KAPR_DICDI
ID KAPR_DICDI Reviewed; 327 AA.
AC P05987; Q54WN1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE AltName: Full=Protein kinase A, regulatory subunit;
DE AltName: Full=Rapid development protein C;
GN Name=pkaR; Synonyms=rdeC; ORFNames=DDB_G0279413;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3467359; DOI=10.1073/pnas.84.1.6;
RA Mutzel R., Lacombe M.-L., Simon M.-N., de Gunzburg J., Veron M.;
RT "Cloning and cDNA sequence of the regulatory subunit of cAMP-dependent
RT protein kinase from Dictyostelium discoideum.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6-10(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP MUTAGENESIS OF ALA-30.
RX PubMed=1312226; DOI=10.1038/356171a0;
RA Simon M.-N., Pelegrini O., Veron M., Kay R.R.;
RT "Mutation of protein kinase A causes heterochronic development of
RT Dictyostelium.";
RL Nature 356:171-172(1992).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=9582274; DOI=10.1093/emboj/17.10.2809;
RA Chang W.-T., Thomason P.A., Gross J.D., Neweil P.C.;
RT "Evidence that the RdeA protein is a component of a multistep phosphorelay
RT modulating rate of development in Dictyostelium.";
RL EMBO J. 17:2809-2816(1998).
CC -!- SUBUNIT: In Dictyostelium the holoenzyme is a dimer composed of a
CC regulatory (R) and a catalytic (C) subunit. In the presence of cAMP it
CC dissociates into the active C subunit and an R monomer. In other
CC eukaryotes the holoenzyme is a tetramer composed of 2 regulatory (R)
CC and 2 catalytic (C) subunits. In the presence of cAMP it dissociates
CC into active monomeric C subunits and an R dimer.
CC -!- DOMAIN: Lacks the N-terminal domain required for the association of
CC regulatory subunits into dimers in other eukaryotes.
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.
CC -!- DISRUPTION PHENOTYPE: AcaA and pkaR double mutant shows no abolition of
CC the ability to sporulate. {ECO:0000269|PubMed:9582274}.
CC -!- MISCELLANEOUS: In D.discoideum each R subunit carries only 1 high-
CC affinity cAMP binding site (2 in other eukaryotes).
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; M15081; AAA33236.1; -; mRNA.
DR EMBL; AAFI02000031; EAL67645.1; -; Genomic_DNA.
DR PIR; A29076; OKDDRC.
DR RefSeq; XP_641686.1; XM_636594.1.
DR AlphaFoldDB; P05987; -.
DR SMR; P05987; -.
DR STRING; 44689.DDB0214950; -.
DR PaxDb; P05987; -.
DR EnsemblProtists; EAL67645; EAL67645; DDB_G0279413.
DR GeneID; 8622094; -.
DR KEGG; ddi:DDB_G0279413; -.
DR dictyBase; DDB_G0279413; pkaR.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_018310_1_1_1; -.
DR InParanoid; P05987; -.
DR OMA; YDNWSPP; -.
DR PhylomeDB; P05987; -.
DR PRO; PR:P05987; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:dictyBase.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0030552; F:cAMP binding; IDA:dictyBase.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:dictyBase.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:dictyBase.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:dictyBase.
DR GO; GO:0061939; P:c-di-GMP signaling; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:dictyBase.
DR GO; GO:0045859; P:regulation of protein kinase activity; IMP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR GO; GO:0031285; P:regulation of sorocarp stalk cell differentiation; IGI:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
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 PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
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 1: Evidence at protein level;
KW cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..327
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205395"
FT REGION 1..65
FT /note="Dimerization and phosphorylation"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..31
FT /note="Pseudophosphorylation motif"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..188
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 136
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 145
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /ligand_note="high affinity"
FT BINDING 189..327
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT BINDING 262
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT BINDING 271
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MUTAGEN 30
FT /note="A->T: In rdeC; aggregation is followed abruptly by
FT the maturation of spore and stalk cells. This is a due to
FT mutation(s) in the R subunit. The mutant R subunit binds
FT cAMP but inhibits poorly the enzymatic activity of the C
FT subunit."
FT /evidence="ECO:0000269|PubMed:1312226"
SQ SEQUENCE 327 AA; 36836 MW; D76BF40E3F2E2CA1 CRC64;
MTNNISHNQK ATEKVEAQNN NNITRKRRGA ISSEPLGDKP ATPLPNIPKT VETQQRLEQA
LSNNIMFSHL EEEERNVVFL AMVEVLYKAG DIIIKQGDEG DLFYVIDSGI CDIYVCQNGG
SPTLVMEVFE GGSFGELALI YGSPRAATVI ARTDVRLWAL NGATYRRILM DQTIKKRKLY
EEFLEKVSIL RHIDKYERVS LADALEPVNF QDGEVIVRQG DPGDRFYIIV EGKVVVTQET
VPGDHSTSHV VSELHPSDYF GEIALLTDRP RAATVTSIGY TKCVELDRQR FNRLCGPIDQ
MLRRNMETYN QFLNRPPSSP NLTSQKS
