MAD_DROME
ID MAD_DROME Reviewed; 455 AA.
AC P42003; Q9VQM3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein mothers against dpp;
GN Name=Mad; ORFNames=CG12399;
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, DEVELOPMENTAL STAGE, MUTAGENESIS OF
RP GLY-409 AND SER-421, AND DISRUPTION PHENOTYPE.
RX PubMed=7768443; DOI=10.1093/genetics/139.3.1347;
RA Sekelsky J.J., Newfeld S.J., Raftery L.A., Chartoff E.H., Gelbart W.M.;
RT "Genetic characterization and cloning of mothers against dpp, a gene
RT required for decapentaplegic function in Drosophila melanogaster.";
RL Genetics 139:1347-1358(1995).
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 [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH SMURF.
RX PubMed=11703946; DOI=10.1016/s1534-5807(01)00057-0;
RA Podos S.D., Hanson K.K., Wang Y.-C., Ferguson E.L.;
RT "The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and
RT temporally during Drosophila embryogenesis.";
RL Dev. Cell 1:567-578(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11997505; DOI=10.1128/mcb.22.11.3685-3697.2002;
RA Sem K.P., Zahedi B., Tan I., Deak M., Lim L., Harden N.;
RT "ACK family tyrosine kinase activity is a component of Dcdc42 signaling
RT during dorsal closure in Drosophila melanogaster.";
RL Mol. Cell. Biol. 22:3685-3697(2002).
RN [7]
RP INTERACTION WITH SMURF, PHOSPHORYLATION AT SER-453 AND SER-455, MUTAGENESIS
RP OF SER-453 AND SER-455, AND UBIQUITINATION.
RX PubMed=12754252; DOI=10.1074/jbc.c300028200;
RA Liang Y.-Y., Lin X., Liang M., Brunicardi F.C., ten Dijke P., Chen Z.,
RA Choi K.-W., Feng X.-H.;
RT "DSmurf selectively degrades decapentaplegic-activated MAD, and its
RT overexpression disrupts imaginal disc development.";
RL J. Biol. Chem. 278:26307-26310(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-25.
RX PubMed=17507407; DOI=10.1242/dev.02853;
RA Zeng Y.A., Rahnama M., Wang S., Sosu-Sedzorme W., Verheyen E.M.;
RT "Drosophila Nemo antagonizes BMP signaling by phosphorylation of Mad and
RT inhibition of its nuclear accumulation.";
RL Development 134:2061-2071(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-455, AND
RP IDENTIFICATION BY 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 [10]
RP INTERACTION WITH MAN1.
RX PubMed=20036230; DOI=10.1016/j.ydbio.2009.11.036;
RA Wagner N., Weyhersmueller A., Blauth A., Schuhmann T., Heckmann M.,
RA Krohne G., Samakovlis C.;
RT "The Drosophila LEM-domain protein MAN1 antagonizes BMP signaling at the
RT neuromuscular junction and the wing crossveins.";
RL Dev. Biol. 339:1-13(2010).
RN [11]
RP INTERACTION WITH SEC13 AND NUP93-1.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-455, AND SUBUNIT.
RX PubMed=19557331; DOI=10.1007/s11427-009-0080-x;
RA Wang C., Chen L., Wang L., Wu J.;
RT "Crystal structure of the MH2 domain of Drosophila Mad.";
RL Sci. China, Ser. C, Life Sci. 52:539-544(2009).
CC -!- FUNCTION: Required for the function of decapentaplegic. May play an
CC important role in mediating Dpp signaling. Involved in the BMP
CC signaling pathway. {ECO:0000269|PubMed:17507407,
CC ECO:0000269|PubMed:7768443}.
CC -!- SUBUNIT: Homotrimer (PubMed:19557331). Interacts with MAN1
CC (PubMed:20036230). Interacts with Sec13 and Nup93-1 (PubMed:20547758).
CC {ECO:0000269|PubMed:19557331, ECO:0000269|PubMed:20036230,
CC ECO:0000269|PubMed:20547758}.
CC -!- INTERACTION:
CC P42003; Q7KNS3: Lis-1; NbExp=2; IntAct=EBI-162238, EBI-156005;
CC P42003; Q45VV3: yki; NbExp=2; IntAct=EBI-162238, EBI-141254;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17507407}. Nucleus
CC {ECO:0000269|PubMed:17507407}.
CC -!- TISSUE SPECIFICITY: Stage 13 embryos display expression in the dorsal
CC epidermis (at protein level). {ECO:0000269|PubMed:11997505}.
