KAP1_RAT
ID KAP1_RAT Reviewed; 381 AA.
AC P81377;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=cAMP-dependent protein kinase type I-beta regulatory subunit;
GN Name=Prkar1b;
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.
RC TISSUE=Brain;
RX PubMed=2372396; DOI=10.1002/mrd.1080260206;
RA Massa J.S., Fellows R.E., Maurer R.A.;
RT "Rat RI beta isoform of type I regulatory subunit of cyclic adenosine
RT monophosphate-dependent protein kinase: cDNA sequence analysis, mRNA tissue
RT specificity, and rat/mouse difference in expression in testis.";
RL Mol. Reprod. Dev. 26:129-133(1990).
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: Abundant in brain and testis. No expression in
CC lung, heart, liver, spleen, kidney and skeletal muscle.
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 PIR; A60669; A60669.
DR AlphaFoldDB; P81377; -.
DR SMR; P81377; -.
DR STRING; 10116.ENSRNOP00000033202; -.
DR GuidetoPHARMACOLOGY; 1473; -.
DR iPTMnet; P81377; -.
DR PhosphoSitePlus; P81377; -.
DR jPOST; P81377; -.
DR PRIDE; P81377; -.
DR Ensembl; ENSRNOT00000101865; ENSRNOP00000083988; ENSRNOG00000028733.
DR UCSC; RGD:3392; rat.
DR RGD; 3392; Prkar1b.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000157513; -.
DR InParanoid; P81377; -.
DR PhylomeDB; P81377; -.
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-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-9634597; GPER1 signaling.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P81377; -.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0005771; C:multivesicular body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
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:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1903367; P:positive regulation of fear response; IMP:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12102; DD_RIbeta_PKA; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR042818; RIbeta_DD.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 2: Evidence at transcript 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_0000205383"
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 /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P31321"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31321"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12849"
FT MOD_RES 97
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P12849"
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; 43282 MW; 7FEA5277FD8D81DE CRC64;
MASPSCFHSE DEDSLKGCEM YVQKHGIQQV LKECIVHLCV AKPDRPLRFL REHFEKLEKE
ENRQILARQK SNSQCDSHDE EISPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK
DYKTMTALAK AISKNVLFSH LDDNERSDIF DAMFPVTHID GETVIQQGNE GDNFYVIDQG
EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA
SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSEILKRNI QRYNSFISLT V
