ID KAPC1_CAEBR Reviewed; 374 AA. AC A8XW88; DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 29-MAY-2024, entry version 109. DE RecName: Full=cAMP-dependent protein kinase catalytic subunit {ECO:0000250|UniProtKB:P21137}; DE Short=PKA C {ECO:0000250|UniProtKB:P21137}; DE EC=2.7.11.11 {ECO:0000250|UniProtKB:P21137}; GN Name=kin-1 {ECO:0000312|WormBase:CBG19814}; GN ORFNames=CBG19814 {ECO:0000312|WormBase:CBG19814}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549}; RN [1] {ECO:0000312|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000312|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R.M., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). RN [2] {ECO:0000305} RP IDENTIFICATION, AND DEVELOPMENTAL STAGE. RX PubMed=16806821; DOI=10.1016/j.cellsig.2006.05.002; RA Bowen L.C., Bicknell A.V., Tabish M., Clegg R.A., Rees H.H., Fisher M.J.; RT "Expression of multiple isoforms of the cAMP-dependent protein kinase (PK- RT A) catalytic subunit in the nematode, Caenorhabditis elegans."; RL Cell. Signal. 18:2230-2237(2006). CC -!- FUNCTION: Essential for larval development. Controls the rhythmic CC contraction of enteric muscles probably by regulating G-protein coupled CC receptor aex-2-mediated calcium influx in GABAergic DVB neurons. Plays CC a role in the control of oocyte meiotic maturation by gonadal sheath CC cells. May play a role in the regulation of neuromuscular junctions. CC {ECO:0000250|UniProtKB:P21137}. 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 Evidence={ECO:0000250|UniProtKB:P21137}; 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; Evidence={ECO:0000250|UniProtKB:P21137}; CC -!- ACTIVITY REGULATION: Binding of cAMP to kin-2 regulatory subunits CC induces dissociation of the heterotetramer. The released catalytic CC subunits are active and able to phosphorylate their substrates. CC {ECO:0000250|UniProtKB:P51817}. CC -!- SUBUNIT: Heterotetramer composed of two regulatory subunits and two CC catalytic subunits. {ECO:0000250|UniProtKB:P51817}. CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the embryo. Expression CC increases after hatching and during larval stages and is followed by a CC decrease in adults (at protein level). {ECO:0000269|PubMed:16806821}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC 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; HE601474; CAP36907.1; -; Genomic_DNA. DR RefSeq; XP_002640742.1; XM_002640696.1. DR AlphaFoldDB; A8XW88; -. DR SMR; A8XW88; -. DR STRING; 6238.A8XW88; -. DR EnsemblMetazoa; CBG19814d.1; CBG19814d.1; WBGene00038974. DR GeneID; 8582736; -. DR KEGG; cbr:CBG_19814; -. DR CTD; 8582736; -. DR WormBase; CBG19814; CBP04602; WBGene00038974; Cbr-kin-1. DR eggNOG; KOG0616; Eukaryota. DR HOGENOM; CLU_000288_63_5_1; -. DR InParanoid; A8XW88; -. DR OMA; FAKEVQD; -. DR OrthoDB; 10768at2759; -. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central. DR CDD; cd14209; STKc_PKA; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 InterPro; IPR044109; STKc_PKA. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR PANTHER; PTHR24353:SF152; UT01108P-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..374 FT /note="cAMP-dependent protein kinase catalytic subunit" FT /evidence="ECO:0000250|UniProtKB:P21137" FT /id="PRO_0000432402" FT DOMAIN 52..305 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 58..66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 81 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 374 AA; 43045 MW; 0DD389B0D230300B CRC64; MLKFLKPKSS DEGSSKDNKS AASLKEFLDK AREDFKQRWE NPAQNTACLD DFDRIKTLGT GSFGRVMLVK HKQSGNYYAM KILDKQKVVK LKQVEHTLNE KRILQAIDFP FLVNMTFSFK DNSNLYMVLE FISGGEMFSH LRRIGRFSEP HSRFYAAQIV LAFEYLHSLD LIYRDLKPEN LLIDSTGYLK ITDFGFAKRV KGRTWTLCGT PEYLAPEIIL SKGYNKAVDW WALGVLIYEM AAGYPPFFAD QPIQIEKIVS GKVKFPSHFS NELKDLLKNL LQVDLTKRYG NLKNGVADIK NHKWFGSTDW IAIYQRKIKP PSFSNGEPKG RLFEALYARV DGPADTRHFV EEVQEPTQFV IASTCQLPEL FEDF //