CC -!- DEVELOPMENTAL STAGE: Is detected in all developmental stages, though it
CC appears most abundant in pupae, adult stages and early embryos. Its
CC abundance decreases throughout embryonic and larval development and
CC then returns to high levels in pupae and adult females.
CC {ECO:0000269|PubMed:7768443}.
CC -!- PTM: Phosphorylation on Ser-453 and/or Ser-455 is required for
CC interaction with Smurf (PubMed:12754252, PubMed:18327897).
CC Phosphorylation on Ser-25 by key/Nemo promotes export from nucleus and
CC antagonizes BMP signaling (PubMed:17507407).
CC {ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:17507407,
CC ECO:0000269|PubMed:18327897}.
CC -!- PTM: Ubiquitinated by Smurf upon phosphorylation; which promotes
CC proteasomal degradation. {ECO:0000269|PubMed:12754252}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit defects in midgut morphogenesis,
CC imaginal disk development and embryonic dorsal-ventral patterning that
CC are very reminiscent of dpp mutant phenotypes.
CC {ECO:0000269|PubMed:7768443}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; U10328; AAB60230.1; -; mRNA.
DR EMBL; AE014134; AAF51142.1; -; Genomic_DNA.
DR EMBL; BT004845; AAO45201.1; -; mRNA.
DR PIR; S55019; S55019.
DR RefSeq; NP_477017.1; NM_057669.3.
DR PDB; 3DIT; X-ray; 3.20 A; A/B/C=259-446.
DR PDB; 3GMJ; X-ray; 2.80 A; A/B/C/D=215-455.
DR PDBsum; 3DIT; -.
DR PDBsum; 3GMJ; -.
DR AlphaFoldDB; P42003; -.
DR SMR; P42003; -.
DR BioGRID; 59745; 123.
DR DIP; DIP-18256N; -.
DR IntAct; P42003; 47.
DR STRING; 7227.FBpp0304648; -.
DR iPTMnet; P42003; -.
DR PaxDb; P42003; -.
DR EnsemblMetazoa; FBtr0077616; FBpp0077302; FBgn0011648.
DR GeneID; 33529; -.
DR KEGG; dme:Dmel_CG12399; -.
DR CTD; 33529; -.
DR FlyBase; FBgn0011648; Mad.
DR VEuPathDB; VectorBase:FBgn0011648; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000163092; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; P42003; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; P42003; -.
DR Reactome; R-DME-201451; Signaling by BMP.
DR Reactome; R-DME-8941326; RUNX2 regulates bone development.
DR SignaLink; P42003; -.
DR BioGRID-ORCS; 33529; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P42003; -.
DR GenomeRNAi; 33529; -.
DR PRO; PR:P42003; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011648; Expressed in wing disc and 32 other tissues.
DR ExpressionAtlas; P42003; baseline and differential.
DR Genevisible; P42003; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IPI: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; IDA:FlyBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; TAS:FlyBase.
DR GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045705; P:negative regulation of salivary gland boundary specification; TAS:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:1904398; P:positive regulation of neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060799; P:transforming growth factor beta receptor signaling pathway involved in endodermal cell fate specification; IMP:FlyBase.
DR GO; GO:0035290; P:trunk segmentation; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR DisProt; DP02623; -.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..455
FT /note="Protein mothers against dpp"
FT /id="PRO_0000090878"
FT DOMAIN 26..150
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 261..455
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 192..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..225
FT /note="Interaction with lack"
FT COMPBIAS 192..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
FT ECO:0000269|PubMed:17507407"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
FT ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
FT ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
FT MUTAGEN 25
FT /note="S->A: Abolishes phosphorylation."
FT MUTAGEN 409
FT /note="G->S: In allele Mad-10; pupal lethal."
FT /evidence="ECO:0000269|PubMed:7768443"
FT MUTAGEN 421
FT /note="S->L: In allele Mad-9; lethal."
FT /evidence="ECO:0000269|PubMed:7768443"
FT MUTAGEN 453
FT /note="S->A: Abolishes interaction with lack; when
FT associated with A-455."
FT /evidence="ECO:0000269|PubMed:12754252"
FT MUTAGEN 455
FT /note="S->A: Abolishes interaction with lack; when
FT associated with A-453."
FT /evidence="ECO:0000269|PubMed:12754252"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:3GMJ"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:3DIT"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3GMJ"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:3GMJ"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:3GMJ"
SQ 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
