ID   KAPR_KLULA              Reviewed;         466 AA.
AC   Q6CPK7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE            Short=PKA regulatory subunit;
GN   Name=PKAR; OrderedLocusNames=KLLA0E04070g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99219.1; -; Genomic_DNA.
DR   RefSeq; XP_454132.1; XM_454132.1.
DR   AlphaFoldDB; Q6CPK7; -.
DR   SMR; Q6CPK7; -.
DR   STRING; 28985.XP_454132.1; -.
DR   PRIDE; Q6CPK7; -.
DR   EnsemblFungi; CAG99219; CAG99219; KLLA0_E04181g.
DR   GeneID; 2893813; -.
DR   KEGG; kla:KLLA0_E04181g; -.
DR   eggNOG; KOG1113; Eukaryota.
DR   HOGENOM; CLU_018310_0_1_1; -.
DR   InParanoid; Q6CPK7; -.
DR   OMA; YFIEYGE; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
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..466
FT                   /note="cAMP-dependent protein kinase regulatory subunit"
FT                   /id="PRO_0000205410"
FT   REGION          25..231
FT                   /note="Dimerization and phosphorylation"
FT                   /evidence="ECO:0000255"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         232..347
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         297
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..466
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         416
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  51276 MW;  60BE1A826165C6BE CRC64;
     MATYQTELDL FKNEVEQKQP NDFLQFAANY FTKRLEQQRT FVRNQESLAL SKGIVLFPST
     SKHDSVAASS ASLSHGSSKA NASQSGISSS GVDEDVLFKS PFVDRGPHST HIVDHLDSTH
     SNTTASPAKA SGGDAPGIFK GNFNVGTESQ RKVNSSVDPM APEPTATTHS FPRRSVVNPK
     PLPINFNAQR RTSVSGETLQ PDHLDDWKPE NFQEKSPEQV SRLEKAVGKN FLFNKLDSDS
     KKLVINSLEE KSIPQGKEII KQGDEGDYFY IVEDGTVEFY VNNQKVNTSG PGSSFGELAL
     MYNSPRAATV IASTDCILWA LDRLTFRRIL LGGSFKKRIL YDDLLKNIPI LKSLSTYDRA
     KLADALDTEY YEAGQTIIKE GDTGENFYFI EYGEADVSQE GKGVITKLGK GDYFGEVALL
     NDLPRQATVT ATARTKVATL GKSGFQRLLG PVVDVLKLND PTRSKH