ID KAPR_YARLI Reviewed; 375 AA.
AC Q6C2X0; Q70IV2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR; OrderedLocusNames=YALI0F04422g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E 129;
RA Cervantes J.A.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC subunits. In the presence of cAMP it dissociates into 2 active
CC monomeric C subunits and an R dimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ579715; CAE30452.2; -; Genomic_DNA.
DR EMBL; CR382132; CAG77799.1; -; Genomic_DNA.
DR RefSeq; XP_504992.1; XM_504992.1.
DR AlphaFoldDB; Q6C2X0; -.
DR SMR; Q6C2X0; -.
DR STRING; 284591.Q6C2X0; -.
DR EnsemblFungi; CAG77799; CAG77799; YALI0_F04422g.
DR GeneID; 2908883; -.
DR KEGG; yli:YALI0F04422g; -.
DR VEuPathDB; FungiDB:YALI0_F04422g; -.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; Q6C2X0; -.
DR OMA; NPYERSK; -.
DR OrthoDB; 55978at2759; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:EnsemblFungi.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12098; DD_R_ScPKA-like; 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:SF152; CAMP-DEPENDENT PROTEIN KINASE TYPE II 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 3: Inferred from homology;
KW cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..375
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205417"
FT REGION 28..142
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT REGION 41..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..258
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 208
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261..375
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 328
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> MAKRLMVISQPRRSFRILSNPV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 22..51
FT /note="QPTDILRFCADYFNERLAKREEADDDGPRS -> RSRPTFCGSARTISTNGW
FT PNEKRLTTTDPVP (in Ref. 1; CAE30452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 40268 MW; 5CC9693282420C34 CRC64;
MTLPPAYVDE LNLLNREVTT KQPTDILRFC ADYFNERLAK REEADDDGPR SKPLGGGFRE
PGFGSSSRST DGSLFRSSFA DTSSEGPGSA SSEPAAPFTR RTSVSAESIA PGAFAGAASG
VASNNLSAEQ LESLYKSVSH NFLFGNLDEE ACRSVLQSLQ EKKCDSGEKI ITQGDEGDYF
YIVESGAVEF IKDGVKVNSS GPGSSFGELA LMYNAPRAAT VVATQPCVLW SLDRVTFRKI
LLDGTHQRRS MYDGFLKEVP ILSDLGSYER NKLADALTSQ VVEPGTAVIT EGEAGDAFYL
VESGEAEVTK KGESGVVATL KQGDYFGEVA LLNDLPRQAT VTAKTKLKVA TLGKDGFQRL
LGPVLDHLKE NDPTK
//
