EGL15_CAEEL
ID EGL15_CAEEL Reviewed; 1040 AA.
AC Q10656; Q7JL68; Q7YZM7; Q7YZM8; Q7YZN0; Q7YZN1; Q7Z025; Q8MQ14; Q93804;
AC Q95QE0; Q95QE1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Myoblast growth factor receptor egl-15;
DE EC=2.7.10.1;
DE AltName: Full=Egg-laying defective protein 15;
DE Flags: Precursor;
GN Name=egl-15; ORFNames=F58A3.2;
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 [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-680 AND PRO-714.
RC STRAIN=Bristol N2;
RX PubMed=7585964; DOI=10.1016/0092-8674(95)90101-9;
RA Devore D.L., Horvitz H.R., Stern M.J.;
RT "An FGF receptor signaling pathway is required for the normal cell
RT migrations of the sex myoblasts in C. elegans hermaphrodites.";
RL Cell 83:611-620(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 932-1040 (ISOFORMS A; C; D AND E), AND FUNCTION.
RX PubMed=12835392; DOI=10.1242/dev.00604;
RA Goodman S.J., Branda C.S., Robinson M.K., Burdine R.D., Stern M.J.;
RT "Alternative splicing affecting a novel domain in the C. elegans EGL-15 FGF
RT receptor confers functional specificity.";
RL Development 130:3757-3766(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP DEPHOSPHORYLATION BY CLR-1.
RC STRAIN=Bristol N2;
RX PubMed=9585503; DOI=10.1101/gad.12.10.1425;
RA Kokel M., Borland C.Z., DeLong L., Horvitz H.R., Stern M.J.;
RT "clr-1 encodes a receptor tyrosine phosphatase that negatively regulates an
RT FGF receptor signaling pathway in Caenorhabditis elegans.";
RL Genes Dev. 12:1425-1437(1998).
RN [5]
RP FUNCTION.
RX PubMed=11689700; DOI=10.1128/mcb.21.23.8104-8116.2001;
RA Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
RA Stern M.J.;
RT "The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like
RT multisubstrate adaptor protein in fibroblast growth factor signal
RT transduction.";
RL Mol. Cell. Biol. 21:8104-8116(2001).
RN [6]
RP FUNCTION.
RX PubMed=14517244; DOI=10.1093/emboj/cdg472;
RA Szewczyk N.J., Jacobson L.A.;
RT "Activated EGL-15 FGF receptor promotes protein degradation in muscles of
RT Caenorhabditis elegans.";
RL EMBO J. 22:5058-5067(2003).
RN [7]
RP FUNCTION.
RX PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
RA Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III,
RA Schafer W.R.;
RT "Identification and characterization of novel nicotinic receptor-associated
RT proteins in Caenorhabditis elegans.";
RL EMBO J. 24:2566-2578(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-714.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
CC -!- FUNCTION: Receptor tyrosine kinase required for larval development
CC (PubMed:7585964). May phosphorylate adapter protein soc-1 which in turn
CC may result in the recruitment and/or activation of phosphatase ptp-2
CC (PubMed:11689700). May activate the Ras/MAPK kinase signaling pathway
CC which includes sem-5, sos-1, let-60/Ras, lin-45/Raf, mek-2 and mpk-1
CC (PubMed:11689700). Acts in the hypodermis to regulate axon growth and
CC fluid homeostasis (PubMed:12835392, PubMed:7585964). Activates protein
CC degradation in muscles (PubMed:14517244). Probably following
CC interaction with ligand let-756, regulates negatively membrane
CC protrusion from body wall muscles during larval development
CC (PubMed:16495308). Plays a role in nicotinic acetylcholine receptor
CC (nAChR)-mediated sensitivity to nicotine (PubMed:15990870). Regulates
CC synaptic levels of nAChR subunit lev-1 in the nerve cord
CC (PubMed:15990870). {ECO:0000269|PubMed:11689700,
CC ECO:0000269|PubMed:12835392, ECO:0000269|PubMed:14517244,
CC ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:7585964}.
CC -!- FUNCTION: [Isoform b]: Affects the maintenance of axon position without
CC affecting axon growth. Interaction with egl-17 is required for the
CC guidance of sex myoblast migration during gonad development.
CC {ECO:0000269|PubMed:12835392}.
CC -!- FUNCTION: [Isoform a]: Interaction with let-756 appears to play a role
CC in maintaining body morphology at higher temperatures.
CC {ECO:0000269|PubMed:12835392}.
CC -!- FUNCTION: [Isoform c]: Interaction with let-756 appears to play a role
CC in maintaining body morphology at higher temperatures.
CC {ECO:0000269|PubMed:12835392}.
CC -!- FUNCTION: [Isoform d]: Interaction with let-756 appears to play a role
CC in maintaining body morphology at higher temperatures.
