LTK_DANRE
ID LTK_DANRE Reviewed; 1530 AA.
AC F1QVU0; B0LVZ8; B1PCZ3; B1PHI5; F1QBU7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000305};
DE EC=2.7.10.1 {ECO:0000250|UniProtKB:P29376};
DE AltName: Full=Anaplastic lymphoma kinase 1 {ECO:0000303|PubMed:29078341};
DE Short=alk-1 {ECO:0000303|PubMed:29078341};
DE AltName: Full=Protein moonstone {ECO:0000303|PubMed:18369445};
DE Short=mne {ECO:0000303|PubMed:26801003};
DE AltName: Full=Protein shady {ECO:0000303|PubMed:18369445};
DE Short=shd {ECO:0000303|PubMed:18369445};
DE Flags: Precursor;
GN Name=ltk {ECO:0000303|PubMed:18369445,
GN ECO:0000312|ZFIN:ZDB-GENE-030616-115};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PRO-759 AND
RP 786-LYS--VAL-1530.
RX PubMed=18369445; DOI=10.1371/journal.pgen.1000026;
RA Lopes S.S., Yang X., Mueller J., Carney T.J., McAdow A.R., Rauch G.J.,
RA Jacoby A.S., Hurst L.D., Delfino-Machin M., Haffter P., Geisler R.,
RA Johnson S.L., Ward A., Kelsh R.N.;
RT "Leukocyte tyrosine kinase functions in pigment cell development.";
RL PLoS Genet. 4:e1000026-e1000026(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=22985331; DOI=10.1021/cb300361a;
RA Rodrigues F.S., Yang X., Nikaido M., Liu Q., Kelsh R.N.;
RT "A simple, highly visual in vivo screen for anaplastic lymphoma kinase
RT inhibitors.";
RL ACS Chem. Biol. 7:1968-1974(2012).
RN [4]
RP FUNCTION.
RX PubMed=23821036; DOI=10.1242/dev.096719;
RA Frohnhoefer H.G., Krauss J., Maischein H.M., Nuesslein-Volhard C.;
RT "Iridophores and their interactions with other chromatophores are required
RT for stripe formation in zebrafish.";
RL Development 140:2997-3007(2013).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PHE-993.
RX PubMed=26801003; DOI=10.1111/pcmr.12454;
RA Fadeev A., Krauss J., Singh A.P., Nuesslein-Volhard C.;
RT "Zebrafish Leucocyte tyrosine kinase controls iridophore establishment,
RT proliferation and survival.";
RL Pigment Cell Melanoma Res. 29:284-296(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29078341; DOI=10.1073/pnas.1710254114;
RA Mo E.S., Cheng Q., Reshetnyak A.V., Schlessinger J., Nicoli S.;
RT "Alk and Ltk ligands are essential for iridophore development in zebrafish
RT mediated by the receptor tyrosine kinase Ltk.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:12027-12032(2017).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29317532; DOI=10.1073/pnas.1719137115;
RA Fadeev A., Mendoza-Garcia P., Irion U., Guan J., Pfeifer K., Wiessner S.,
RA Serluca F., Singh A.P., Nuesslein-Volhard C., Palmer R.H.;
RT "ALKALs are in vivo ligands for ALK family receptor tyrosine kinases in the
RT neural crest and derived cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E630-E638(2018).
CC -!- FUNCTION: Receptor tyrosine kinase required for the establishment and
CC proliferation of iridophores and their progenitors from multipotent
CC neural crest cells (PubMed:18369445, PubMed:23821036, PubMed:26801003,
CC PubMed:29078341, PubMed:29317532). Iridophores are the blue-tinted
CC cells that reflect light to give fish their metallic shine and which,
CC together with yellow xanthophore and black melanophores, generate the
CC zebrafish's stripes (PubMed:18369445, PubMed:23821036,
CC PubMed:26801003). Following activation by alkal ligands (alkal1,
CC alkal2a or alkal2b) at the cell surface, transduces an extracellular
CC signal into an intracellular response (PubMed:29078341,
CC PubMed:29317532). Ligand-binding to the extracellular domain induces
CC tyrosine kinase activation, resulting in the activation of the mitogen-
CC activated protein kinase (MAPK) pathway (By similarity). Phosphorylates
CC almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By
CC similarity). {ECO:0000250|UniProtKB:Q9UM73,
CC ECO:0000269|PubMed:18369445, ECO:0000269|PubMed:23821036,
CC ECO:0000269|PubMed:26801003, ECO:0000269|PubMed:29078341,
CC ECO:0000269|PubMed:29317532}.
