STAT_DROME
ID STAT_DROME Reviewed; 761 AA.
AC Q24151; Q0KI43; Q24181; Q59DV7; Q5BIB0; Q8IN54; Q8SX55; Q9VDL8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Signal transducer and transcription activator;
DE Short=d-STAT;
DE AltName: Full=Protein marelle;
GN Name=Stat92E; Synonyms=MARE, mrL, Stat; ORFNames=CG4257;
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] (ISOFORM F), FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=8608595; DOI=10.1016/s0092-8674(00)81286-6;
RA Hou X.S., Melnick M.B., Perrimon N.;
RT "Marelle acts downstream of the Drosophila HOP/JAK kinase and encodes a
RT protein similar to the mammalian STATs.";
RL Cell 84:411-419(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PHOSPHORYLATION AT TYR-711, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=8608596; DOI=10.1016/s0092-8674(00)81287-8;
RA Yan R., Small S., Desplan C., Dearolf C.R., Darnell J.E. Jr.;
RT "Identification of a Stat gene that functions in Drosophila development.";
RL Cell 84:421-430(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 F).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-761 (ISOFORM F).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-711, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION.
RX PubMed=34644293; DOI=10.1371/journal.pgen.1009834;
RA Yang Y., Kong R., Goh F.G., Somers W.G., Hime G.R., Li Z., Cai Y.;
RT "dRTEL1 is essential for the maintenance of Drosophila male germline stem
RT cells.";
RL PLoS Genet. 17:e1009834-e1009834(2021).
CC -!- FUNCTION: Might play a role in signal transduction and activation of
CC transcription. Plays an important role in the segmental pattern
CC formation in the early embryo by activating specific stripes of pair
CC rule gene expression in early development as part of the Janus kinase-
CC STAT pathway (PubMed:8608595). Might play a role in male germline stem
CC cell maintenance (PubMed:34644293). {ECO:0000269|PubMed:34644293,
CC ECO:0000269|PubMed:8608595}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocated into the nucleus in response to phosphorylation.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=F; Synonyms=Long;
CC IsoId=Q24151-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q24151-3; Sequence=VSP_012752, VSP_006290;
CC Name=C; Synonyms=E, Short;
CC IsoId=Q24151-2; Sequence=VSP_006290;
CC Name=G;
CC IsoId=Q24151-4; Sequence=VSP_012752;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic, larval, pupal, and
CC adult stages, with some decrease in the late embryonic stages. The
CC expression is uniform in unfertilized or just fertilized eggs,
CC suggesting maternally deposited mRNA. At blastoderm stage, expression
CC pattern shows stripes, that are reminiscent of many pair rule genes
CC pattern.
CC -!- PTM: Tyrosine phosphorylated by hopscotch. Phosphorylation is required
CC for DNA-binding activity and dimerization.
CC {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:8608596}.
CC -!- DISRUPTION PHENOTYPE: Exibits aberrant expression of the pair rule gene
CC even-skipped at the cellular blastoderm stage, leading to larval
CC segmentation defects. {ECO:0000269|PubMed:8608595,
CC ECO:0000269|PubMed:8608596}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40070; AAC46984.1; -; mRNA.
DR EMBL; U46688; AAB02195.1; -; mRNA.
DR EMBL; AE014297; AAN14350.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14351.2; -; Genomic_DNA.
DR EMBL; AE014297; AAS65180.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52969.1; -; Genomic_DNA.
DR EMBL; BT021314; AAX33462.1; -; mRNA.
DR EMBL; AY094839; AAM11192.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014643.1; NM_001014643.2. [Q24151-4]
DR RefSeq; NP_001262757.1; NM_001275828.1. [Q24151-4]
DR RefSeq; NP_001262762.1; NM_001275833.1. [Q24151-1]
DR RefSeq; NP_732516.2; NM_169899.3. [Q24151-2]
DR RefSeq; NP_732517.2; NM_169900.3. [Q24151-3]
DR RefSeq; NP_996242.1; NM_206520.2. [Q24151-2]
DR RefSeq; NP_996243.1; NM_206521.2. [Q24151-1]
DR AlphaFoldDB; Q24151; -.
DR SMR; Q24151; -.
DR BioGRID; 67407; 63.
DR DIP; DIP-29510N; -.
DR IntAct; Q24151; 4.
DR STRING; 7227.FBpp0088489; -.
DR iPTMnet; Q24151; -.
DR PaxDb; Q24151; -.
DR PRIDE; Q24151; -.
DR DNASU; 42428; -.
DR EnsemblMetazoa; FBtr0089484; FBpp0088487; FBgn0016917. [Q24151-3]
DR EnsemblMetazoa; FBtr0089485; FBpp0088488; FBgn0016917. [Q24151-2]
DR EnsemblMetazoa; FBtr0089486; FBpp0088489; FBgn0016917. [Q24151-1]
DR EnsemblMetazoa; FBtr0089487; FBpp0088978; FBgn0016917. [Q24151-2]
DR EnsemblMetazoa; FBtr0100457; FBpp0099882; FBgn0016917. [Q24151-4]
DR EnsemblMetazoa; FBtr0334581; FBpp0306648; FBgn0016917. [Q24151-4]
DR EnsemblMetazoa; FBtr0334586; FBpp0306653; FBgn0016917. [Q24151-1]
DR GeneID; 42428; -.
DR KEGG; dme:Dmel_CG4257; -.
DR CTD; 42428; -.
DR FlyBase; FBgn0016917; Stat92E.
DR VEuPathDB; VectorBase:FBgn0016917; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR InParanoid; Q24151; -.