CC {ECO:0000269|PubMed:12835392}.
CC -!- FUNCTION: [Isoform e]: Interaction with let-756 appears to play a role
CC in maintaining body morphology at higher temperatures.
CC {ECO:0000269|PubMed:12835392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a;
CC IsoId=Q10656-1; Sequence=Displayed;
CC Name=b; Synonyms=EGL-15(5A);
CC IsoId=Q10656-2; Sequence=VSP_019861;
CC Name=c;
CC IsoId=Q10656-3; Sequence=VSP_002991, VSP_002992, VSP_002994;
CC Name=d;
CC IsoId=Q10656-4; Sequence=VSP_002991, VSP_002992, VSP_019862;
CC Name=e;
CC IsoId=Q10656-5; Sequence=VSP_002991, VSP_002992, VSP_019863;
CC -!- PTM: Activity is regulated by the phosphatase clr-1, however it is not
CC known whether clr-1 acts directly on egl-15.
CC {ECO:0000269|PubMed:9585503}.
CC -!- DISRUPTION PHENOTYPE: Early arrest in larval development. Impaired
CC guided migration of sex myoblasts (PubMed:7585964). RNAi-mediated
CC knockdown causes ectopic membrane extension from body wall muscles
CC (PubMed:16495308). {ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:7585964}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U39761; AAC46934.1; -; mRNA.
DR EMBL; AY268435; AAP31029.1; -; mRNA.
DR EMBL; AY268436; AAP31030.1; -; mRNA.
DR EMBL; AY288941; AAP44084.1; -; mRNA.
DR EMBL; AY288942; AAP44085.1; -; mRNA.
DR EMBL; AY292532; AAP74805.1; -; mRNA.
DR EMBL; Z81017; CAB02673.2; -; Genomic_DNA.
DR EMBL; Z81017; CAC70094.2; -; Genomic_DNA.
DR EMBL; Z81017; CAC70095.2; -; Genomic_DNA.
DR EMBL; Z81017; CAD44136.1; -; Genomic_DNA.
DR EMBL; Z81017; CAE47468.1; -; Genomic_DNA.
DR PIR; A57638; A57638.
DR PIR; T22889; T22889.
DR RefSeq; NP_001024723.1; NM_001029552.2.
DR RefSeq; NP_001024724.3; NM_001029553.5.
DR RefSeq; NP_001024725.2; NM_001029554.4.
DR RefSeq; NP_001024726.2; NM_001029555.4.
DR RefSeq; NP_509842.2; NM_077441.6.
DR AlphaFoldDB; Q10656; -.
DR SMR; Q10656; -.
DR BioGRID; 46202; 161.
DR IntAct; Q10656; 1.
DR STRING; 6239.F58A3.2c; -.
DR iPTMnet; Q10656; -.
DR PaxDb; Q10656; -.
DR PeptideAtlas; Q10656; -.
DR PRIDE; Q10656; -.
DR EnsemblMetazoa; F58A3.2a.1; F58A3.2a.1; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2a.2; F58A3.2a.2; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2a.3; F58A3.2a.3; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2a.4; F58A3.2a.4; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2a.5; F58A3.2a.5; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2a.6; F58A3.2a.6; WBGene00001184. [Q10656-1]
DR EnsemblMetazoa; F58A3.2b.1; F58A3.2b.1; WBGene00001184. [Q10656-2]
DR UCSC; F58A3.2e; c. elegans. [Q10656-1]
DR WormBase; F58A3.2a; CE28238; WBGene00001184; egl-15. [Q10656-1]
DR WormBase; F58A3.2b; CE35726; WBGene00001184; egl-15. [Q10656-2]
DR WormBase; F58A3.2c; CE50149; WBGene00001184; egl-15.
DR WormBase; F58A3.2d; CE50303; WBGene00001184; egl-15.
DR WormBase; F58A3.2e; CE50247; WBGene00001184; egl-15.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000167157; -.
DR InParanoid; Q10656; -.
DR OrthoDB; 220433at2759; -.
DR PhylomeDB; Q10656; -.
DR BRENDA; 2.7.10.1; 1045.
DR Reactome; R-CEL-109704; PI3K Cascade.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR Reactome; R-CEL-210993; Tie2 Signaling.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-9607240; FLT3 Signaling.
DR SignaLink; Q10656; -.
DR PRO; PR:Q10656; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001184; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q10656; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:WormBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:WormBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0031344; P:regulation of cell projection organization; IMP:WormBase.