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:0000250|UniProtKB:P29376};
CC -!- ACTIVITY REGULATION: Inhibited by ALK inhibitor TAE684.
CC {ECO:0000269|PubMed:22985331}.
CC -!- SUBUNIT: Homodimer; homodimerizes upon binding to alkal ligands
CC (alkal1, alkal2a or alkal2b). {ECO:0000250|UniProtKB:P29376}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29376};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F1QVU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F1QVU0-2; Sequence=VSP_061497;
CC -!- TISSUE SPECIFICITY: Mainly expressed in neural crest cells (NCCs) and
CC iridophores (PubMed:18369445, PubMed:29317532). In adults, expressed in
CC the head and iridophores of the trunk and eyes, as well as in the swim
CC bladder (PubMed:29317532). {ECO:0000269|PubMed:18369445,
CC ECO:0000269|PubMed:29317532}.
CC -!- DEVELOPMENTAL STAGE: Expressed in notochord from 18-24 hours post-
CC fertilization (hpf) and prominently in brain and swim bladder from 3
CC days post-fertilization (dpf). {ECO:0000269|PubMed:18369445}.
CC -!- DISRUPTION PHENOTYPE: Complete absence of iridophores (PubMed:29078341,
CC PubMed:29317532). Fishes do not survive past 6 days post-fertilization
CC (dpf), possibly because the swim bladder cannot fill with air
CC (PubMed:29317532). {ECO:0000269|PubMed:29078341,
CC ECO:0000269|PubMed:29317532}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; EU380906; ABY83136.1; -; mRNA.
DR EMBL; EU399812; ACA79941.1; -; mRNA.
DR EMBL; EU420091; ACA79942.1; -; mRNA.
DR EMBL; BX539317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001006661.1; NM_001006660.1.
DR RefSeq; XP_005158843.1; XM_005158786.3.
DR AlphaFoldDB; F1QVU0; -.
DR SMR; F1QVU0; -.
DR STRING; 7955.ENSDARP00000061546; -.
DR PaxDb; F1QVU0; -.
DR Ensembl; ENSDART00000061547; ENSDARP00000061546; ENSDARG00000042861. [F1QVU0-1]
DR Ensembl; ENSDART00000062907; ENSDARP00000062906; ENSDARG00000042861. [F1QVU0-2]
DR GeneID; 564470; -.
DR KEGG; dre:564470; -.
DR CTD; 4058; -.
DR ZFIN; ZDB-GENE-030616-115; ltk.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000164602; -.
DR HOGENOM; CLU_001878_2_2_1; -.
DR InParanoid; F1QVU0; -.
DR OMA; FESPCLW; -.
DR OrthoDB; 40108at2759; -.
DR PhylomeDB; F1QVU0; -.
DR TreeFam; TF351636; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000042861; Expressed in mature ovarian follicle and 10 other tissues.
DR ExpressionAtlas; F1QVU0; baseline.
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-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0048066; P:developmental pigmentation; IMP:UniProtKB.
DR GO; GO:0050935; P:iridophore differentiation; IMP:UniProtKB.
DR GO; GO:0098727; P:maintenance of cell number; IMP:ZFIN.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
DR GO; GO:0097324; P:melanocyte migration; IMP:ZFIN.
DR GO; GO:0070285; P:pigment cell development; IMP:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:ZFIN.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IMP:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd06263; MAM; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR026984; LTK.
DR InterPro; IPR000998; MAM_dom.
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 InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF294; PTHR24416:SF294; 1.
DR Pfam; PF00629; MAM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50060; MAM_2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Disulfide bond;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1530
FT /note="Tyrosine-protein kinase receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_5003268704"
FT TOPO_DOM 26..851
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 51..221
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 231..269
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 275..436
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 935..1211
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 635..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1068
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 941..949
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 969
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 232..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 240..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 252..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 474..487
FT /evidence="ECO:0000250|UniProtKB:P29376"
FT DISULFID 569..580
FT /evidence="ECO:0000250|UniProtKB:P29376"
FT DISULFID 696..718
FT /evidence="ECO:0000250|UniProtKB:P29376"
FT VAR_SEQ 813..838
FT /note="Missing (in isoform 2)"
FT /id="VSP_061497"
FT MUTAGEN 759
FT /note="P->S: In shd(j9s1) mutant; reduced iridophores in
FT the body and eyes."
FT /evidence="ECO:0000269|PubMed:18369445"
FT MUTAGEN 786..1530
FT /note="Missing: In shd(ty82) mutant; fishes have very few
FT iridophores and die as larvae."
FT /evidence="ECO:0000269|PubMed:18369445"
FT MUTAGEN 993
FT /note="F->I: In mne mutant; dominant mutation; fishes
FT display ectopic iridophore ,probably caused by
FT hyperactivity of the tyrosine kinase activity."
