DTX_DROME
ID DTX_DROME Reviewed; 738 AA.
AC Q23985; A9YJA9; A9YJB1; A9YJB7; B3LF71; Q86P53; Q9W3Z1;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein deltex;
DE AltName: Full=Probable E3 ubiquitin-protein ligase deltex;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE AltName: Full=RING-type E3 ubiquitin transferase deltex {ECO:0000305};
GN Name=dx; ORFNames=CG3929;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8150285; DOI=10.1093/genetics/136.2.585;
RA Busseau I., Diederich R.J., Xu T., Artavanis-Tsakonas S.;
RT "A member of the Notch group of interacting loci, deltex encodes a
RT cytoplasmic basic protein.";
RL Genetics 136:585-596(1994).
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 Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-738.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-567, AND VARIANTS LEU-511 AND
RP GLN-514 INS.
RC STRAIN=ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141,
RC ZW142, ZW143, and ZW144;
RX PubMed=17989248; DOI=10.1101/gr.6691007;
RA Andolfatto P.;
RT "Hitchhiking effects of recurrent beneficial amino acid substitutions in
RT the Drosophila melanogaster genome.";
RL Genome Res. 17:1755-1762(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH NOTCH.
RX PubMed=7671825; DOI=10.1242/dev.121.8.2633;
RA Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M.,
RA Artavanis-Tsakonas S.;
RT "Deltex acts as a positive regulator of Notch signaling through
RT interactions with the Notch ankyrin repeats.";
RL Development 121:2633-2644(1995).
RN [8]
RP FUNCTION.
RX PubMed=11719214; DOI=10.1016/s0960-9822(01)00562-0;
RA Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C.,
RA Heitzler P.;
RT "Novel Notch alleles reveal a Deltex-dependent pathway repressing neural
RT fate.";
RL Curr. Biol. 11:1729-1738(2001).
RN [9]
RP FUNCTION, HOMOMULTIMERIZATION, AND MUTAGENESIS OF 476-ARG--PRO-484; HIS-571
RP AND HIS-574.
RX PubMed=11861487; DOI=10.1242/dev.129.4.1049;
RA Matsuno K., Ito M., Hori K., Miyashita F., Suzuki S., Kishi N.,
RA Artavanis-Tsakonas S., Okano H.;
RT "Involvement of a proline-rich motif and RING-H2 finger of Deltex in the
RT regulation of Notch signaling.";
RL Development 129:1049-1059(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-261, AND INTERACTION WITH
RP NOTCH.
RX PubMed=16271883; DOI=10.1016/j.str.2005.07.015;
RA Zweifel M.E., Leahy D.J., Barrick D.;
RT "Structure and Notch receptor binding of the tandem WWE domain of Deltex.";
RL Structure 13:1599-1611(2005).
CC -!- FUNCTION: Regulator of Notch signaling, a signaling pathway involved in
CC cell-cell communications that regulates a broad spectrum of cell-fate
CC determinations. Mainly acts as a positive regulator of Notch, but it
CC may also act as a negative regulator, depending on the developmental
CC and cell context. Mediates the antineural activity of Notch. May
CC function as a ubiquitin ligase protein in the Notch pathway.
CC {ECO:0000269|PubMed:11719214, ECO:0000269|PubMed:11861487,
CC ECO:0000269|PubMed:7671825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q61010};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homomultimer; the oligomerization is required for its
CC function. Interacts with the ankyrin repeats of Notch.
CC {ECO:0000269|PubMed:16271883, ECO:0000269|PubMed:7671825}.
CC -!- INTERACTION:
CC Q23985; P07207: N; NbExp=4; IntAct=EBI-190618, EBI-103438;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8150285}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at low levels throughout
CC embryogenesis and in larvae. {ECO:0000269|PubMed:8150285}.
CC -!- DOMAIN: The WWE domains are thought to mediate some protein-protein
CC interaction, and are frequently found in ubiquitin ligases.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39479.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U09789; AAA18501.1; -; mRNA.
DR EMBL; AE014298; AAF46170.1; -; Genomic_DNA.
DR EMBL; BT033059; ACE82582.1; -; mRNA.
DR EMBL; BT003476; AAO39479.1; ALT_INIT; mRNA.
DR EMBL; EU217842; ABW92761.1; -; Genomic_DNA.
DR EMBL; EU217843; ABW92762.1; -; Genomic_DNA.
DR EMBL; EU217844; ABW92763.1; -; Genomic_DNA.
DR EMBL; EU217845; ABW92764.1; -; Genomic_DNA.
DR EMBL; EU217846; ABW92765.1; -; Genomic_DNA.
DR EMBL; EU217847; ABW92766.1; -; Genomic_DNA.
DR EMBL; EU217848; ABW92767.1; -; Genomic_DNA.
DR EMBL; EU217849; ABW92768.1; -; Genomic_DNA.
DR EMBL; EU217850; ABW92769.1; -; Genomic_DNA.
DR EMBL; EU217851; ABW92770.1; -; Genomic_DNA.
DR EMBL; EU217852; ABW92771.1; -; Genomic_DNA.
DR EMBL; EU217853; ABW92772.1; -; Genomic_DNA.
DR PIR; S47857; S47857.
DR RefSeq; NP_511064.2; NM_078509.3.
