KAP0_RAT
ID KAP0_RAT Reviewed; 381 AA.
AC P09456;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
DE Contains:
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed;
GN Name=Prkar1a;
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].
RC TISSUE=Brain;
RX PubMed=3619906; DOI=10.1016/0006-291x(87)90612-7;
RA Kuno T., Ono Y., Hirai M., Hashimoto S., Shuntoh H., Tanaka C.;
RT "Molecular cloning and cDNA structure of the regulatory subunit of type I
RT cAMP-dependent protein kinase from rat brain.";
RL Biochem. Biophys. Res. Commun. 146:878-883(1987).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-83 AND SER-258, 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).
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 PRKACA and
CC PRKACB (By similarity). PRKAR1A also interacts with RFC2; the complex
CC may be involved in cell survival. Interacts with AKAP4. Interacts with
CC RARA; the interaction occurs in the presence of cAMP or FSH and
CC regulates RARA transcriptional activity. Interacts with the
CC phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with
CC PRKX; regulates this cAMP-dependent protein kinase (By similarity).
CC Interacts with smAKAP; this interaction may target PRKAR1A to the
CC plasma membrane. Interacts with AICDA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10644}.
CC -!- INTERACTION:
CC P09456; Q5VU43-11: PDE4DIP; Xeno; NbExp=2; IntAct=EBI-916215, EBI-10769071;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
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 -!- MISCELLANEOUS: Two types of regulatory chains are found: type I, which
CC predominates in skeletal muscle, and type II, which predominates in
CC cardiac muscle.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; M17086; AAB54276.1; -; mRNA.
DR PIR; A26910; OKRT1R.
DR RefSeq; NP_037313.1; NM_013181.1.
DR RefSeq; XP_008766533.1; XM_008768311.1.
DR RefSeq; XP_017452536.1; XM_017597047.1.
DR AlphaFoldDB; P09456; -.
DR SMR; P09456; -.
DR BioGRID; 247754; 1.
DR IntAct; P09456; 2.
DR STRING; 10116.ENSRNOP00000067771; -.
DR GuidetoPHARMACOLOGY; 1472; -.
DR iPTMnet; P09456; -.
DR PhosphoSitePlus; P09456; -.
DR jPOST; P09456; -.
DR PaxDb; P09456; -.
DR PRIDE; P09456; -.
DR GeneID; 25725; -.
DR KEGG; rno:25725; -.
DR CTD; 5573; -.
DR RGD; 3391; Prkar1a.
DR VEuPathDB; HostDB:ENSRNOG00000049876; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_1_0_1; -.
DR InParanoid; P09456; -.
DR OMA; DQWERAN; -.
DR OrthoDB; 1047290at2759; -.
DR PhylomeDB; P09456; -.
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:P09456; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000049876; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P09456; RN.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005771; C:multivesicular body; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0097224; C:sperm connecting piece; 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:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0007143; P:female meiotic nuclear division; IEP:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:RGD.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IEP:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
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; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 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 1: Evidence at protein level;
KW Acetylation; cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..381
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000205380"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00514"
FT CHAIN 2..381
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit, N-terminally processed"
FT /id="PRO_0000423218"
FT REGION 2..136
FT /note="Dimerization and phosphorylation"
FT REGION 65..96
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 2
FT /note="N-acetylalanine; in cAMP-dependent protein kinase
FT type I-alpha regulatory subunit, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P00514"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 43095 MW; AF00CA8DECE462FC CRC64;
MASGSMAASE EERSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE
EARQIQSLQK SGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG
EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V
