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KAPR_YARLI
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   03-AUG-2022, entry version 105.
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}.
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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; 4952.CAG77799; -.
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; REAVSHN; -.
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:0005737; C:cytoplasm; 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:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:EnsemblFungi.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:EnsemblFungi.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IEA:EnsemblFungi.
DR   GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; 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   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   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
 
 
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