FGFR2_DROME
ID FGFR2_DROME Reviewed; 1052 AA.
AC Q09147; A4V1Y3; Q712V2; Q9VUC8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Fibroblast growth factor receptor homolog 2;
DE EC=2.7.10.1;
DE AltName: Full=Protein breathless;
DE AltName: Full=Tyrosine kinase 2;
DE Short=dTk2;
DE AltName: Full=Tyrosine kinase receptor HD-311;
DE AltName: Full=dFGF-R1;
DE Flags: Precursor;
GN Name=btl; Synonyms=FR2, HD-311, Tk2; ORFNames=CG32134;
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, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-240, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=1325393; DOI=10.1101/gad.6.9.1668;
RA Klaembt C., Glazer L., Shilo B.-Z.;
RT "Breathless, a Drosophila FGF receptor homolog, is essential for migration
RT of tracheal and specific midline glial cells.";
RL Genes Dev. 6:1668-1678(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 262-1052, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1849109; DOI=10.1101/gad.5.4.697;
RA Glazer L., Shilo B.-Z.;
RT "The Drosophila FGF-R homolog is expressed in the embryonic tracheal system
RT and appears to be required for directed tracheal cell extension.";
RL Genes Dev. 5:697-705(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 868-923.
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 870-922.
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:
CC generation of mesodermal and endodermal layers, invaginations of
CC various types of cells, and CNS formation. Essential for the ability of
CC the migrating tracheal and midline cells to recognize external guiding
CC cues. {ECO:0000269|PubMed:1325393, ECO:0000269|PubMed:1849109,
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: During embryogenesis, expression is seen in
CC mesoderm, endodermal precursor cells, CNS midline cells and trachea and
CC salivary duct ectodermal cells. {ECO:0000269|PubMed:1325393,
CC ECO:0000269|PubMed:1849109, ECO:0000269|PubMed:8330538}.
CC -!- DEVELOPMENTAL STAGE: All stages of development.
CC {ECO:0000269|PubMed:1849109}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74031; CAA52190.1; -; mRNA.
DR EMBL; AE014296; AAF49759.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52746.1; -; Genomic_DNA.
DR EMBL; X72830; CAA51340.1; -; Genomic_DNA.
DR EMBL; X57746; CAA40912.1; -; mRNA.
DR EMBL; S55971; AAB19904.1; -; Genomic_DNA.
DR EMBL; AJ002918; CAA05753.1; -; Genomic_DNA.
DR PIR; A39627; A39627.
DR PIR; A44065; A44065.
DR PIR; B49120; B49120.
DR RefSeq; NP_001014583.1; NM_001014583.2.
DR RefSeq; NP_729956.1; NM_168577.3.
DR AlphaFoldDB; Q09147; -.
DR SMR; Q09147; -.
DR BioGRID; 64900; 26.
DR IntAct; Q09147; 6.
DR STRING; 7227.FBpp0075520; -.
DR GlyGen; Q09147; 15 sites.
DR PaxDb; Q09147; -.
DR PRIDE; Q09147; -.
DR EnsemblMetazoa; FBtr0075778; FBpp0075520; FBgn0285896.
DR EnsemblMetazoa; FBtr0100676; FBpp0100143; FBgn0285896.
DR GeneID; 39564; -.
DR KEGG; dme:Dmel_CG32134; -.
DR UCSC; CG32134-RB; d. melanogaster.
DR CTD; 39564; -.
DR FlyBase; FBgn0285896; btl.
DR VEuPathDB; VectorBase:FBgn0285896; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000167157; -.
DR HOGENOM; CLU_000288_74_1_1; -.
DR InParanoid; Q09147; -.
DR OMA; YACVTNS; -.
DR OrthoDB; 220433at2759; -.
DR PhylomeDB; Q09147; -.
DR BRENDA; 2.7.10.1; 1994.
DR SignaLink; Q09147; -.
DR BioGRID-ORCS; 39564; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39564; -.
DR PRO; PR:Q09147; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0285896; Expressed in presumptive embryonic/larval tracheal system and 37 other tissues.
DR ExpressionAtlas; Q09147; baseline and differential.
DR Genevisible; Q09147; DM.
DR GO; GO:0035230; C:cytoneme; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IDA:FlyBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0035153; P:epithelial cell type specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:FlyBase.