DR PhylomeDB; Q24151; -.
DR Reactome; R-DME-1059683; Interleukin-6 signaling.
DR Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-201556; Signaling by ALK.
DR Reactome; R-DME-209228; Formation of the activated STAT92E dimer and transport to the nucleus.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-209405; JAK/STAT pathway.
DR Reactome; R-DME-210671; Transcriptional repression by nuclear factors.
DR Reactome; R-DME-210688; Dephosphorylation by PTP61F phosphatases.
DR Reactome; R-DME-210693; STAT92E dimer dephosphorylated in the nucleus and transported to the cytosol.
DR Reactome; R-DME-3249367; STAT6-mediated induction of chemokines.
DR Reactome; R-DME-6783783; Interleukin-10 signaling.
DR Reactome; R-DME-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-DME-877300; Interferon gamma signaling.
DR Reactome; R-DME-877312; Regulation of IFNG signaling.
DR Reactome; R-DME-8854691; Interleukin-20 family signaling.
DR Reactome; R-DME-8983432; Interleukin-15 signaling.
DR Reactome; R-DME-8984722; Interleukin-35 Signalling.
DR Reactome; R-DME-8985947; Interleukin-9 signaling.
DR Reactome; R-DME-9008059; Interleukin-37 signaling.
DR Reactome; R-DME-9020591; Interleukin-12 signaling.
DR Reactome; R-DME-9020933; Interleukin-23 signaling.
DR Reactome; R-DME-9020956; Interleukin-27 signaling.
DR Reactome; R-DME-909733; Interferon alpha/beta signaling.
DR Reactome; R-DME-9701898; STAT3 nuclear events downstream of ALK signaling.
DR SignaLink; Q24151; -.
DR BioGRID-ORCS; 42428; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42428; -.
DR PRO; PR:Q24151; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0016917; Expressed in embryonic/larval hemocyte (Drosophila) and 66 other tissues.
DR ExpressionAtlas; Q24151; baseline and differential.
DR Genevisible; Q24151; DM.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005126; F:cytokine receptor binding; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; ISS:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0043697; P:cell dedifferentiation; IEP:FlyBase.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:FlyBase.
DR GO; GO:0071481; P:cellular response to X-ray; IMP:FlyBase.
DR GO; GO:0006952; P:defense response; IDA:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0008348; P:negative regulation of antimicrobial humoral response; IMP:FlyBase.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0007538; P:primary sex determination; IMP:FlyBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007379; P:segment specification; IMP:FlyBase.
DR GO; GO:0017145; P:stem cell division; IMP:FlyBase.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0042246; P:tissue regeneration; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR036535; STAT_N_sf.
DR InterPro; IPR013800; STAT_TF_alpha.
DR InterPro; IPR015988; STAT_TF_coiled-coil.
DR InterPro; IPR013801; STAT_TF_DNA-bd.
DR InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR InterPro; IPR013799; STAT_TF_prot_interaction.
DR PANTHER; PTHR11801; PTHR11801; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF01017; STAT_alpha; 1.
DR Pfam; PF02864; STAT_bind; 1.
DR Pfam; PF02865; STAT_int; 1.
DR SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF47655; SSF47655; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
KW Transcription; Transcription regulation.
FT CHAIN 1..761
FT /note="Signal transducer and transcription activator"
FT /id="PRO_0000182435"
FT DOMAIN 594..658
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT MOD_RES 711
FT /note="Phosphotyrosine; by JAK"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:8608596"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform B and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_012752"
FT VAR_SEQ 699..705
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:8608596"
FT /id="VSP_006290"
FT CONFLICT 105
FT /note="S -> T (in Ref. 2; AAB02195)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="L -> H (in Ref. 2; AAB02195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 86415 MW; BF3A622A29899161 CRC64;
MSLWKRISSH VDCEQRMAAY YEEKGMLELR LCLAPWIEDR IMSEQITPNT TDQLERVALK
FNEDLQQKLL STRTASDQAL KFRVVELCAL IQRISAVELY THLRSGLQKE LQLVTEKSVA
ATAGQSMPLN PYNMNNTPMV TGYMVDPSDL LAVSNSCNPP VVQGIGPIHN VQNTGIASPA
LGMVTPKVEL YEVQHQIMQS LNEFGNCANA LKLLAQNYSY MLNSTSSPNA EAAYRSLIDE
KAAIVLTMRR SFMYYESLHE MVIHELKNWR HQQAQAGNGA PFNEGSLDDI QRCFEMLESF
IAHMLAAVKE LMRVRLVTEE PELTHLLEQV QNAQKNLVCS AFIVDKQPPQ VMKTNTRFAA
SVRWLIGSQL GIHNNPPTVE CIIMSEIQSQ RFVTRNTQMD NSSLSGQSSG EIQNASSTME
YQQNNHVFSA SFRNMQLKKI KRAEKKGTES VMDEKFALFF YTTTTVNDFQ IRVWTLSLPV
VVIVHGNQEP QSWATITWDN AFAEIVRDPF MITDRVTWAQ LSVALNIKFG SCTGRSLTID
NLDFLYEKLQ REERSEYITW NQFCKEPMPD RSFTFWEWFF AIMKLTKDHM LGMWKAGCIM
GFINKTKAQT DLLRSVYGIG TFLLRFSDSE LGGVTIAYVN ENGLVTMLAP WTARDFQVLN
LADRIRDLDV LCWLHPSDRN ASPVKRDVAF GEFYSKRQEP EPLVLDPVTG YVKSTLHVHV
CRNGENGSTS GTPHHAQESM QLGNGDFGMA DFDTITNFEN F