FT /evidence="ECO:0000269|PubMed:26801003"
FT CONFLICT 20
FT /note="L -> V (in Ref. 1; ABY83136/ACA79941/ACA79942)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> S (in Ref. 1; ABY83136)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> E (in Ref. 1; ABY83136)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> N (in Ref. 1; ABY83136/ACA79941/ACA79942)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="G -> A (in Ref. 1; ABY83136)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="T -> I (in Ref. 1; ABY83136/ACA79941/ACA79942)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> S (in Ref. 1; ABY83136/ACA79941/ACA79942)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="P -> S (in Ref. 1; ABY83136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1482..1483
FT /note="PG -> AS (in Ref. 1; ABY83136/ACA79941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1530 AA; 165479 MW; D938550CBE000FE3 CRC64;
MDYITRQTFV KLALFIFTVL RSSCALLEKA AEDPVHPNPL QSSPAEDSDV SFCDFESPCS
WTLSSHSTGG DWFITSAQQH RSSRRDTQPI RDYSTGKSEG HFLLLKPSSS HLSAGRCSFH
MTSPVVLSSG PFCHLQLARF QPEPHAGNIS AFVKHTDSTD IKPIDLTIKE QESDSSQWEV
LEAVIGQLNE PFQVTVQYSA CSSHEVGFLA FDSLELKNCV MGDDYVDLGS DCEKYSSLQC
HSGGCIEKQR VCDFHTDCPE GEDEGLICST LPLGSYCSFE LGSCGWLAAD TQSSWRLVSG
QQLIEDTHLL GTTLKNTQGH FLFLKVRGHG DEREALVQSP ALPSTISNQD CQLQFSLYRY
GDFNGTVLLS VVESGASAPA LIWERSGHWK DAWQEITLPI TEILNGFHLK VQAFWTSGSK
ADIALDDISL SAACFDTELN ELLHEGLPHD LDFSPLPEPS ASEASPITWW FTSCGASGPF
GPTQAQCDSA YRNTNVSVVV GKEGPLRGVQ MWKVPATNTY KISAYGAAGG KGAKNHNKRS
HGVFISATFP LEKGDILYIL IGHQGEDACP GRNPQTHKIC LGESSVIEDG FDSDGSALKW
AGGGGGGGGA TYIYRMENGQ PLPLLIAAGG GGKAYLEDPE SSQDQSFREQ YENDTTVSGV
SGRSGAAGGG GGWSDVSSLS WAGKSLVEGG QGGSSCPEAL SVLGWATFGG FGGGGGACSA
GGGGGGYRGG DAPLLDDISA DGQDGLSFVH PMGKIFLQPL AAMESHGEAE IVVYLNCSHC
KTQSCKRDED TKLILCLCDS DEVLAPDNVT CAGTKHSLCQ FINKHLQHNS SPLVCPPLVV
PMGSLADGPP SLVFIMAVIV STVVTGVVLT CASLTLIYYR KKNHLHAVRI RLQSPEYKLS
KIRSSTIMTD YNPNYGYFGK AASLSELKEV PRKNITLLRA LGHGAFGEVY EGQVLGMNGE
NTAMQVAIKT LPEICSEQDE MDFLMEALIM SKFSHQNIVR CIGVSLQILP RFILLELMTG
GDMKSFLRLN RPRTNHSSSL SMLELLHMAR DIALGCRYLE ENHFIHRDIA ARNCLLTCPG
PDRVAKIGDF GMARDIYRAS YYRKGGRAML PVKWMPPEAF LEGIFTCKTD TWSFGVLLWE
IFSLGYMPYP CKTNQEVLEF VTGGGRMDPP KSCPGPVYRI MTQCWQHCPE HRPNFTTILE
RINYCTQDPD VINTPLPVEC GPPVEEEGGT VIRPDGSGSM TPLLVARSLS QDASPRASIT
SVTPQALKPR LQLQRPVHLT QEVGTYRETL EPCWAEPVPA SGVCPGPWLQ VPEHRPCSRS
SSSSGSQKLK NKTKNLWNPT YGSWVLESFG RGKSALCHTQ SMPLSCNPTS VSAPSSTSEH
TDPVVEVNAN VSASPPPSAA PSQTTLTPTA APSRKSPTGA AGVSLATVMD LAKLQSFPCG
NVNYAYDEQS YETESLPVVV SKSLEPSTSS AATSSLVALS QPGSFTHKPL VKRHASYGHE
DVRRYTQPEK PTRDRDSGFS LSEDLSVTPV
