Protein mothers against dpp

 MAD_DROME               Reviewed;         455 AA.
 P42003; Q9VQM3;
 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1995, sequence version 1.
 02-DEC-2020, entry version 188.
 RecName: Full=Protein mothers against dpp;
 Name=Mad; ORFNames=CG12399;
 Drosophila melanogaster (Fruit fly).
 Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
 Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea;
 Drosophilidae; Drosophila; Sophophora.
 NCBI_TaxID=7227;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF
 GLY-409 AND SER-421, AND DISRUPTION PHENOTYPE.
 PubMed=7768443;
 Sekelsky J.J., Newfeld S.J., Raftery L.A., Chartoff E.H., Gelbart W.M.;
 "Genetic characterization and cloning of mothers against dpp, a gene
 required for decapentaplegic function in Drosophila melanogaster.";
 Genetics 139:1347-1358(1995).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=Berkeley;
 PubMed=10731132; DOI=10.1126/science.287.5461.2185;
 Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
 Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
 George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
 Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
 Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
 Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
 An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
 Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
 Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
 Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
 Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
 Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
 Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
 Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
 Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
 Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
 Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
 Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
 Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
 Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
 Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
 McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
 Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
 Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
 Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
 Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
 Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
 Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
 Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
 Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
 Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
 Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
 Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
 Venter J.C.;
 "The genome sequence of Drosophila melanogaster.";
 Science 287:2185-2195(2000).
 [3]
 GENOME REANNOTATION.
 STRAIN=Berkeley;
 PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
 Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
 Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
 Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
 Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
 Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
 Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
 "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
 review.";
 Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=Berkeley; TISSUE=Embryo;
 Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
 Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
 Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
 Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
 Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
 Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
 [5]
 INTERACTION WITH SMURF.
 PubMed=11703946; DOI=10.1016/s1534-5807(01)00057-0;
 Podos S.D., Hanson K.K., Wang Y.-C., Ferguson E.L.;
 "The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and
 temporally during Drosophila embryogenesis.";
 Dev. Cell 1:567-578(2001).
 [6]
 TISSUE SPECIFICITY.
 PubMed=11997505; DOI=10.1128/mcb.22.11.3685-3697.2002;
 Sem K.P., Zahedi B., Tan I., Deak M., Lim L., Harden N.;
 "ACK family tyrosine kinase activity is a component of Dcdc42 signaling
 during dorsal closure in Drosophila melanogaster.";
 Mol. Cell. Biol. 22:3685-3697(2002).
 [7]
 INTERACTION WITH SMURF, PHOSPHORYLATION AT SER-453 AND SER-455, MUTAGENESIS
 OF SER-453 AND SER-455, AND UBIQUITINATION.
 PubMed=12754252; DOI=10.1074/jbc.c300028200;
 Liang Y.-Y., Lin X., Liang M., Brunicardi F.C., ten Dijke P., Chen Z.,
 Choi K.-W., Feng X.-H.;
 "DSmurf selectively degrades decapentaplegic-activated MAD, and its
 overexpression disrupts imaginal disc development.";
 J. Biol. Chem. 278:26307-26310(2003).
 [8]
 FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-25.
 PubMed=17507407; DOI=10.1242/dev.02853;
 Zeng Y.A., Rahnama M., Wang S., Sosu-Sedzorme W., Verheyen E.M.;
 "Drosophila Nemo antagonizes BMP signaling by phosphorylation of Mad and
 inhibition of its nuclear accumulation.";
 Development 134:2061-2071(2007).
 [9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-455, AND
 IDENTIFICATION BY MASS SPECTROMETRY.
 TISSUE=Embryo;
 PubMed=18327897; DOI=10.1021/pr700696a;
 Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
 "Phosphoproteome analysis of Drosophila melanogaster embryos.";
 J. Proteome Res. 7:1675-1682(2008).
 [10]
 INTERACTION WITH MAN1.
 PubMed=20036230; DOI=10.1016/j.ydbio.2009.11.036;
 Wagner N., Weyhersmueller A., Blauth A., Schuhmann T., Heckmann M.,
 Krohne G., Samakovlis C.;
 "The Drosophila LEM-domain protein MAN1 antagonizes BMP signaling at the
 neuromuscular junction and the wing crossveins.";
 Dev. Biol. 339:1-13(2010).
 [11]
 INTERACTION WITH SEC13 AND NUP93-1.
 PubMed=20547758; DOI=10.1128/mcb.00124-10;
 Chen X., Xu L.;
 "Specific nucleoporin requirement for Smad nuclear translocation.";
 Mol. Cell. Biol. 30:4022-4034(2010).
 [12]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-455, AND SUBUNIT.
 PubMed=19557331; DOI=10.1007/s11427-009-0080-x;
 Wang C., Chen L., Wang L., Wu J.;
 "Crystal structure of the MH2 domain of Drosophila Mad.";
 Sci. China, Ser. C, Life Sci. 52:539-544(2009).