DR GO; GO:0035215; P:genital disc development; IEP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IGI:FlyBase.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:FlyBase.
DR GO; GO:0042690; P:negative regulation of crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0045614; P:negative regulation of plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0007428; P:primary branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007429; P:secondary branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0035154; P:terminal cell fate specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0060438; P:trachea development; IMP:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IMP:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 4.
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; IPR013151; Immunoglobulin.
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; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1052
FT /note="Fibroblast growth factor receptor homolog 2"
FT /id="PRO_0000016795"
FT TOPO_DOM 20..600
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..1052
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 124..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 240..340
FT /note="Ig-like C2-type 3"
FT DOMAIN 393..478
FT /note="Ig-like C2-type 4"
FT DOMAIN 487..585
FT /note="Ig-like C2-type 5"
FT DOMAIN 712..1000
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 358..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 864
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 718..726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 895
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 507..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 104
FT /note="V -> I (in Ref. 1; CAA52190 and 4; CAA51340)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> I (in Ref. 1; CAA52190 and 4; CAA51340)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="N -> I (in Ref. 1; CAA52190)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> F (in Ref. 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="E -> D (in Ref. 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="E -> D (in Ref. 1; CAA52190 and 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 480..481
FT /note="ND -> KH (in Ref. 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="K -> Q (in Ref. 1; CAA52190 and 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="T -> S (in Ref. 1; CAA52190)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="A -> P (in Ref. 1; CAA52190)"
FT /evidence="ECO:0000305"
FT CONFLICT 911..921
FT /note="ESLQEKKYDSQ -> SRCRRRSTTH (in Ref. 5; CAA40912)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="E -> Q (in Ref. 5; CAA40912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 117813 MW; 74FBB9A5A2154D55 CRC64;
MAKVPITLVM IIAIVSAAAD LGCDYGHHRC YIDVTVENSP RQRHLLSDMD ITLQCVRPMA
KWFYEDKFQL RATLLRLERA QSGNSGNYGC LDSQNRWYNI SLVVGHKEPV GNDIASFVKL
EDAPALPESD LFFQPLNESR SLKLLQPLPK TVQRTAGGLF QLNCSPMDPD AKGVNISWLH
NDTQILGGRG RIKLKRWSLT VGQLQPEDAG SYHCELCVEQ DCQRSNPTQL EVISRKHTVP
MLKPGYPRNT SIALGDNVSI ECLLEDSALE PKITWLHKGN ADNIDDLLQR LREQSQLPVD
VTRLITRMDE PQVLRLGNVL MEDGGWYICI AENQVGRTVA ASYVDLYSPS DTTTVRTTTT
TTVASPIPTA STGEDNDDDV ENPAAEASGG VGPPVFRKEL KRLQHSLSGN TVNLACPVYG
KANITWTKDK KPLNRELGVY VQKNWTLRFV EATSEDSGLY NCKVCNAWGC IQFDFSVQIN
DRTRSAPIIV VPQNQTVKVN GSLVMKCTVY SDLHPTVSWK RVVLKNASLD GLKSVEIQNL
NFTVTNDSVV LTLRNVTFDQ EGWYTCLASS GLGRSNSSVY LRVVSPLPPL EIYALLHAHP
LGFTLAAITI VALFLLGSAF ITFMLRRLRR EKLLKLRIET VHQWTKKVII YRPGGEEGSG
CSSGDLQMPV IRIEKQRTTV STTGTGGTDP AQGFNEYEFP LDSNWEIPRQ QLSLGSILGE
GAFGRVVMAE AEGLPRSPQL AETIVAVKMV KEEHTDTDMA SLVREMEVMK MIGKHINIIN
LLGCCSQGGP LWVIVEYAPH GNLKDFLKQN RPGAPQRRSD SDGYLDDKPL ISTQHLGEKE
LTKFAFQIAR GMEYLASRRC IHRDLAARNV LVSDGYVMKI ADFGLARDIQ DTEYYRKNTN
GRLPIKWMAP ESLQEKKYDS QSDVWSYGVL LWEIMTYGDQ PYPHILSAEE LYSYLITGQR
MEKPAKCSLN IYVVMRQCWH FESCARPTFA ELVESFDGIL QQASSNPNDA YLDLSMPMLE
TPPSSGDEDD GSDTETFRET SPLRYQYTYK FN
