NU301_DROME
ID NU301_DROME Reviewed; 2669 AA.
AC Q9W0T1; Q4V464; Q7KVD8; Q95VB8; Q960Y3; Q9W0T2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nucleosome-remodeling factor subunit NURF301;
DE AltName: Full=Enhancer of bithorax;
DE AltName: Full=Nucleosome-remodeling factor 215 kDa subunit;
DE Short=NURF-215;
GN Name=E(bx); ORFNames=CG32346, CG7022, Nurf301;
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 A), PROTEIN SEQUENCE OF 172-179;
RP 195-202; 508-516; 594-603; 673-678; 1186-1192; 1233-1239; 1249-1254;
RP 1561-1578; 1622-1639; 1731-1751 AND 1911-1937, IDENTIFICATION IN THE NURF
RP COMPLEX, FUNCTION, AND INTERACTION WITH TRL.
RX PubMed=11583616; DOI=10.1016/s1097-2765(01)00345-8;
RA Xiao H., Sandaltzopoulos R., Wang H.-M., Hamiche A., Ranallo R., Lee K.-M.,
RA Fu D., Wu C.;
RT "Dual functions of largest NURF subunit NURF301 in nucleosome sliding and
RT transcription factor interactions.";
RL Mol. Cell 8:531-543(2001).
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, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-701 AND 1029-2669 (ISOFORM D).
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 [5]
RP FUNCTION.
RX PubMed=8521501; DOI=10.1016/0092-8674(95)90216-3;
RA Tsukiyama T., Wu C.;
RT "Purification and properties of an ATP-dependent nucleosome remodeling
RT factor.";
RL Cell 83:1011-1020(1995).
RN [6]
RP FUNCTION.
RX PubMed=12502740; DOI=10.1101/gad.1032202;
RA Badenhorst P., Voas M., Rebay I., Wu C.;
RT "Biological functions of the ISWI chromatin remodeling complex NURF.";
RL Genes Dev. 16:3186-3198(2002).
RN [7]
RP FUNCTION.
RX PubMed=16264191; DOI=10.1101/gad.1342605;
RA Badenhorst P., Xiao H., Cherbas L., Kwon S.Y., Voas M., Rebay I.,
RA Cherbas P., Wu C.;
RT "The Drosophila nucleosome remodeling factor NURF is required for
RT Ecdysteroid signaling and metamorphosis.";
RL Genes Dev. 19:2540-2545(2005).
RN [8]
RP INTERACTION WITH HISTONE H3K4ME3.
RX PubMed=16728976; DOI=10.1038/nature04815;
RA Wysocka J., Swigut T., Xiao H., Milne T.A., Kwon S.Y., Landry J., Kauer M.,
RA Tackett A.J., Chait B.T., Badenhorst P., Wu C., Allis C.D.;
RT "A PHD finger of NURF couples histone H3 lysine 4 trimethylation with
RT chromatin remodelling.";
RL Nature 442:86-90(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-52; SER-55; SER-59;
RP SER-62; SER-1417; THR-1527; SER-2395; SER-2398 AND SER-2403, 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).
CC -!- FUNCTION: Histone-binding component of NURF (nucleosome remodeling
CC factor), a complex which catalyzes ATP-dependent nucleosome sliding and
CC facilitates transcription of chromatin. Specifically recognizes H3
CC tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC start sites of virtually all active genes. Required for homeotic gene
CC expression, proper larval blood cell development, normal male X
CC chromosome morphology, ecdysteroid signaling and metamorphosis.
CC {ECO:0000269|PubMed:11583616, ECO:0000269|PubMed:12502740,
CC ECO:0000269|PubMed:16264191, ECO:0000269|PubMed:8521501}.
CC -!- SUBUNIT: Component of the NURF complex composed of Caf1-55, E(bx),
CC Nurf-38 and Iswi. Interacts with Trl. Interacts with histone H3-K4Me3.
CC {ECO:0000269|PubMed:11583616, ECO:0000269|PubMed:16728976}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q9W0T1-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9W0T1-2; Sequence=VSP_020422;
CC Name=C;
CC IsoId=Q9W0T1-3; Sequence=VSP_020423, VSP_020424;
CC Name=D;
CC IsoId=Q9W0T1-4; Sequence=VSP_020422, VSP_020423, VSP_020424;
CC -!- DOMAIN: The second PHD-type zinc finger mediates binding to histone
CC H3K4Me3.
CC -!- MISCELLANEOUS: Highly susceptible to proteolysis.
CC -!- SIMILARITY: Belongs to the BPTF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY51526.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAY55558.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF417921; AAL16644.1; -; mRNA.
DR EMBL; AE014296; AAN11431.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47361.2; -; Genomic_DNA.
DR EMBL; AE014296; AAS64922.1; -; Genomic_DNA.