 -!- FUNCTION: Required for the function of decapentaplegic. May play an
     important role in mediating Dpp signaling. Involved in the BMP
     signaling pathway. {ECO:0000269|PubMed:17507407,
     ECO:0000269|PubMed:7768443}.
 -!- SUBUNIT: Homotrimer (PubMed:19557331). Interacts with MAN1
     (PubMed:20036230). Interacts with Sec13 and Nup93-1 (PubMed:20547758).
     {ECO:0000269|PubMed:19557331, ECO:0000269|PubMed:20036230,
     ECO:0000269|PubMed:20547758}.
 -!- INTERACTION:
     P42003; Q7KNS3: Lis-1; NbExp=2; IntAct=EBI-162238, EBI-156005;
     P42003; Q45VV3: yki; NbExp=2; IntAct=EBI-162238, EBI-141254;
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17507407}. Nucleus
     {ECO:0000269|PubMed:17507407}.
 -!- TISSUE SPECIFICITY: Stage 13 embryos display expression in the dorsal
     epidermis (at protein level). {ECO:0000269|PubMed:11997505}.
 -!- DEVELOPMENTAL STAGE: Is detected in all developmental stages, though it
     appears most abundant in pupae, adult stages and early embryos. Its
     abundance decreases throughout embryonic and larval development and
     then returns to high levels in pupae and adult females.
     {ECO:0000269|PubMed:7768443}.
 -!- PTM: Phosphorylation on Ser-453 and/or Ser-455 is required for
     interaction with Smurf (PubMed:12754252, PubMed:18327897).
     Phosphorylation on Ser-25 by key/Nemo promotes export from nucleus and
     antagonizes BMP signaling (PubMed:17507407).
     {ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:17507407,
     ECO:0000269|PubMed:18327897}.
 -!- PTM: Ubiquitinated by Smurf upon phosphorylation; which promotes
     proteasomal degradation. {ECO:0000269|PubMed:12754252}.
 -!- DISRUPTION PHENOTYPE: Mutants exhibit defects in midgut morphogenesis,
     imaginal disk development and embryonic dorsal-ventral patterning that
     are very reminiscent of dpp mutant phenotypes.
     {ECO:0000269|PubMed:7768443}.
 -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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 EMBL; U10328; AAB60230.1; -; mRNA.
 EMBL; AE014134; AAF51142.1; -; Genomic_DNA.
 EMBL; BT004845; AAO45201.1; -; mRNA.
 PIR; S55019; S55019.
 RefSeq; NP_477017.1; NM_057669.3.
 PDB; 3DIT; X-ray; 3.20 A; A/B/C=259-446.
 PDB; 3GMJ; X-ray; 2.80 A; A/B/C/D=215-455.
 PDBsum; 3DIT; -.
 PDBsum; 3GMJ; -.
 SMR; P42003; -.
 BioGRID; 59745; 104.
 DIP; DIP-18256N; -.
 IntAct; P42003; 47.
 STRING; 7227.FBpp0304648; -.
 iPTMnet; P42003; -.
 PaxDb; P42003; -.
 EnsemblMetazoa; FBtr0077616; FBpp0077302; FBgn0011648.
 GeneID; 33529; -.
 KEGG; dme:Dmel_CG12399; -.
 CTD; 33529; -.
 FlyBase; FBgn0011648; Mad.
 eggNOG; KOG3701; Eukaryota.
 GeneTree; ENSGT00940000163092; -.
 HOGENOM; CLU_026736_0_2_1; -.
 InParanoid; P42003; -.
 OrthoDB; 608001at2759; -.
 PhylomeDB; P42003; -.
 Reactome; R-DME-201451; Signaling by BMP.
 Reactome; R-DME-5689880; Ub-specific processing proteases.
 Reactome; R-DME-8941326; RUNX2 regulates bone development.
 SignaLink; P42003; -.
 BioGRID-ORCS; 33529; 0 hits in 3 CRISPR screens.
 EvolutionaryTrace; P42003; -.
 GenomeRNAi; 33529; -.
 PRO; PR:P42003; -.
 Proteomes; UP000000803; Chromosome 2L.
 Bgee; FBgn0011648; Expressed in wing disc (Drosophila) and 44 other tissues.
 ExpressionAtlas; P42003; baseline and differential.
 Genevisible; P42003; DM.
 GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
 GO; GO:0005829; C:cytosol; IDA:FlyBase.
 GO; GO:0071144; C:heteromeric SMAD protein complex; IDA:FlyBase.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:FlyBase.
 GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
 GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
 GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
 GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
 GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:FlyBase.
 GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
 GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
 GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
 GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
 GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
 GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
 GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
 GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
 GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
 GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
 GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
 GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
 GO; GO:0007507; P:heart development; TAS:FlyBase.
 GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
 GO; GO:0007560; P:imaginal disc morphogenesis; IMP:FlyBase.
 GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
 GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
 GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
 GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
 GO; GO:0045705; P:negative regulation of salivary gland boundary specification; TAS:FlyBase.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
 GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
 GO; GO:1904398; P:positive regulation of neuromuscular junction development; IMP:FlyBase.
 GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
 GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
 GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
 GO; GO:0060395; P:SMAD protein signal transduction; IDA:FlyBase.
 GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
 GO; GO:0060799; P:transforming growth factor beta receptor signaling pathway involved in endodermal cell fate specification; IMP:FlyBase.
 GO; GO:0035290; P:trunk segmentation; IMP:FlyBase.
 GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
 GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
 Gene3D; 2.60.200.10; -; 1.
 Gene3D; 3.90.520.10; -; 1.
 InterPro; IPR013790; Dwarfin.
 InterPro; IPR003619; MAD_homology1_Dwarfin-type.
 InterPro; IPR013019; MAD_homology_MH1.
 InterPro; IPR017855; SMAD-like_dom_sf.
 InterPro; IPR001132; SMAD_dom_Dwarfin-type.
 InterPro; IPR008984; SMAD_FHA_dom_sf.
 InterPro; IPR036578; SMAD_MH1_sf.
 PANTHER; PTHR13703; PTHR13703; 1.
 Pfam; PF03165; MH1; 1.
 Pfam; PF03166; MH2; 1.
 SMART; SM00523; DWA; 1.
 SMART; SM00524; DWB; 1.
 SUPFAM; SSF49879; SSF49879; 1.
 SUPFAM; SSF56366; SSF56366; 1.
 PROSITE; PS51075; MH1; 1.
 PROSITE; PS51076; MH2; 1.
 1: Evidence at protein level;
 3D-structure; Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
 Nucleus; Phosphoprotein; Reference proteome; Transcription;
 Transcription regulation; Ubl conjugation; Zinc.
 CHAIN           1..455
                 /note="Protein mothers against dpp"
                 /id="PRO_0000090878"
 DOMAIN          26..150
                 /note="MH1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
 DOMAIN          261..455
                 /note="MH2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
 REGION          221..225
                 /note="Interaction with lack"
 METAL           78
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           123
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           135
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           140
                 /note="Zinc"
                 /evidence="ECO:0000250"
 MOD_RES         25
                 /note="Phosphoserine"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
                 ECO:0000269|PubMed:17507407"
 MOD_RES         453
                 /note="Phosphoserine"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
                 ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
 MOD_RES         455
                 /note="Phosphoserine"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
                 ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
 MUTAGEN         25
                 /note="S->A: Abolishes phosphorylation."
 MUTAGEN         409
                 /note="G->S: In allele Mad-10; pupal lethal."
                 /evidence="ECO:0000269|PubMed:7768443"
 MUTAGEN         421
                 /note="S->L: In allele Mad-9; lethal."
                 /evidence="ECO:0000269|PubMed:7768443"
 MUTAGEN         453
                 /note="S->A: Abolishes interaction with lack; when
                 associated with A-455."
                 /evidence="ECO:0000269|PubMed:12754252"
 MUTAGEN         455
                 /note="S->A: Abolishes interaction with lack; when
                 associated with A-453."
                 /evidence="ECO:0000269|PubMed:12754252"
 STRAND          261..268
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          271..279
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          281..289
                 /evidence="ECO:0000244|PDB:3GMJ"
 TURN            294..296
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          297..300
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           301..303
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           311..320
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          324..329
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          332..337
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          339..341
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          343..346
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           348..353
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          362..364
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          369..373
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           375..384
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           386..388
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           391..396
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           397..400
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          401..408
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          411..415
                 /evidence="ECO:0000244|PDB:3DIT"
 HELIX           419..421
                 /evidence="ECO:0000244|PDB:3GMJ"
 STRAND          422..430
                 /evidence="ECO:0000244|PDB:3GMJ"
 HELIX           431..441
                 /evidence="ECO:0000244|PDB:3GMJ"
 SEQUENCE   455 AA;  50505 MW;  6C8570674C3AB9D8 CRC64;
 MDTDDVESNT SSAMSTLGSL FSFTSPAVKK LLGWKQGDEE EKWAEKAVDS LVKKLKKRKG
 AIEELERALS CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL
 ELCQYPFSAK QKEVCINPYH YKRVESPVLP PVLVPRHSEF APGHSMLQFN HVAEPSMPHN
 VSYSNSGFNS HSLSTSNTSV GSPSSVNSNP NSPYDSLAGT PPPAYSPSED GNSNNPNDGG
 QLLDAQMGDV AQVSYSEPAF WASIAYYELN CRVGEVFHCN NNSVIVDGFT NPSNNSDRCC
 LGQLSNVNRN STIENTRRHI GKGVHLYYVT GEVYAECLSD SAIFVQSRNC NYHHGFHPST
 VCKIPPGCSL KIFNNQEFAQ LLSQSVNNGF EAVYELTKMC TIRMSFVKGW GAEYHRQDVT
 STPCWIEIHL HGPLQWLDKV LTQMGSPHNA ISSVS

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