EZ_DROME
ID EZ_DROME Reviewed; 760 AA.
AC P42124; B7Z0G2; Q9VTA3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Histone-lysine N-methyltransferase E(z);
DE EC=2.1.1.356;
DE AltName: Full=Lysine N-methyltransferase 6;
DE AltName: Full=Protein enhancer of zeste;
GN Name=E(z); Synonyms=KMT6; ORFNames=CG6502;
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].
RX PubMed=8413234; DOI=10.1128/mcb.13.10.6357-6366.1993;
RA Jones R.S., Gelbart W.M.;
RT "The Drosophila Polycomb-group gene Enhancer of zeste contains a region
RT with sequence similarity to trithorax.";
RL Mol. Cell. Biol. 13:6357-6366(1993).
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=Ovary;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9012527; DOI=10.1242/dev.122.12.4073;
RA Carrington E.A., Jones R.S.;
RT "The Drosophila Enhancer of zeste gene encodes a chromosomal protein:
RT examination of wild-type and mutant protein distribution.";
RL Development 122:4073-4083(1996).
RN [6]
RP INTERACTION WITH ESC.
RX PubMed=9566901; DOI=10.1128/mcb.18.5.2825;
RA Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.;
RT "The Drosophila esc and E(z) proteins are direct partners in polycomb
RT group-mediated repression.";
RL Mol. Cell. Biol. 18:2825-2834(1998).
RN [7]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND HDAC1.
RX PubMed=11124122; DOI=10.1242/dev.128.2.275;
RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
RT "The Drosophila polycomb group proteins ESC and E(Z) are present in a
RT complex containing the histone-binding protein p55 and the histone
RT deacetylase RPD3.";
RL Development 128:275-286(2001).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; PHO AND ESC, AND TRANSIENT
RP INTERACTION WITH THE PRC1 COMPLEX.
RX PubMed=11581156; DOI=10.1101/gad.208901;
RA Poux S., Melfi R., Pirrotta V.;
RT "Establishment of Polycomb silencing requires a transient interaction
RT between PC and ESC.";
RL Genes Dev. 15:2509-2514(2001).
RN [9]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; HDAC1 AND SU(Z)12,
RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, AND MUTAGENESIS OF
RP 702-ASN-HIS-703.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [10]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND SU(Z)12,
RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, AND MUTAGENESIS OF ARG-699 AND
RP HIS-703.
RX PubMed=12408864; DOI=10.1016/s0092-8674(02)00976-5;
RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B.,
RA Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
RT "Histone methyltransferase activity of a Drosophila Polycomb group
RT repressor complex.";
RL Cell 111:197-208(2002).
RN [11]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND HDAC1.
RX PubMed=12533794; DOI=10.1002/gene.10173;
RA Furuyama T., Tie F., Harte P.J.;
RT "Polycomb group proteins ESC and E(Z) are present in multiple distinct
RT complexes that undergo dynamic changes during development.";
RL Genesis 35:114-124(2003).
RN [12]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; PCL; HDAC1 AND
RP SU(Z)12.
RX PubMed=12697833; DOI=10.1128/mcb.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike
RT and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [13]
RP INTERACTION WITH CORTO.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493 AND THR-502, 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 [15]
RP INTERACTION WITH NUP93-1.
RX PubMed=31784359; DOI=10.1016/j.molcel.2019.10.017;
RA Gozalo A., Duke A., Lan Y., Pascual-Garcia P., Talamas J.A., Nguyen S.C.,
RA Shah P.P., Jain R., Joyce E.F., Capelson M.;
RT "Core Components of the Nuclear Pore Bind Distinct States of Chromatin and
RT Contribute to Polycomb Repression.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' of histone H3,
CC leading to transcriptional repression of the affected target gene.
CC While PcG proteins are generally required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development, this protein is specifically required during the first 6
CC hours of embryogenesis to establish the repressed state. The Esc/E(z)
CC complex is necessary but not sufficient for the repression of homeotic
CC target genes, suggesting that the recruitment of the distinct PRC1
CC complex is also required.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC -!- SUBUNIT: Component of the Esc/E(z) complex, composed of Caf1-55, esc,
CC E(z), Su(z)12, and possibly pho. The Esc/E(z) complex may also
CC associate with Pcl and HDAC1/Rpd3 during early embryogenesis. This
CC complex is distinct from the PRC1 complex, which contains many other
CC PcG proteins like Pc, Ph, Psc, Su(z)2. The two complexes however
CC cooperate and interact together during the first 3 hours of development
CC to establish PcG silencing. Interacts with corto in vitro. Interacts
CC with Nup93-1 (PubMed:31784359). {ECO:0000269|PubMed:11124122,
CC ECO:0000269|PubMed:11581156, ECO:0000269|PubMed:12408863,
CC ECO:0000269|PubMed:12408864, ECO:0000269|PubMed:12533794,
CC ECO:0000269|PubMed:12697833, ECO:0000269|PubMed:12771214,
CC ECO:0000269|PubMed:31784359, ECO:0000269|PubMed:9566901}.
CC -!- INTERACTION:
CC P42124; Q9VEX9: Bin1; NbExp=7; IntAct=EBI-112315, EBI-129424;
CC P42124; Q24572: Caf1-55; NbExp=7; IntAct=EBI-112315, EBI-75924;
CC P42124; P41046: corto; NbExp=2; IntAct=EBI-112315, EBI-300379;
CC P42124; Q24338: esc; NbExp=21; IntAct=EBI-112315, EBI-88911;
CC P42124; Q95SW6: escl; NbExp=2; IntAct=EBI-112315, EBI-1207935;
CC P42124; Q94517: HDAC1; NbExp=9; IntAct=EBI-112315, EBI-302197;
CC P42124; Q24459: Pcl; NbExp=14; IntAct=EBI-112315, EBI-430086;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9012527}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; U00180; AAC46462.1; -; mRNA.
