KAP0_CHICK
ID KAP0_CHICK Reviewed; 382 AA.
AC Q5ZM91;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
GN Name=PRKAR1A; ORFNames=RCJMB04_2n5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain but is not phosphorylated. The
CC physiological significance of phosphorylations by other kinases is
CC unclear (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; AJ719493; CAG31152.1; -; mRNA.
DR RefSeq; NP_001007846.1; NM_001007845.1.
DR RefSeq; XP_015135378.1; XM_015279892.1.
DR RefSeq; XP_015135379.1; XM_015279893.1.
DR RefSeq; XP_015135380.1; XM_015279894.1.
DR AlphaFoldDB; Q5ZM91; -.
DR SMR; Q5ZM91; -.
DR STRING; 9031.ENSGALP00000033915; -.
DR PaxDb; Q5ZM91; -.
DR Ensembl; ENSGALT00000034558; ENSGALP00000033915; ENSGALG00000004237.
DR Ensembl; ENSGALT00000093676; ENSGALP00000070816; ENSGALG00000004237.
DR GeneID; 417438; -.
DR KEGG; gga:417438; -.
DR CTD; 5573; -.
DR VEuPathDB; HostDB:geneid_417438; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000155148; -.
DR HOGENOM; CLU_018310_1_0_1; -.
DR InParanoid; Q5ZM91; -.
DR OMA; DQWERAN; -.
DR OrthoDB; 1047290at2759; -.
DR PhylomeDB; Q5ZM91; -.
DR Reactome; R-GGA-163615; PKA activation.
DR Reactome; R-GGA-164378; PKA activation in glucagon signalling.
DR Reactome; R-GGA-180024; DARPP-32 events.
DR Reactome; R-GGA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-GGA-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-GGA-5610787; Hedgehog 'off' state.
DR Reactome; R-GGA-9634597; GPER1 signaling.
DR Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q5ZM91; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000004237; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; Q5ZM91; baseline and differential.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
DR GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR GO; GO:0097224; C:sperm connecting piece; IEA:Ensembl.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
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; 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 Acetylation; cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00514"
FT CHAIN 2..382
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000293483"
FT REGION 2..136
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="Pseudophosphorylation motif"
FT BINDING 138..255
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 203
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 256..382
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 327
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00514"
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 382 AA; 43350 MW; B7F778C55FC866D8 CRC64;
MATSSSSSSE EERSLRECEL YVQKHNIQQL LKDCIVQLCT VRPDRPMGFL REYFERLEKE
ETKQLLNQQK SGSRSDSRED EISPPPPMNP VVKGRRRRGA ISAEVYTEED AASYVRKVIP
KDYKTMAALA KAIEKNVLFA HLDDNERSDI FDAMFPVTYI AGETVIQQGD EGDNFYVVDQ
GEMDVYVNNE WATSVGEGGS FGELALIYGT PRAATVKAKT NVKLWGIDRD SYRRILMGST
LRKRKMYEEF LSKVSILESL DKWERLTVAD ALEPVQFEDG QKIVVQGEPG DEFFIILEGT
AAVLQRRSEN EEFVEVGRLA PSDYFGEIAL LMNRPRAATV VARGLLKCVK LDRPRFERVL
GPCSDILKRN IQQYNSFVSL SV
