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 04-NOV-2026, entry version 163. 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 (Social amoeba). 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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 FunCoup; P34099; 1. DR STRING; 44689.P34099; -. DR PaxDb; 44689-P34099; -. DR GeneID; 8624359; -. DR KEGG; ddi:DDB_G0283907; -. DR dictyBase; DDB_G0283907; pkaC. DR VEuPathDB; AmoebaDB:DDB_G0283907; -. DR eggNOG; KOG0616; Eukaryota. DR HOGENOM; CLU_000288_63_5_1; -. DR InParanoid; P34099; -. DR OMA; CLTCMQL; -. DR PhylomeDB; P34099; -. DR BRENDA; 2.7.11.11; 1939. DR Reactome; R-DDI-163615; PKA activation. DR Reactome; R-DDI-164378; PKA activation in glucagon signalling. DR Reactome; R-DDI-180024; DARPP-32 events. DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-DDI-392517; Rap1 signalling. DR Reactome; R-DDI-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-DDI-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase. DR Reactome; R-DDI-5610787; Hedgehog 'off' state. DR Reactome; R-DDI-8963896; HDL assembly. DR Reactome; R-DDI-9634597; GPER1 signaling. DR Reactome; R-DDI-9837999; Mitochondrial protein degradation. DR Reactome; R-DDI-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells. 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; IBA:GO_Central. 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:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. 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; IDA:dictyBase. DR GO; GO:0071964; P:establishment of cell polarity regulating cell shape; IMP:dictyBase. DR GO; GO:0140986; P:G protein-coupled chemorepellent receptor signaling pathway; 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:0140676; P:oscillatory cAMP signaling; IDA:dictyBase. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:dictyBase. DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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:1904643; P:response to curcumin; IDA:dictyBase. DR GO; GO:0007165; P:signal transduction; IGI:dictyBase. DR GO; GO:0007264; P:small GTPase-mediated signal transduction; IMP: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 CDD; cd05580; STKc_PKA_like; 1. DR FunFam; 3.30.200.20:FF:000042; Aurora kinase A; 1. DR FunFam; 1.10.510.10:FF:000005; cAMP-dependent protein kinase catalytic subunit alpha; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24353:SF37; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT PRKX; 1. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 1..20 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..67 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..175 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..254 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..290 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 //