KAPC2_CAEEL
ID KAPC2_CAEEL Reviewed; 398 AA.
AC Q7JP68; Q20541; Q8MQ39; Q95ZT2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=cAMP-dependent protein kinase, catalytic subunit-like {ECO:0000303|PubMed:10085246};
DE EC=2.7.11.11 {ECO:0000250|UniProtKB:P21137};
GN ORFNames=F47F2.1 {ECO:0000312|WormBase:F47F2.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|EMBL:CAB41352.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-398.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB41352.1};
RX PubMed=10085246; DOI=10.1042/bj3390209;
RA Tabish M., Clegg R.A., Rees H.H., Fisher M.J.;
RT "Organization and alternative splicing of the Caenorhabditis elegans cyclic
RT AMP-dependent protein kinase (PK-A) catalytic subunit gene (kin-1).";
RL Biochem. J. 339:209-216(1999).
RN [3] {ECO:0000305}
RP 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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:F47F2.1b};
CC IsoId=Q7JP68-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:F47F2.1c};
CC IsoId=Q7JP68-2; Sequence=VSP_057511;
CC Name=a {ECO:0000312|WormBase:F47F2.1a};
CC IsoId=Q7JP68-3; Sequence=VSP_057510;
CC -!- DEVELOPMENTAL STAGE: No obvious expression before embryo hatching but
CC is expressed at later stages (at protein level).
CC {ECO:0000269|PubMed:16806821}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. cAMP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FO081408; CCD71418.1; -; Genomic_DNA.
DR EMBL; FO081408; CCD71419.1; -; Genomic_DNA.
DR EMBL; FO081408; CCD71417.1; -; Genomic_DNA.
DR EMBL; AJ012357; CAB41352.1; ALT_INIT; mRNA.
DR PIR; T16391; T16391.
DR RefSeq; NP_508671.2; NM_076270.3. [Q7JP68-1]
DR RefSeq; NP_508672.1; NM_076271.3.
DR RefSeq; NP_741759.1; NM_171660.3.
DR AlphaFoldDB; Q7JP68; -.
DR SMR; Q7JP68; -.
DR STRING; 6239.F47F2.1b; -.
DR EPD; Q7JP68; -.
DR PaxDb; Q7JP68; -.
DR EnsemblMetazoa; F47F2.1b.1; F47F2.1b.1; WBGene00018569. [Q7JP68-1]
DR EnsemblMetazoa; F47F2.1c.1; F47F2.1c.1; WBGene00018569. [Q7JP68-2]
DR EnsemblMetazoa; F47F2.1c.2; F47F2.1c.2; WBGene00018569. [Q7JP68-2]
DR EnsemblMetazoa; F47F2.1c.3; F47F2.1c.3; WBGene00018569. [Q7JP68-2]
DR EnsemblMetazoa; F47F2.1c.4; F47F2.1c.4; WBGene00018569. [Q7JP68-2]
DR GeneID; 180673; -.
DR UCSC; F47F2.1b; c. elegans.
DR CTD; 180673; -.
DR WormBase; F47F2.1a; CE27166; WBGene00018569; -. [Q7JP68-3]
DR WormBase; F47F2.1b; CE37114; WBGene00018569; -. [Q7JP68-1]
DR WormBase; F47F2.1c; CE31171; WBGene00018569; -. [Q7JP68-2]
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000159832; -.
DR InParanoid; Q7JP68; -.
DR OMA; WACGILC; -.
DR OrthoDB; 963519at2759; -.
DR PhylomeDB; Q7JP68; -.
DR PRO; PR:Q7JP68; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018569; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q7JP68; baseline and differential.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:WormBase.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Alternative splicing; ATP-binding; cAMP; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..398
FT /note="cAMP-dependent protein kinase, catalytic subunit-
FT like"
FT /id="PRO_0000432401"
FT DOMAIN 90..344
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 345..398
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 96..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057510"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057511"
FT CONFLICT 27
FT /note="L -> Q (in Ref. 2; CAB41352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45893 MW; 6FF2B21775F3212F CRC64;
MVILSHHKRS PPLLMRLFRI CRFFRRLMSS STSSVESVED ESCSNECSAS FTFDTNNNSR
GNNQVNELAE ETHMKLSITP TRESFSLSQL ERIITIGKGT FGRVELARDK ITGAHYALKV
LNIRRVVDMR QTQHVHNEKR VLLQLKHPFI VKMYASEKDS NHLYMIMEFV PGGEMFSYLR
ASRSFSNSMA RFYASEIVCA LEYIHSLGIV YRDLKPENLM LSKEGHIKMA DFGFAKELRD
RTYTICGTPD YLAPESLART GHNKGVDWWA LGILIYEMMV GKPPFRGKTT SEIYDAIIEH
KLKFPRSFNL AAKDLVKKLL EVDRTQRIGC MKNGTQDVKD HKWFEKVNWD DTLHLRVEPP
IVPTLYHPGD TGNFDDYEED TTGGPLCSQR DRDLFAEW
