KAPC1_CAEEL
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 03-AUG-2022, entry version 189.
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=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:0000269|PubMed:9299544};
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: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_493605.1; NM_061204.3. [P21137-2]
DR RefSeq; NP_493606.1; NM_061205.3.
DR RefSeq; NP_740954.1; NM_170958.3. [P21137-8]
DR RefSeq; NP_740955.1; NM_170959.4.
DR RefSeq; NP_740956.1; NM_170960.3. [P21137-7]
DR RefSeq; NP_740957.1; NM_170961.1.
DR RefSeq; NP_740958.1; NM_170962.3. [P21137-6]
DR RefSeq; NP_740959.1; NM_170963.1.
DR RefSeq; NP_740960.1; NM_170964.3. [P21137-12]
DR RefSeq; NP_740961.1; NM_170965.1. [P21137-1]
DR RefSeq; NP_740962.1; NM_170966.1. [P21137-13]
DR RefSeq; NP_740963.1; NM_170967.3.
DR RefSeq; NP_740964.1; NM_170968.3.
DR AlphaFoldDB; P21137; -.
DR SMR; P21137; -.
DR BioGRID; 532725; 17.
DR DIP; DIP-26547N; -.
DR STRING; 6239.ZK909.2c; -.
DR EPD; P21137; -.
DR PaxDb; P21137; -.
DR PeptideAtlas; P21137; -.
DR EnsemblMetazoa; ZK909.2a.1; ZK909.2a.1; WBGene00002189. [P21137-2]
DR EnsemblMetazoa; ZK909.2b.1; ZK909.2b.1; WBGene00002189. [P21137-3]
DR EnsemblMetazoa; ZK909.2b.2; ZK909.2b.2; WBGene00002189. [P21137-3]
DR EnsemblMetazoa; ZK909.2c.1; ZK909.2c.1; WBGene00002189. [P21137-4]
DR EnsemblMetazoa; ZK909.2d.1; ZK909.2d.1; WBGene00002189. [P21137-5]
DR EnsemblMetazoa; ZK909.2e.1; ZK909.2e.1; WBGene00002189. [P21137-1]
DR EnsemblMetazoa; ZK909.2f.1; ZK909.2f.1; WBGene00002189. [P21137-6]
DR EnsemblMetazoa; ZK909.2g.1; ZK909.2g.1; WBGene00002189. [P21137-7]
DR EnsemblMetazoa; ZK909.2h.1; ZK909.2h.1; WBGene00002189. [P21137-8]
DR EnsemblMetazoa; ZK909.2i.1; ZK909.2i.1; WBGene00002189. [P21137-9]
DR EnsemblMetazoa; ZK909.2j.1; ZK909.2j.1; WBGene00002189. [P21137-10]
DR EnsemblMetazoa; ZK909.2k.1; ZK909.2k.1; WBGene00002189. [P21137-11]
DR EnsemblMetazoa; ZK909.2l.1; ZK909.2l.1; WBGene00002189. [P21137-12]
DR EnsemblMetazoa; ZK909.2m.1; ZK909.2m.1; WBGene00002189. [P21137-13]
DR GeneID; 3565407; -.
DR UCSC; ZK909.2h.1; c. elegans.
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 GeneTree; ENSGT00940000163111; -.
DR InParanoid; P21137; -.
DR OMA; WQDSRNL; -.
DR OrthoDB; 963519at2759; -.
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-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-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-CEL-9634597; GPER1 signaling.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P21137; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002189; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P21137; baseline.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; ISS:WormBase.
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; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:WormBase.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
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 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