DR PDB; 2A90; X-ray; 2.15 A; A=26-261.
DR PDBsum; 2A90; -.
DR AlphaFoldDB; Q23985; -.
DR SMR; Q23985; -.
DR BioGRID; 58076; 78.
DR DIP; DIP-18159N; -.
DR IntAct; Q23985; 8.
DR STRING; 7227.FBpp0070876; -.
DR iPTMnet; Q23985; -.
DR PaxDb; Q23985; -.
DR DNASU; 31589; -.
DR EnsemblMetazoa; FBtr0070914; FBpp0070876; FBgn0000524.
DR GeneID; 31589; -.
DR KEGG; dme:Dmel_CG3929; -.
DR UCSC; CG3929-RA; d. melanogaster.
DR CTD; 31589; -.
DR FlyBase; FBgn0000524; dx.
DR VEuPathDB; VectorBase:FBgn0000524; -.
DR eggNOG; ENOG502QQ9M; Eukaryota.
DR GeneTree; ENSGT00940000170587; -.
DR HOGENOM; CLU_030422_4_0_1; -.
DR InParanoid; Q23985; -.
DR OMA; SRMGSHR; -.
DR OrthoDB; 600021at2759; -.
DR PhylomeDB; Q23985; -.
DR Reactome; R-DME-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR SignaLink; Q23985; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 31589; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q23985; -.
DR GenomeRNAi; 31589; -.
DR PRO; PR:Q23985; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000524; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q23985; baseline and differential.
DR Genevisible; Q23985; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0007220; P:Notch receptor processing; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd09633; Deltex_C; 1.
DR DisProt; DP02460; -.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; PTHR12622; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF117839; SSF117839; 2.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Notch signaling pathway;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..738
FT /note="Protein deltex"
FT /id="PRO_0000219079"
FT DOMAIN 35..118
FT /note="WWE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 119..201
FT /note="WWE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 548..603
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..304
FT /note="Interaction with Notch"
FT REGION 216..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 480..484
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 216..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 511
FT /note="Q -> L (in strain: ZW141)"
FT /evidence="ECO:0000269|PubMed:17989248"
FT VARIANT 514
FT /note="Q -> QQ (in strain: ZW122)"
FT /evidence="ECO:0000269|PubMed:17989248"
FT MUTAGEN 476..484
FT /note="Missing: Dominant-negative mutant that inhibits
FT Notch signaling."
FT /evidence="ECO:0000269|PubMed:11861487"
FT MUTAGEN 571
FT /note="H->A: Loss of function. Abolishes
FT homomultimerization; when associated with A-574."
FT /evidence="ECO:0000269|PubMed:11861487"
FT MUTAGEN 574
FT /note="H->A: Loss of function. Abolishes
FT homomultimerization; when associated with A-571."
FT /evidence="ECO:0000269|PubMed:11861487"
FT CONFLICT 107..108
FT /note="AG -> R (in Ref. 1; AAA18501)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="F -> L (in Ref. 1; AAA18501)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="QL -> HV (in Ref. 1; AAA18501)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> L (in Ref. 1; AAA18501)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="R -> S (in Ref. 5; AAO39479)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="L -> V (in Ref. 1; AAA18501)"
FT /evidence="ECO:0000305"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2A90"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2A90"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2A90"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2A90"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2A90"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2A90"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2A90"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2A90"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2A90"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2A90"
SQ SEQUENCE 738 AA; 82186 MW; 7B1CF29E024D26AF CRC64;
MASSAGSAAS GSVVPGGGGS AASSCATMAL STAGSGGPPV NHAHAVCVWE FESRGKWLPY
SPAVSQHLER AHAKKLTRVM LSDADPSLEQ YYVNVRTMTQ ESEAETAGSG LLTIGVRRMF
YAPSSPAGKG TKWEWSGGSA DSNNDWRPYN MHVQCIIEDA WARGEQTLDL CNTHIGLPYT
INFCNLTQLR QPSGPMRSIR RTQQAPYPLV KLTPQQANQL KSNSASVSSQ YNTLPKLGDT
KSLHRVPMTR QQHPLPTSHQ VQQQQHQHQH QQQQQQQHHH QHQQQQHQQQ QQHQMQHHQI
HHQTAPRKPP KKHSEISTTN LRQILNNLNI FSSSTKHQSN MSTAASASSS SSSASLHHAN
HLSHAHFSHA KNMLTASMNS HHSRCSEGSL QSQRSSRMGS HRSRSRTRTS DTDTNSVKSH
RRRPSVDTVS TYLSHESKES LRSRNFAISV NDLLDCSLGS DEVFVPSLPP SSLGERAPVP
PPLPLHPRQQ QQQQQQQQQL QMQQQQQAQQ QQQQSIAGSI VGVDPASDMI SRFVKVVEPP
LWPNAQPCPM CMEELVHSAQ NPAISLSRCQ HLMHLQCLNG MIIAQQNEMN KNLFIECPVC
GIVYGEKVGN QPIGSMSWSI ISKNLPGHEG QNTIQIVYDI ASGLQTEEHP HPGRAFFAVG
FPRICYLPDC PLGRKVLRFL KIAFDRRLLF SIGRSVTTGR EDVVIWNSVD HKTQFNMFPD
PTYLQRTMQQ LVHLGVTD
