42287E553FA16023 CRC64;
     MASPSCFHSE DEDSLKGCEM YVQKHGIQQV LKECIVHLCV AKPDRPLRFL REHFEKLEKE
     ENRQILARQK SNSQCDSHDE EISPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK
     DYKTMTALAK AISKNVLFSH LDDNERSDIF DAMFPVTHIG GETVIQQGNE GDNFYVIDQG
     EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL
     RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA
     SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG
     PCSEILKRNI QRYNSFISLT V
//