DR EMBL; AE014296; AAF50149.1; -; Genomic_DNA.
DR EMBL; AE014296; ACL83287.1; -; Genomic_DNA.
DR EMBL; AY051785; AAK93209.1; -; mRNA.
DR RefSeq; NP_001137932.1; NM_001144460.3.
DR RefSeq; NP_524021.2; NM_079297.3.
DR AlphaFoldDB; P42124; -.
DR SMR; P42124; -.
DR BioGRID; 64582; 45.
DR DIP; DIP-20386N; -.
DR IntAct; P42124; 23.
DR MINT; P42124; -.
DR STRING; 7227.FBpp0306192; -.
DR BindingDB; P42124; -.
DR ChEMBL; CHEMBL2169719; -.
DR iPTMnet; P42124; -.
DR PaxDb; P42124; -.
DR DNASU; 39203; -.
DR EnsemblMetazoa; FBtr0076279; FBpp0076008; FBgn0000629.
DR EnsemblMetazoa; FBtr0273338; FBpp0271846; FBgn0000629.
DR GeneID; 39203; -.
DR KEGG; dme:Dmel_CG6502; -.
DR CTD; 39203; -.
DR FlyBase; FBgn0000629; E(z).
DR VEuPathDB; VectorBase:FBgn0000629; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011342_0_0_1; -.
DR InParanoid; P42124; -.
DR OrthoDB; 875190at2759; -.
DR PhylomeDB; P42124; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR SignaLink; P42124; -.
DR BioGRID-ORCS; 39203; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39203; -.
DR PRO; PR:P42124; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000629; Expressed in oviduct (Drosophila) and 39 other tissues.
DR ExpressionAtlas; P42124; baseline and differential.
DR Genevisible; P42124; DM.
DR GO; GO:0000785; C:chromatin; NAS:UniProtKB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:FlyBase.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:FlyBase.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0140718; P:facultative heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
DR GO; GO:0031062; P:positive regulation of histone methylation; IMP:UniProtKB.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19218; SET_EZH2; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR044439; EZH2_SET.
DR InterPro; IPR041343; PRC2_HTH_1.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR45747; PTHR45747; 2.
DR Pfam; PF18118; PRC2_HTH_1; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01114; CXC; 1.
DR SMART; SM00717; SANT; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Developmental protein; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..760
FT /note="Histone-lysine N-methyltransferase E(z)"
FT /id="PRO_0000213989"
FT DOMAIN 443..491
FT /note="SANT"
FT DOMAIN 518..619
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 626..741
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 195..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 505..510
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 196..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 699
FT /note="R->A,H: Strongly reduces methyltransferase activity
FT of the Esc/E(z) complex."
FT /evidence="ECO:0000269|PubMed:12408864"
FT MUTAGEN 702..703
FT /note="NH->AA: Abolishes methyltransferase activity of the
FT Esc/E(z) complex."
FT /evidence="ECO:0000269|PubMed:12408863"
FT MUTAGEN 703
FT /note="H->A,K: Strongly reduces methyltransferase activity
FT of the Esc/E(z) complex."
FT /evidence="ECO:0000269|PubMed:12408864"
FT CONFLICT 185..187
FT /note="GTA -> STS (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="T -> P (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="G -> C (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="D -> E (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="E -> D (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> V (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> A (in Ref. 1; AAC46462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 86935 MW; 022360ED7772EB60 CRC64;
MNSTKVPPEW KRRVKSEYIK IRQQKRYKRA DEIKEAWIRN WDEHNHNVQD LYCESKVWQA
KPYDPPHVDC VKRAEVTSYN GIPSGPQKVP ICVINAVTPI PTMYTWAPTQ QNFMVEDETV
LHNIPYMGDE VLDKDGKFIE ELIKNYDGKV HGDKDPSFMD DAIFVELVHA LMRSYSKELE
EAAPGTATAI KTETLAKSKQ GEDDGVVDVD ADGESPMKLE KTDSKGDLTE VEKKETEEPL
ETEDADVKPD VEEVKDKLPF PAPIIFQAIS ANFPDKGTAQ ELKEKYIELT EHQDPERPQE
CTPNIDGIKA ESVSRERTMH SFHTLFCRRC FKYDCFLHRL QGHAGPNLQK RRYPELKPFA
EPCSNSCYML IDGMKEKLAA DSKTPPIDSC NEASSEDSND SNSQFSNKDF NHENSKDNGL
TVNSAAVAEI NSIMAGMMNI TSTQCVWTGA DQALYRVLHK VYLKNYCAIA HNMLTKTCRQ
VYEFAQKEDA EFSFEDLRQD FTPPRKKKKK QRLWSLHCRK IQLKKDSSSN HVYNYTPCDH
PGHPCDMNCS CIQTQNFCEK FCNCSSDCQN RFPGCRCKAQ CNTKQCPCYL AVRECDPDLC
QACGADQFKL TKITCKNVCV QRGLHKHLLM APSDIAGWGI FLKEGAQKNE FISEYCGEII
SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSINPNCY AKVMMVTGDH
RIGIFAKRAI QPGEELFFDY RYGPTEQLKF VGIEREMEIV
