ID KAPR_EREGS Reviewed; 458 AA.
AC Q75AM2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=PKAR; OrderedLocusNames=ADL099C;
OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51821.1; -; Genomic_DNA.
DR RefSeq; NP_983997.1; NM_209350.1.
DR AlphaFoldDB; Q75AM2; -.
DR SMR; Q75AM2; -.
DR STRING; 284811.Q75AM2; -.
DR EnsemblFungi; AAS51821; AAS51821; AGOS_ADL099C.
DR GeneID; 4620139; -.
DR KEGG; ago:AGOS_ADL099C; -.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; Q75AM2; -.
DR OMA; MPYERSK; -.
DR OrthoDB; 55978at2759; -.
DR Proteomes; UP000000591; Chromosome IV.
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; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 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; 1.
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..458
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205399"
FT REGION 28..222
FT /note="Dimerization and phosphorylation"
FT /evidence="ECO:0000255"
FT BINDING 223..338
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 288
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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 341..457
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 407
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 51335 MW; E5212B8159BA68D3 CRC64;
MVLSQEHRDL LDAFQKEVEQ RRPGDLLQFA ANYFNKKLEE ERLFVRSQES LALSKGVVLF
PGSEGCGANR AAGSPDARKT GEDEDVMFKL PFVEHDPHSR HIYDDNKHGH DSCDPHTSFS
REPGAGLFQG GYNMGQEAQK EAQTDFDPKA SEVSSILKQR NVPRKSGVNS KPLPMNFNAE
RRTSVSGETL KPDHFSDWTP ENYTEKTREQ LKGLESAVGK NFLFNKLDSD SKTLVINSLE
EKLVSKGQEI IRQGDEGDYF YIVEKGTVDF FLDDRKVNTY GPGSCFGELA LMYNSPRAVT
AVAATDCVLW ALDRLTFRRI LLSGSFKKRL LYDDFLKSMP LLKSLSNYDR AKLADALETE
YYEAGQQVIS EGDVGENFYL IEYGEADVSK RGVGVVQHLK KGDYFGEVAL LNDLPRQATV
TATTKLKVAT LGKSGFQRLL GPVVEVLRLN DPTRADKR
//
