ID   KAPC1_CAEEL             Reviewed;         404 AA.
AC   P21137; O18310; O18311; Q9UB39; Q9XZP8; Q9XZP9; Q9XZQ0; Q9XZQ8; Q9XZQ9;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 3.
DT   04-NOV-2026, entry version 208.
DE   RecName: Full=cAMP-dependent protein kinase catalytic subunit;
DE            Short=PKA C;
DE            EC=2.7.11.11 {ECO:0000269|PubMed:9299544};
GN   Name=kin-1; ORFNames=ZK909.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND B),
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2;
RX   PubMed=2324104; DOI=10.1016/s0021-9258(19)39234-8;
RA   Gross R.E., Bagchi S., Lu X., Rubin C.S.;
RT   "Cloning, characterization, and expression of the gene for the catalytic
RT   subunit of cAMP-dependent protein kinase in Caenorhabditis elegans.
RT   Identification of highly conserved and unique isoforms generated by
RT   alternative splicing.";
RL   J. Biol. Chem. 265:6896-6907(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-73, AND ALTERNATIVE SPLICING.
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   [4]
RP   CATALYTIC ACTIVITY, AND MYRISTOYLATION.
RX   PubMed=9299544; DOI=10.1006/bbrc.1997.7165;
RA   Aspbury R.A., Fisher M.J., Rees H.H., Clegg R.A.;
RT   "N-Myristoylation of the catalytic subunit of cAMP-dependent protein kinase
RT   in the free-living nematode Caenorhabditis elegans.";
RL   Biochem. Biophys. Res. Commun. 238:523-527(1997).
RN   [5]
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).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CHARACTERIZATION OF ISOFORMS A; B; F
RP   AND K.
RX   PubMed=18077108; DOI=10.1016/j.gene.2007.10.034;
RA   Murray P., Clegg R.A., Rees H.H., Fisher M.J.;
RT   "siRNA-mediated knockdown of a splice variant of the PK-A catalytic subunit
RT   gene causes adult-onset paralysis in C. elegans.";
RL   Gene 408:157-163(2008).
RN   [7]
RP   MYRISTOYLATION AT GLY-2 (ISOFORMS H AND J).
RX   PubMed=22286028; DOI=10.1016/j.abb.2012.01.008;
RA   Clegg R.A., Bowen L.C., Bicknell A.V., Tabish M., Prescott M.C., Rees H.H.,
RA   Fisher M.J.;
RT   "Characterisation of the N'1 isoform of the cyclic AMP-dependent protein
RT   kinase (PK-A) catalytic subunit in the nematode, Caenorhabditis elegans.";
RL   Arch. Biochem. Biophys. 519:38-45(2012).
RN   [8]
RP   FUNCTION.
RX   PubMed=22887816; DOI=10.1534/genetics.112.143271;
RA   Kim S., Govindan J.A., Tu Z.J., Greenstein D.;
RT   "SACY-1 DEAD-Box helicase links the somatic control of oocyte meiotic
RT   maturation to the sperm-to-oocyte switch and gamete maintenance in
RT   Caenorhabditis elegans.";
RL   Genetics 192:905-928(2012).
RN   [9]
RP   FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-125 AND TRP-234.
RX   PubMed=24086161; DOI=10.1371/journal.pgen.1003831;
RA   Wang H., Sieburth D.;
RT   "PKA controls calcium influx into motor neurons during a rhythmic
RT   behavior.";
RL   PLoS Genet. 9:E1003831-E1003831(2013).
CC   -!- FUNCTION: Essential for larval development (PubMed:22887816). Controls
CC       the rhythmic contraction of enteric muscles probably by regulating G
CC       protein-coupled receptor aex-2-mediated calcium influx in GABAergic DVB
CC       neurons (PubMed:24086161). Plays a role in the control of oocyte
CC       meiotic maturation by gonadal sheath cells (PubMed:22887816).
CC       {ECO:0000269|PubMed:22887816, ECO:0000269|PubMed:24086161}.
CC   -!- FUNCTION: Isoforms a and b: May play a role in the regulation of
CC       neuromuscular junctions. {ECO:0000269|PubMed:18077108}.
