TRH_DROME
ID TRH_DROME Reviewed; 1022 AA.
AC Q24119; A8JNH0; A8WHG8; Q0E8K2; Q24165; Q8SX13; Q9W0Q7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Protein trachealess;
GN Name=trh; ORFNames=CG6883;
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] (ISOFORMS A; B AND E), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8557198; DOI=10.1101/gad.10.1.93;
RA Wilk R., Weizman I., Shilo B.-Z.;
RT "Trachealess encodes a bHLH-PAS protein that is an inducer of tracheal cell
RT fates in Drosophila.";
RL Genes Dev. 10:93-102(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=8557189; DOI=10.1101/gad.10.1.103;
RA Isaac D.D., Andrew D.J.;
RT "Tubulogenesis in Drosophila: a requirement for the trachealess gene
RT product.";
RL Genes Dev. 10:103-117(1996).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1022 (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
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 [7]
RP FUNCTION.
RX PubMed=9374395; DOI=10.1242/dev.124.20.3975;
RA Ohshiro T., Saigo K.;
RT "Transcriptional regulation of breathless FGF receptor gene by binding of
RT TRACHEALESS/dARNT heterodimers to three central midline elements in
RT Drosophila developing trachea.";
RL Development 124:3975-3986(1997).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-233.
RX PubMed=10502111; DOI=10.1007/s004270050287;
RA Jack J., Myette G.;
RT "Mutations that alter the morphology of the malpighian tubules in
RT Drosophila.";
RL Dev. Genes Evol. 209:546-554(1999).
RN [9]
RP PHOSPHORYLATION AT SER-673, MUTAGENESIS OF SER-579 AND SER-673, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11740943; DOI=10.1016/s1534-5807(01)00090-9;
RA Jin J., Anthopoulos N., Wetsch B., Binari R.C., Isaac D.D., Andrew D.J.,
RA Woodgett J.R., Manoukian A.S.;
RT "Regulation of Drosophila tracheal system development by protein kinase
RT B.";
RL Dev. Cell 1:817-827(2001).
RN [10]
RP READTHROUGH OF STOP CODON.
RX PubMed=21994247; DOI=10.1101/gr.119974.110;
RA Jungreis I., Lin M.F., Spokony R., Chan C.S., Negre N., Victorsen A.,
RA White K.P., Kellis M.;
RT "Evidence of abundant stop codon readthrough in Drosophila and other
RT metazoa.";
RL Genome Res. 21:2096-2113(2011).
CC -!- FUNCTION: Transcription factor, master regulator of tracheal cell fates
CC in the embryo, necessary for the development of the salivary gland
CC duct, Malpighian tubules and the posterior spiracles (PubMed:8557189,
CC PubMed:8557198, PubMed:9374395, PubMed:10502111). It may induce a
CC general fate of branched tubular structures of epithelial origin
CC (PubMed:8557189, PubMed:8557198, PubMed:10502111). Functions with tgo
CC to regulate expression of btl (PubMed:9374395).
CC {ECO:0000269|PubMed:10502111, ECO:0000269|PubMed:8557189,
CC ECO:0000269|PubMed:8557198, ECO:0000269|PubMed:9374395}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Heterodimer with tgo.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:11740943}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=D;
CC IsoId=Q24119-5; Sequence=Displayed;
CC Name=A;
CC IsoId=Q24119-1; Sequence=VSP_043934;
CC Name=B;
CC IsoId=Q24119-3; Sequence=VSP_043933, VSP_043934;
CC Name=C;
CC IsoId=Q24119-6; Sequence=VSP_043931, VSP_043933, VSP_043934;
CC Name=E;
CC IsoId=Q24119-2; Sequence=VSP_043932, VSP_043934;
CC -!- TISSUE SPECIFICITY: Trachea, salivary gland ducts, posterior spiracles
CC (Filzkoeper primordia) and a subset of cells in the CNS.
CC {ECO:0000269|PubMed:8557189, ECO:0000269|PubMed:8557198}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, first detected in the
CC tracheal placodes at stage 8, and expression continues throughout
CC embryonic and larval development. In the developing salivary gland,
CC expression is observed in the entire gland at stage 9 and by stage 12,
CC expression is confined to the salivary ducts.
CC {ECO:0000269|PubMed:8557198}.
