KAPC_DICDI
ID KAPC_DICDI Reviewed; 648 AA.
AC P34099; Q54QA9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit;
DE EC=2.7.11.11;
DE AltName: Full=Dd GPK2;
DE AltName: Full=DdPK3;
GN Name=pkaC; Synonyms=PK2, PK3; ORFNames=DDB_G0283907;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=1864510; DOI=10.1016/0378-1119(91)90538-m;
RA Buerki E., Anjard C., Scholder J.-C., Reymond C.D.;
RT "Isolation of two genes encoding putative protein kinases regulated during
RT Dictyostelium discoideum development.";
RL Gene 102:57-65(1991).
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 CHARACTERIZATION.
RX PubMed=8373760; DOI=10.1021/bi00088a003;
RA Anjard C., Etchebehere L., Pinaud S., Veron M., Reymond C.D.;
RT "An unusual catalytic subunit for the cAMP-dependent protein kinase of
RT Dictyostelium discoideum.";
RL Biochemistry 32:9532-9538(1993).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=AX3;
RX PubMed=1332055; DOI=10.1073/pnas.89.22.10701;
RA Mann S.K.O., Yonemoto W.M., Taylor S.S., Firtel R.A.;
RT "DdPK3, which plays essential roles during Dictyostelium development,
RT encodes the catalytic subunit of cAMP-dependent protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10701-10705(1992).
CC -!- FUNCTION: Essential for differentiation and fruit morphogenesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.11;
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.
CC -!- DEVELOPMENTAL STAGE: CAPK activity is low in vegetatively growing
CC amoebae, increases during development of aggregation and reaches a
CC maximum at culmination.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {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; M38703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFI02000058; EAL65441.1; -; Genomic_DNA.
DR PIR; JQ1150; JQ1150.
DR RefSeq; XP_638835.1; XM_633743.1.
DR AlphaFoldDB; P34099; -.
DR SMR; P34099; -.
DR STRING; 44689.DDB0215408; -.
DR PaxDb; P34099; -.
DR EnsemblProtists; EAL65441; EAL65441; DDB_G0283907.
DR GeneID; 8624359; -.
DR KEGG; ddi:DDB_G0283907; -.
DR dictyBase; DDB_G0283907; pkaC.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P34099; -.
DR OMA; RDNGPFI; -.
DR PhylomeDB; P34099; -.
DR BRENDA; 2.7.11.11; 1939.
DR PRO; PR:P34099; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:dictyBase.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:dictyBase.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:dictyBase.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IDA:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0061939; P:c-di-GMP signaling; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:dictyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:dictyBase.
DR GO; GO:0010737; P:protein kinase A signaling; IMP:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:dictyBase.
DR GO; GO:1905301; P:regulation of macropinocytosis; IMP:dictyBase.
DR GO; GO:1901261; P:regulation of sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031285; P:regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; IGI:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..648
FT /note="cAMP-dependent protein kinase catalytic subunit"
FT /id="PRO_0000086068"
FT DOMAIN 336..590
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 591..648
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 342..350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 490
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 342
FT /note="I -> L (in Ref. 1; M38703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 74458 MW; 20FBC07E4A82142C CRC64;
MSNSNNNSSS GNHNSTTINN PKVNVYSNIP NSTTYTYGSG GGGTLSGNNT NNNNTNNNNN
NNNNSSGDNK NHSPVTSATD RLTKMDIEEK WDNKNYEKDE REKSPLFHIL ASNLNSFGNF
KVPSTFSLTP PEPNKQQQPQ QQPQQQQPQQ QQPQQQQPQQ QQQQQPQQQQ QPQQQLQQNN
QQQQQQLQQQ QLQQQLQQQQ QQQQQQQQQQ QQKQQKQQQQ QQQHLHQDGI VNTPSTTQTS
TTTTTTTTTT NPHTSGLSLQ HAHSSYTPSN VLHSPTHFQS SLPTRLDTNP ITTPIRQQQQ
SQQQLQQQQL QQIPPPTVNS FFLPPPVNAR ERLKEFKQIR VIGTGTFGKV YLIQNTKDGC
YYAMKCLNKA YVVQLKQVEH LNSEKSILSS IHHPFIVNLY QAFQDEKKLY LLFEYVAGGE
VFTHLRKSMK FSNSTAKFYA AEIVLALEFL HKQNIVYRDL KPENLLIDNQ GHIKITDFGF
AKRVEDRTFT LCGTPEYLAP EIIQSKGHGK AVDWWALGIL IFEMLAGYPP FYDDDTFAIY
NKILAGRITF PLGFDVDAKD LIKRLLTADR TRRLGALKDG ALDVKNHRWF SDINWERLYQ
RRDNGPFIPK IQHQGDSSNF EMYDEEEMVE EPPSSNYVDP YAHLFKDF