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         Evidence={ECO:0000269|PubMed:9299544};
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         Evidence={ECO:0000269|PubMed:9299544};
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=e;
CC         IsoId=P21137-1; Sequence=Displayed;
CC       Name=a; Synonyms=Major;
CC         IsoId=P21137-2; Sequence=VSP_004751, VSP_004758;
CC       Name=b; Synonyms=Minor;
CC         IsoId=P21137-3; Sequence=VSP_004751;
CC       Name=c;
CC         IsoId=P21137-4; Sequence=VSP_004756, VSP_004757;
CC       Name=d;
CC         IsoId=P21137-5; Sequence=VSP_004750;
CC       Name=f;
CC         IsoId=P21137-6; Sequence=VSP_004752, VSP_004758;
CC       Name=g;
CC         IsoId=P21137-7; Sequence=VSP_004754, VSP_004758;
CC       Name=h;
CC         IsoId=P21137-8; Sequence=VSP_004753, VSP_004758;
CC       Name=i;
CC         IsoId=P21137-9; Sequence=VSP_004754;
CC       Name=j;
CC         IsoId=P21137-10; Sequence=VSP_004753;
CC       Name=k;
CC         IsoId=P21137-11; Sequence=VSP_004752;
CC       Name=l;
CC         IsoId=P21137-12; Sequence=VSP_004758;
CC       Name=m;
CC         IsoId=P21137-13; Sequence=VSP_004750, VSP_004758;
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels in the embryo. Expression
CC       increases after hatching and during larval stages and, despite a
CC       decrease, remains high in adults (at protein level).
CC       {ECO:0000269|PubMed:16806821, ECO:0000269|PubMed:2324104}.
CC   -!- PTM: Isoform h and isoform j are myristoylated.
CC       {ECO:0000269|PubMed:22286028, ECO:0000269|PubMed:9299544}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of isoforms a and b in
CC       neurons shows a temperature-sensitive adult onset paralysis of the
CC       distal part of the body resulting in the loss of backward movements and
CC       an inability to lay eggs. RNAi-mediated knockdown of isoforms f and k
CC       results in no obvious phenotype. {ECO:0000269|PubMed:18077108}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR   EMBL; M37119; AAA51610.1; -; Genomic_DNA.
DR   EMBL; M37114; AAA51610.1; JOINED; Genomic_DNA.
DR   EMBL; M37115; AAA51610.1; JOINED; Genomic_DNA.
DR   EMBL; M37116; AAA51610.1; JOINED; Genomic_DNA.
DR   EMBL; M37117; AAA51610.1; JOINED; Genomic_DNA.
DR   EMBL; M37118; AAA51610.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45613.1; -; Genomic_DNA.
DR   EMBL; Z82096; CAD45614.1; -; Genomic_DNA.
DR   EMBL; Z82096; CAD45615.1; -; Genomic_DNA.
DR   EMBL; Z82096; CAD45616.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45616.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45617.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45617.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45618.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45618.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45619.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45619.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45620.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45620.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45621.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45621.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45622.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45622.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAD45623.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAD45623.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAB05034.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAB05034.1; JOINED; Genomic_DNA.
DR   EMBL; Z82096; CAB05035.1; -; Genomic_DNA.
DR   EMBL; Z81511; CAB05035.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011936; CAB41353.1; -; mRNA.
DR   EMBL; AJ011937; CAB41354.1; -; mRNA.
DR   EMBL; AJ011938; CAB41355.1; -; mRNA.
DR   EMBL; AJ012354; CAB41349.1; -; mRNA.
DR   EMBL; AJ012355; CAB41350.1; -; mRNA.
DR   EMBL; AJ012356; CAB41351.1; -; mRNA.
DR   PIR; A35755; OKKWC1.
DR   PIR; B35755; OKKWC2.
DR   PIR; T21211; T21211.
DR   PIR; T21212; T21212.
DR   RefSeq; NP_001366905.1; NM_001381272.1. [P21137-3]
DR   RefSeq; NP_001367021.1; NM_001381275.2. [P21137-4]
DR   RefSeq; NP_001367022.1; NM_001381274.1. [P21137-5]
DR   RefSeq; NP_001367023.1; NM_001381271.1. [P21137-9]
DR   RefSeq; NP_001367024.1; NM_001381270.1. [P21137-10]
DR   RefSeq; NP_001367025.1; NM_001381273.1. [P21137-11]
DR   RefSeq; NP_493605.1; NM_061204.5. [P21137-2]
DR   RefSeq; NP_740954.1; NM_170958.6. [P21137-8]
DR   RefSeq; NP_740956.1; NM_170960.7. [P21137-7]
DR   RefSeq; NP_740958.1; NM_170962.5. [P21137-6]
DR   RefSeq; NP_740960.1; NM_170964.6. [P21137-12]
DR   RefSeq; NP_740961.1; NM_170965.3. [P21137-1]
DR   RefSeq; NP_740962.1; NM_170966.3. [P21137-13]
DR   AlphaFoldDB; P21137; -.
