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 08-MAY-2019, entry version 85. 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., RA D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R., RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., RA Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for RT comparative 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., RA Fisher M.J.; RT "Expression of multiple isoforms of the cAMP-dependent protein kinase RT (PK-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 CC coupled receptor aex-2-mediated calcium influx in GABAergic DVB CC neurons. Plays a role in the control of oocyte meiotic maturation CC by gonadal sheath cells. May play a role in the regulation of CC neuromuscular junctions. {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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.11; 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 CC two catalytic subunits. {ECO:0000250|UniProtKB:P51817}. CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the embryo. CC Expression increases after hatching and during larval stages and CC is followed by a decrease in adults (at protein level). CC {ECO:0000269|PubMed:16806821}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. 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; HE601474; CAP36907.1; -; Genomic_DNA. DR RefSeq; XP_002640742.1; XM_002640696.1. DR SMR; A8XW88; -. DR STRING; 6238.CBG19814; -. DR PRIDE; A8XW88; -. DR EnsemblMetazoa; CBG19814d; CBG19814d; WBGene00038974. DR GeneID; 8582736; -. DR KEGG; cbr:CBG19814; -. DR CTD; 8582736; -. DR WormBase; CBG19814; CBP04602; WBGene00038974; Cbr-kin-1. DR eggNOG; KOG0616; Eukaryota. DR eggNOG; ENOG410XPQQ; LUCA. DR HOGENOM; HOG000233033; -. DR InParanoid; A8XW88; -. DR KO; K04345; -. DR OMA; SLFDHYP; -. DR OrthoDB; 963519at2759; -. DR Proteomes; UP000008549; Chromosome I. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR039083; PKA_C-beta. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24353:SF116; PTHR24353:SF116; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 374 cAMP-dependent protein kinase catalytic FT subunit. {ECO:0000250|UniProtKB:P21137}. FT /FTId=PRO_0000432402. FT DOMAIN 52 305 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 58 66 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 175 175 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 81 81 ATP. {ECO:0000255|PROSITE- FT 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 //