FGFR1_DROME
ID FGFR1_DROME Reviewed; 729 AA.
AC Q07407; A4V320; O18371; Q26294; Q9VED5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Fibroblast growth factor receptor homolog 1;
DE EC=2.7.10.1;
DE AltName: Full=DmHD-38;
DE AltName: Full=Protein heartless;
DE AltName: Full=Tyrosine kinase 1;
DE Short=dTk1;
DE Flags: Precursor;
GN Name=htl; Synonyms=FR1, Tk1; ORFNames=CG7223;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S; TISSUE=Pupae;
RX PubMed=8330538; DOI=10.1242/dev.117.2.751;
RA Shishido E., Higashijima S., Emori Y., Saigo K.;
RT "Two FGF-receptor homologues of Drosophila: one is expressed in mesodermal
RT primordium in early embryos.";
RL Development 117:751-761(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8112607; DOI=10.1016/0378-1119(94)90758-7;
RA Ito M., Matsui T., Taniguchi T., Chihara K.;
RT "Alternative splicing generates two distinct transcripts for the Drosophila
RT melanogaster fibroblast growth factor receptor homolog.";
RL Gene 139:215-218(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 560-615.
RX PubMed=1915852; DOI=10.1016/0014-5793(91)81078-m;
RA Shishido E., Emori Y., Saigo K.;
RT "Identification of seven novel protein-tyrosine kinase genes of Drosophila
RT by the polymerase chain reaction.";
RL FEBS Lett. 289:235-238(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 562-614.
RC TISSUE=Embryo;
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
CC -!- FUNCTION: May be required for patterning of muscle precursor cells. May
CC be essential for generation of mesodermal and endodermal layers,
CC invaginations of various types of cells and CNS formation.
CC {ECO:0000269|PubMed:8330538}.
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 -!- INTERACTION:
CC Q07407; O96757: stumps; NbExp=6; IntAct=EBI-74984, EBI-74922;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: In early embryos, expression is specific to
CC mesodermal primordium and invaginated mesodermal cells. At later
CC stages, expression is seen in putative muscle precursor cells and in
CC the CNS. {ECO:0000269|PubMed:8330538}.
CC -!- DEVELOPMENTAL STAGE: Embryogenesis. {ECO:0000269|PubMed:8330538}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X74030; CAA52189.1; -; mRNA.
DR EMBL; D14976; BAA03616.1; -; mRNA.
DR EMBL; D14977; BAA03617.1; -; mRNA.
DR EMBL; AE014297; AAF55489.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55490.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13755.1; -; Genomic_DNA.
DR EMBL; AY051812; AAK93236.1; -; mRNA.
DR EMBL; S55969; AAB19903.1; -; Genomic_DNA.
DR EMBL; AJ002913; CAA05748.1; -; Genomic_DNA.
DR PIR; A49120; A49120.
DR RefSeq; NP_524394.2; NM_079670.3.
DR RefSeq; NP_732286.1; NM_169784.2.
DR RefSeq; NP_732287.1; NM_169785.2.
DR AlphaFoldDB; Q07407; -.
DR SMR; Q07407; -.
DR BioGRID; 67184; 16.
DR IntAct; Q07407; 3.
DR STRING; 7227.FBpp0082970; -.
DR GlyGen; Q07407; 10 sites.
DR PaxDb; Q07407; -.
DR PRIDE; Q07407; -.
DR DNASU; 42160; -.
DR EnsemblMetazoa; FBtr0083548; FBpp0082970; FBgn0010389.
DR EnsemblMetazoa; FBtr0083549; FBpp0082971; FBgn0010389.
DR EnsemblMetazoa; FBtr0083550; FBpp0082972; FBgn0010389.
DR GeneID; 42160; -.
DR KEGG; dme:Dmel_CG7223; -.
DR UCSC; CG7223-RB; d. melanogaster.
DR CTD; 3343; -.
DR FlyBase; FBgn0010389; htl.
DR VEuPathDB; VectorBase:FBgn0010389; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000167157; -.
DR HOGENOM; CLU_000288_74_1_1; -.
DR InParanoid; Q07407; -.
DR OMA; NRPFGRD; -.
DR OrthoDB; 220433at2759; -.
DR PhylomeDB; Q07407; -.