DR   SMR; P21137; -.
DR   BioGRID; 532725; 18.
DR   DIP; DIP-26547N; -.
DR   FunCoup; P21137; 2000.
DR   STRING; 6239.ZK909.2n.2; -.
DR   iPTMnet; P21137; -.
DR   PaxDb; 6239-ZK909.2n.2; -.
DR   PeptideAtlas; P21137; -.
DR   EnsemblMetazoa; ZK909.2a.1; ZK909.2a.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2b.1; ZK909.2b.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2b.2; ZK909.2b.2; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2c.1; ZK909.2c.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2d.1; ZK909.2d.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2e.1; ZK909.2e.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2f.1; ZK909.2f.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2g.1; ZK909.2g.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2h.1; ZK909.2h.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2i.1; ZK909.2i.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2j.1; ZK909.2j.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2k.1; ZK909.2k.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2l.1; ZK909.2l.1; WBGene00002189.
DR   EnsemblMetazoa; ZK909.2m.1; ZK909.2m.1; WBGene00002189.
DR   GeneID; 3565407; -.
DR   KEGG; cel:CELE_ZK909.2; -.
DR   UCSC; ZK909.2h.1; c. elegans.
DR   AGR; WB:WBGene00002189; -.
DR   CTD; 3565407; -.
DR   WormBase; ZK909.2a; CE15473; WBGene00002189; kin-1. [P21137-2]
DR   WormBase; ZK909.2b; CE15475; WBGene00002189; kin-1. [P21137-3]
DR   WormBase; ZK909.2c; CE31755; WBGene00002189; kin-1. [P21137-4]
DR   WormBase; ZK909.2d; CE31756; WBGene00002189; kin-1. [P21137-5]
DR   WormBase; ZK909.2e; CE31757; WBGene00002189; kin-1. [P21137-1]
DR   WormBase; ZK909.2f; CE31758; WBGene00002189; kin-1. [P21137-6]
DR   WormBase; ZK909.2g; CE31759; WBGene00002189; kin-1. [P21137-7]
DR   WormBase; ZK909.2h; CE31760; WBGene00002189; kin-1. [P21137-8]
DR   WormBase; ZK909.2i; CE31761; WBGene00002189; kin-1. [P21137-9]
DR   WormBase; ZK909.2j; CE31762; WBGene00002189; kin-1. [P21137-10]
DR   WormBase; ZK909.2k; CE31763; WBGene00002189; kin-1. [P21137-11]
DR   WormBase; ZK909.2l; CE31764; WBGene00002189; kin-1. [P21137-12]
DR   WormBase; ZK909.2m; CE31765; WBGene00002189; kin-1. [P21137-13]
DR   eggNOG; KOG0616; Eukaryota.
DR   InParanoid; P21137; -.
DR   OrthoDB; 63267at2759; -.
DR   PhylomeDB; P21137; -.
DR   BRENDA; 2.7.11.11; 1045.
DR   Reactome; R-CEL-163615; PKA activation.
DR   Reactome; R-CEL-164378; PKA activation in glucagon signalling.
DR   Reactome; R-CEL-180024; DARPP-32 events.
DR   Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-CEL-392517; Rap1 signalling.
DR   Reactome; R-CEL-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CEL-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR   Reactome; R-CEL-5578775; Ion homeostasis.
DR   Reactome; R-CEL-5610787; Hedgehog 'off' state.
DR   Reactome; R-CEL-9634597; GPER1 signaling.
DR   Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR   Reactome; R-CEL-9837999; Mitochondrial protein degradation.
DR   Reactome; R-CEL-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells.
DR   PRO; PR:P21137; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002189; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   ExpressionAtlas; P21137; baseline and differential.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; ISS:WormBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:WormBase.
DR   GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:WormBase.
DR   CDD; cd14209; STKc_PKA; 1.