CC -!- PTM: Ser-673 phosphorylation by PKB/Akt1 is required for nuclear
CC targeting and transcriptional activity. {ECO:0000269|PubMed:11740943}.
CC -!- DISRUPTION PHENOTYPE: Tube-forming cells of the salivary gland,
CC trachea, and filzkorper fail to invaginate to form tubes and remain on
CC the embryo surface (PubMed:8557189). In embryo Malpighian tubules, cell
CC rearrangement is incomplete and the resulting tubules are wider than
CC normal (PubMed:10502111). {ECO:0000269|PubMed:10502111,
CC ECO:0000269|PubMed:8557189}.
CC -!- MISCELLANEOUS: Readthrough of the terminator UGA may occur between the
CC codons for 958-Ser and 960-Val.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA96754.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM11264.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U33427; AAA96257.1; ALT_INIT; mRNA.
DR EMBL; U42699; AAA96754.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF47386.1; -; Genomic_DNA.
DR EMBL; AE014296; ABI31226.1; -; Genomic_DNA.
DR EMBL; BT031114; ABX00736.1; -; mRNA.
DR EMBL; AY094911; AAM11264.1; ALT_INIT; mRNA.
DR RefSeq; NP_001036575.1; NM_001043110.2. [Q24119-3]
DR RefSeq; NP_001097461.2; NM_001103991.2. [Q24119-6]
DR RefSeq; NP_001261207.1; NM_001274278.1. [Q24119-5]
DR RefSeq; NP_523872.2; NM_079148.3. [Q24119-1]
DR BioGRID; 63620; 8.
DR IntAct; Q24119; 4.
DR STRING; 7227.FBpp0306032; -.
DR iPTMnet; Q24119; -.
DR PaxDb; Q24119; -.
DR EnsemblMetazoa; FBtr0304120; FBpp0293063; FBgn0262139. [Q24119-1]
DR EnsemblMetazoa; FBtr0304121; FBpp0293064; FBgn0262139. [Q24119-3]
DR EnsemblMetazoa; FBtr0304122; FBpp0293065; FBgn0262139. [Q24119-6]
DR EnsemblMetazoa; FBtr0330146; FBpp0303179; FBgn0262139. [Q24119-5]
DR EnsemblMetazoa; FBtr0330147; FBpp0303180; FBgn0262139. [Q24119-2]
DR GeneID; 38065; -.
DR KEGG; dme:Dmel_CG42865; -.
DR UCSC; CG6883-RB; d. melanogaster.
DR CTD; 7200; -.
DR FlyBase; FBgn0262139; trh.
DR VEuPathDB; VectorBase:FBgn0262139; -.
DR eggNOG; KOG3558; Eukaryota.
DR GeneTree; ENSGT00940000174266; -.
DR InParanoid; Q24119; -.
DR PhylomeDB; Q24119; -.
DR SignaLink; Q24119; -.
DR BioGRID-ORCS; 38065; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Hn; fly.
DR GenomeRNAi; 38065; -.
DR PRO; PR:Q24119; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262139; Expressed in embryonic/larval salivary gland (Drosophila) and 37 other tissues.
DR ExpressionAtlas; Q24119; baseline and differential.
DR Genevisible; Q24119; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IPI:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0048736; P:appendage development; IMP:FlyBase.
DR GO; GO:0007425; P:epithelial cell fate determination, open tracheal system; IMP:FlyBase.
DR GO; GO:0072175; P:epithelial tube formation; IMP:FlyBase.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007431; P:salivary gland development; IMP:UniProtKB.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IMP:FlyBase.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1022
FT /note="Protein trachealess"
FT /id="PRO_0000127476"
FT DOMAIN 86..139
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 174..244
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 391..461
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 465..508
FT /note="PAC"
FT REGION 58..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 629..636
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 673
FT /note="Phosphoserine; by PKB/Akt1"
FT /evidence="ECO:0000269|PubMed:11740943"
FT VAR_SEQ 2..82
FT /note="LPYQAAVAMDYAGYQRQPTPGHPGSHMATMGSLGMPAVPFTHSWMVPTQDLC
FT AMPPYNKMTGHQQPPGAGMHAQQQPLEPG -> EHHGSGFVASPWAAVLGHHSMASDAG
FT FAAAAAAAHVQNHSMHHPIHSHHHHHSHSHPHPHPHSHPHHHPHLGTAGGMPMDLHVPQ
FT GFPYYRYREDALCWGDRKSMEEIGAAQSSVNAR (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_043931"
FT VAR_SEQ 281..286
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:8557198"
FT /id="VSP_043932"
FT VAR_SEQ 328..356
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8557198, ECO:0000303|Ref.5"
FT /id="VSP_043933"
FT VAR_SEQ 959..1022
FT /note="Missing (in isoform A, isoform B, isoform C and
FT isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8557189, ECO:0000303|PubMed:8557198,
FT ECO:0000303|Ref.5"
FT /id="VSP_043934"
FT MUTAGEN 233
FT /note="I->N: Malpighian tubules empty into a single large
FT sack that is attached to the hindgut and no ureters are
FT evident. Distal segments of the tubules are tubular but
FT fail to elongate or undergo cell rearrangement, resulting
FT in tubules that are shorter and wider than normal. Hindguts
FT are normal in shape but shortened."