DR BRENDA; 2.7.10.1; 1994.
DR BioGRID-ORCS; 42160; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42160; -.
DR PRO; PR:Q07407; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010389; Expressed in crop (Drosophila) and 57 other tissues.
DR Genevisible; Q07407; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098975; C:postsynapse of neuromuscular junction; IMP:FlyBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; TAS:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0007493; P:endodermal cell fate determination; IEP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0021782; P:glial cell development; IMP:FlyBase.
DR GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
DR GO; GO:0042065; P:glial cell growth; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0007506; P:gonadal mesoderm development; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0007523; P:larval visceral muscle development; IMP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0035169; P:lymph gland plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:FlyBase.
DR GO; GO:0001710; P:mesodermal cell fate commitment; IMP:FlyBase.
DR GO; GO:0007500; P:mesodermal cell fate determination; IEP:UniProtKB.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR GO; GO:0048626; P:myoblast fate specification; IMP:FlyBase.
DR GO; GO:0110122; P:myotube cell migration; IMP:FlyBase.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; IMP:FlyBase.
DR GO; GO:0061320; P:pericardial nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:1903977; P:positive regulation of glial cell migration; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR GO; GO:0007522; P:visceral muscle development; IMP:FlyBase.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR016248; FGF_rcpt_fam.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; PF13895; Ig_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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 ATP-binding; Developmental protein; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..729
FT /note="Fibroblast growth factor receptor homolog 1"
FT /id="PRO_0000016794"
FT TOPO_DOM 37..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 106..192
FT /note="Ig-like C2-type 1"
FT DOMAIN 203..279
FT /note="Ig-like C2-type 2"
FT DOMAIN 416..692
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 56..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 556
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 422..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 587
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 220..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 21
FT /note="L -> V (in Ref. 1; CAA52189 and 2; BAA03616/
FT BAA03617)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="S -> T (in Ref. 1; CAA52189 and 2; BAA03616/
FT BAA03617)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> V (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="G -> A (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="M -> S (in Ref. 2; BAA03616/BAA03617)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="C -> V (in Ref. 2; BAA03616/BAA03617)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="I -> II (in Ref. 2; BAA03616/BAA03617)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="V -> M (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="K -> R (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 507..508
FT /note="PF -> RS (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="V -> L (in Ref. 1; CAA52189)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="Missing (in Ref. 7; CAA05748)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="L -> Q (in Ref. 2; BAA03616/BAA03617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82586 MW; 199166043EC87386 CRC64;
MAAAWSWRAS HSTITMTSGS LVVLFLLLSI WQPAVQVEGR RQMANSQEMI KDHLGARSQN
KTPAITNNAN QSSTSSADLD DGAADDDDNK ADLPVNVSSK PYWRNPKKMS FLQTRPSGSL
LTLNCHALGN PEPNITWYRN GTVDWTRGYG SLKRNRWTLT MEDLVPGDCG NYTCKVCNSL
GCIRHDTQVI VSDRVNHKPI LMTGPLNLTL VVNSTGSMHC KYLSDLTSKK AWIFVPCHGM
TNCSNNRSII AEDKDQLDFV NVRMEQEGWY TCVESNSLGQ SNSTAYLRVV RSLHVLEAGV
ASGSLHSTSF VYIFVFGGLI FIFMTTLFVF YAIRKMKHEK VLKQRIETVH QWTKKVIIFK
PEGGGDSSGS MDTMIMPVVR IQKQRTTVLQ NGNEPAPFNE YEFPLDSNWE LPRSHLVLGA
TLGEGAFGRV VMAEVNNAIV AVKMVKEGHT DDDIASLVRE MEVMKIIGRH INIINLLGCC
SQNGPLYVIV EYAPHGNLKD FLYKNRPFGR DQDRDSSQPP PSPPAHVITE KDLIKFAHQI
ARGMDYLASR RCIHRDLAAR NVLVSDDYVL KIADFGLARD IQSTDYYRKN TNGRLPIKWM
APESLQEKFY DSKSDVWSYG ILLWEIMTYG QQPYPTIMSA EELYTYLMSG QRMEKPAKCS
MNIYILMRQC WHFNADDRPP FTEIVEYMDK LLQTKEDYLD VDIANLDTPP STSDEEEDET
DNLQKWCNY