DR   FunFam; 3.30.200.20:FF:000005; cAMP-dependent protein kinase catalytic subunit; 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; 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:SF153; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT 1; 1.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 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   Alternative splicing; ATP-binding; cAMP; Kinase; Lipoprotein; Myristate;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..404
FT                   /note="cAMP-dependent protein kinase catalytic subunit"
FT                   /id="PRO_0000086067"
FT   DOMAIN          81..335
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         87..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         376
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..72
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   FKEFLDKAREDFKQRWENPA -> MEEEEWRRRLSAAIRREDEGSLEEDEEDEGFILHP
FT                   LCRTGPLQMTVKASNSTTTLTPSSTTTTSPSMPSSPSDSPSDDFSDDTNTSGVFPLTTA
FT                   LSFPVAPLSPRNTTSSITTGLVKKRRSSSSPEDICREKIPHILLKTSSGVVVPLASRGQ
FT                   RAPAITLQNPPPSAAIRTVPPPSFSTFSVRSLPFKTPNCGSKDDTDAENMEGLDDDYLR
FT                   QPTTSTSAPVSPIDHRQVRRGGRGVVVESQVPNFTAEIFWLKTQLSDHWSMKWLF (in
FT                   isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004756"
FT   VAR_SEQ         1..53
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   F -> MLKFLKPKSSDEGSSKDNKNSASL (in isoform a and isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004751"
FT   VAR_SEQ         1..53
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   F -> MLSSSFFRGSMKERKNEALKNHKSKYISGGYLETV (in isoform f and
FT                   isoform k)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004752"
FT   VAR_SEQ         1..53
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   F -> MGSMVFIV (in isoform g and isoform i)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004754"
FT   VAR_SEQ         1..53
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   F -> MGNAASGGSSGGGGSARRGNGGGNNGSDYNNAMVFSNGRLAAAETI (in
FT                   isoform h and isoform j)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004753"
FT   VAR_SEQ         1..52
FT                   /note="MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVED
FT                   -> MSSSSNKKVQVKF (in isoform d and isoform m)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004750"
FT   VAR_SEQ         348..404
FT                   /note="ITPPSFSKGESNGRLFEALYPRVDGPADTRHFVEEVQEPTEFVIAATPQLEE
FT                   LFVEF -> VSSYPI (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004757"
FT   VAR_SEQ         349..404
FT                   /note="TPPSFSKGESNGRLFEALYPRVDGPADTRHFVEEVQEPTEFVIAATPQLEEL
FT                   FVEF -> EAPFLPKCRGPGDASNFDDYEEEPLRISGTEKCAKEFAEF (in
FT                   isoform a, isoform f, isoform g, isoform h, isoform l and
FT                   isoform m)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004758"
FT   MUTAGEN         125
FT                   /note="H->Q: Loss of interaction with kin-2 resulting in
FT                   constitutive activation; when associated with R-234 (in
FT                   isoform a)."
FT                   /evidence="ECO:0000269|PubMed:24086161"
FT   MUTAGEN         234
FT                   /note="W->R: Loss of interaction with kin-2 resulting in
FT                   constitutive activation; when associated with Q-125 (in
FT                   isoform a)."
FT                   /evidence="ECO:0000269|PubMed:24086161"
FT   CONFLICT        148
FT                   /note="F -> L (in Ref. 1; AAA51610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="I -> V (in Ref. 1; AAA51610)"
FT                   /evidence="ECO:0000305"
FT   INIT_MET        P21137-8:1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   LIPID           P21137-8:2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:22286028"
FT   INIT_MET        P21137-10:1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   LIPID           P21137-10:2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:22286028"
SQ   SEQUENCE   404 AA;  46346 MW;  A7AF458E47B58876 CRC64;
     MPTRLDIVGN LQFSSSTDNG DEDQEADVTA CFVLPSPSSF SKLSILDDPV EDFKEFLDKA
     REDFKQRWEN PAQNTACLDD FDRIKTLGTG SFGRVMLVKH KQSGNYYAMK ILDKQKVVKL
     KQVEHTLNEK RILQAIDFPF LVNMTFSFKD NSNLYMVLEF ISGGEMFSHL RRIGRFSEPH
     SRFYAAQIVL AFEYLHSLDL IYRDLKPENL LIDSTGYLKI TDFGFAKRVK GRTWTLCGTP
     EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS GKVKFPSHFS
     NELKDLLKNL LQVDLTKRYG NLKNGVADIK NHKWFGSTDW IAIYQKKITP PSFSKGESNG
     RLFEALYPRV DGPADTRHFV EEVQEPTEFV IAATPQLEEL FVEF
//