FT /evidence="ECO:0000269|PubMed:10502111"
FT MUTAGEN 579
FT /note="S->A: No effect on phosphorylation by Akt1; no
FT effect on transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11740943"
FT MUTAGEN 673
FT /note="S->A: Abolishes phosphorylation by Akt1, nuclear
FT localization, and transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11740943"
FT MUTAGEN 673
FT /note="S->D: Slightly increases transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11740943"
FT CONFLICT 78
FT /note="P -> A (in Ref. 1; AAA96257)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="G -> GG (in Ref. 2; AAA96754)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="S -> P (in Ref. 5; ABX00736)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="A -> T (in Ref. 1; AAA96257)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="A -> P (in Ref. 1; AAA96257)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="A -> V (in Ref. 1; AAA96257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1022 AA; 109260 MW; CDF4C8CE3FB38E37 CRC64;
MLPYQAAVAM DYAGYQRQPT PGHPGSHMAT MGSLGMPAVP FTHSWMVPTQ DLCAMPPYNK
MTGHQQPPGA GMHAQQQPLE PGILELRKEK SRDAARSRRG KENYEFYELA KMLPLPAAIT
SQLDKASIIR LTISYLKLRD FSGHGDPPWT REASSSSKLK SAAIRRSPAV DLFEQHQGTH
ILQSLDGFAL AVAADGRFLY ISETVSIYLG LSQVEMTGSS IFDYIHQADH SEIADQLGLS
LTSGGGGGGG SSSSGGGGGG AGGGMASPTS GASDDGSGTH GTNNPDVAAS MTQASTSGYK
GYDRSFCVRM KSTLTKRGCH FKSSGYRASD ATSNCNNGNN ASNNAKNVKN PGSNYSVVLL
LCKLRPQYTF SHSRKSQPPL LGMVALAIAL PPPSVHEIRL ECDMFVTRVN FDLRVAHCEP
RVSDLLDYSP EDLVNKSLYS LCHAEDANRL RKSHSDLIEK GQVLTGYYRL MNKSGGYTWL
QTCATVVCST KNADEQNIIC VNYVISNREN ENMILDCCQL EPSPDSIKHE EGLGNDKSSG
SPGGDASGEG NSHLSAGDMK LNSPKTDSEG HSHRGRGRSA AASHGSSMNS LTMIKDSPTP
LGVEIDSGVL PTTVATPVPA ATPPVQSTKR KRKTKASQHA EDQGQEQVIS EQPLPKLPTM
EQRDQQPRSR LPSIVDEQPS SAADSAVKDL EQAMSKHLPS PAAVVSVAPP NTDFSADSLL
KQQQQQQQLD PNEKSSTIQW IGTPYQQPPA PMPATALLRQ LYANRESVIR ATARQTPTGV
GPGVFYGDQQ TGPLPTPPGS ESSYENQYLQ LHSAASGGHP GGQKTSADAF TNLVSTYGGY
HSSIDYHNAM TPPSSVSPRD SNQPGKAAPV LASNGGYDYA PDPLRGQYAT SSGDVVPATL
PLKPQASYTA TMHPSGSTTT EGGVTYSNLD QPQYFAPHSS FHLYHKGSPA SGWYSTPSXV
VDDQGQVPPS CQDQYHHHHH HHHHQDGSAG SSASQASERW DFVGALGKVA RMFFSARKGN
PG