DR GO; GO:0031647; P:regulation of protein stability; IGI:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1040
FT /note="Myoblast growth factor receptor egl-15"
FT /id="PRO_0000016796"
FT TOPO_DOM 20..525
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..1040
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 287..383
FT /note="Ig-like C2-type 2"
FT DOMAIN 391..501
FT /note="Ig-like C2-type 3"
FT DOMAIN 640..931
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 234..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 797
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 646..654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 828
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 314..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 414..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 129..245
FT /note="FCDYFLFPDIHHLNIPMECVCLWKYNKEAKRSDVNYAAVTGEVCSKYASRMI
FT NRARKPLPMIPCFGDHCKEFDTTPVSDFGLPGKPEDDPLVKRVVLKKDDVIVPVHDSEE
FT SPSESR -> PLKLFDWLTEHRVFDISHLLPKLLPPAEMRRVKSQLGGWEKMNNEQKIV
FT RARHILRLRQINHALG (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_019861"
FT VAR_SEQ 829
FT /note="R -> RL (in isoform c, isoform d and isoform e)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_002991"
FT VAR_SEQ 984
FT /note="E -> EVDQN (in isoform c, isoform d and isoform e)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_002992"
FT VAR_SEQ 1027..1040
FT /note="RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGYVRQDKLARAVSGVANQSLD
FT SALGSPAWPSYDRPSNKASCLDQTHQYYNTTSKIQYLHFTFDDPDCMTRSRDSAIFEES
FT YHPNYIQSHPLYSKIIIKKNMTPRNPLPTKETIV (in isoform c)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_002994"
FT VAR_SEQ 1027..1040
FT /note="RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGYVRQDKLARAVSGVANQSLD
FT SALGSPAWPSYDRPSNKASCLDDEKHHYYYS (in isoform d)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_019862"
FT VAR_SEQ 1027..1040
FT /note="RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGSNSPVL (in isoform
FT e)"
FT /evidence="ECO:0000303|PubMed:12835392"
FT /id="VSP_019863"
FT MUTAGEN 680
FT /note="E->K: In n1775; loss of activity."
FT /evidence="ECO:0000269|PubMed:7585964"
FT MUTAGEN 714
FT /note="P->L: In n1783; loss of activity. Ectopic membrane
FT extension in body wall muscles."
FT /evidence="ECO:0000269|PubMed:16495308,
FT ECO:0000269|PubMed:7585964"
FT CONFLICT 551
FT /note="Q -> G (in Ref. 2; AAP44084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1040 AA; 118956 MW; 8CA227195DDBCD69 CRC64;
MSYFLASCLG VGLLSTVSCS LQGLTSHYRE NIPRFKHVAN ERYEVFLGDE IKFDCQTAAS
KISAFVEWYR NDKLLKNDQI DKDKIRKDNN RMMLHLKNID VSDQGLWSCR VHNAYGQISR
NFTVEVIDFC DYFLFPDIHH LNIPMECVCL WKYNKEAKRS DVNYAAVTGE VCSKYASRMI
NRARKPLPMI PCFGDHCKEF DTTPVSDFGL PGKPEDDPLV KRVVLKKDDV IVPVHDSEES
PSESRTEFIN ADEKENKEDE EEDYSVSQPV APDAGLTELN ITAEEPPYFK SNDNIVLFNE
THALPAGRTL KLNCRAKGYP EPQIIWYKNG KMLKKSSARS GGYEFKFNRW SLEVEDAVVA
DSGEFHCEAL NKVGSAKKYF HVIIVNRMRR PPIIVPNILA NQSVNINDTA TFHCKVVSDL
LPHIIWVRIN KINGSYSYYN NSAEEYMFNY TEMDTFDKAH VHHVGDESTL TIFNVSLDDQ
GIYACLSGNS LGMSMANATL TVNEFMAIHL LTGDEPKIDR WTTSDYIFTT ILLFLLLAAT
LFGILFMVCK QTLHKKGFMD DTVGLVARKK RVVVSKRPMN EDNENSDDEP SPYQIQIIET
PITKKEAARK QRKRMNSENT VLSEYEVDSD PVWEVERSKL SLVHMLGEGA FGEVWKATYK
ETENNEIAVA VKKLKMSAHE KELIDLVSEM ETFKVIGEHE NVLRLIGCCT GAGPLYVVVE
LCKHGNLRDF LRAHRPKEEK AKKSSQELTD YLEPRKASDK DDIELIPNLT QRHLVQFAWQ
VAQGMNFLAS KKIIHRDLAA RNVLVGDGHV LKISDFGLSR DVHCNDYYRK RGNGRLPIKW
MALEALDSNV YTVESDVWSY GVLLWEIMTL GGTPYPTIAM PELYANLKEG YRMEPPHLCP
QEVYHLMCSC WREKLEERPS FKTIVDYLDW MLTMTNETIE GSQEFNDQFF SERSTASGPV
SPMESFQKKR KHRPLSAPVN LPSEPQHTIC DDYESNFSVE PPNDPNHLYC NDNMLKNHII
TPETSQRIPS NNNSMSKPEF
