KAPC1_CAEBR
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 03-AUG-2022, entry version 102.
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}.
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DR EMBL; HE601474; CAP36907.1; -; Genomic_DNA.
DR RefSeq; XP_002640742.1; XM_002640696.1.
DR AlphaFoldDB; A8XW88; -.
DR SMR; A8XW88; -.
DR STRING; 6238.CBG19814; -.
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; GNARYNK; -.
DR OrthoDB; 963519at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd14209; STKc_PKA; 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 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; 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