DR EMBL; AY051776; AAK93200.1; ALT_INIT; mRNA.
DR EMBL; BT023142; AAY55558.1; ALT_SEQ; mRNA.
DR EMBL; BT022131; AAY51526.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001163304.1; NM_001169833.2. [Q9W0T1-1]
DR RefSeq; NP_001261190.1; NM_001274261.1. [Q9W0T1-1]
DR RefSeq; NP_728505.1; NM_167817.3. [Q9W0T1-2]
DR RefSeq; NP_728507.1; NM_167819.3. [Q9W0T1-1]
DR RefSeq; NP_995946.1; NM_206224.3. [Q9W0T1-3]
DR AlphaFoldDB; Q9W0T1; -.
DR SMR; Q9W0T1; -.
DR BioGRID; 69297; 34.
DR IntAct; Q9W0T1; 10.
DR STRING; 7227.FBpp0304412; -.
DR iPTMnet; Q9W0T1; -.
DR PaxDb; Q9W0T1; -.
DR PRIDE; Q9W0T1; -.
DR EnsemblMetazoa; FBtr0072521; FBpp0072421; FBgn0000541. [Q9W0T1-1]
DR EnsemblMetazoa; FBtr0072522; FBpp0072422; FBgn0000541. [Q9W0T1-2]
DR EnsemblMetazoa; FBtr0072523; FBpp0089425; FBgn0000541. [Q9W0T1-3]
DR EnsemblMetazoa; FBtr0301348; FBpp0290562; FBgn0000541. [Q9W0T1-1]
DR EnsemblMetazoa; FBtr0301349; FBpp0290563; FBgn0000541. [Q9W0T1-4]
DR EnsemblMetazoa; FBtr0332104; FBpp0304414; FBgn0000541. [Q9W0T1-1]
DR GeneID; 44811; -.
DR KEGG; dme:Dmel_CG32346; -.
DR CTD; 44811; -.
DR FlyBase; FBgn0000541; E(bx).
DR VEuPathDB; VectorBase:FBgn0000541; -.
DR eggNOG; KOG1473; Eukaryota.
DR eggNOG; KOG1632; Eukaryota.
DR GeneTree; ENSGT00940000154830; -.
DR InParanoid; Q9W0T1; -.
DR OMA; CESDREF; -.
DR PhylomeDB; Q9W0T1; -.
DR SignaLink; Q9W0T1; -.
DR BioGRID-ORCS; 44811; 1 hit in 1 CRISPR screen.
DR ChiTaRS; E(bx); fly.
DR GenomeRNAi; 44811; -.
DR PRO; PR:Q9W0T1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000541; Expressed in brain and 28 other tissues.
DR ExpressionAtlas; Q9W0T1; baseline and differential.
DR Genevisible; Q9W0T1; DM.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0016589; C:NURF complex; IDA:FlyBase.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0030097; P:hemopoiesis; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:FlyBase.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0048515; P:spermatid differentiation; IMP:FlyBase.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR038028; BPTF.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45975; PTHR45975; 3.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF15612; WHIM1; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 3.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Chromatin regulator; Coiled coil;
KW Developmental protein; Direct protein sequencing; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2669
FT /note="Nucleosome-remodeling factor subunit NURF301"
FT /id="PRO_0000249322"
FT DOMAIN 188..248
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 2573..2643
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DNA_BIND 6..18
FT /note="A.T hook"
FT ZN_FING 339..386
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 2481..2546
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..121
FT /note="Required for function in nucleosome sliding"
FT REGION 505..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2181..2203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2283..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2382..2432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..515
FT /evidence="ECO:0000255"
FT COILED 688..720
FT /evidence="ECO:0000255"
FT COILED 2338..2373
FT /evidence="ECO:0000255"
FT COMPBIAS 37..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2403..2426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2497
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 2504
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 2510
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 2519
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1527
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2403
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1800..1819
FT /note="Missing (in isoform B and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_020422"
FT VAR_SEQ 2156..2159
FT /note="TNNI -> VSSF (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_020423"
FT VAR_SEQ 2160..2669
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_020424"
FT CONFLICT 307
FT /note="D -> Y (in Ref. 1; AAL16644)"
FT /evidence="ECO:0000305"
FT CONFLICT 2156
FT /note="T -> A (in Ref. 1; AAL16644)"
FT /evidence="ECO:0000305"
FT CONFLICT 2252
FT /note="S -> A (in Ref. 1; AAL16644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2669 AA; 300686 MW; 261FF7B7CEEF781B CRC64;
MSGRGSRKRG RPPKTPNERA SGRFNYQLLK KPKYLSEGKS QPSTPSASRG ISPQSDEGSR
SSHNNHTNRS RGSAAKRGRG RKSAVQPNTS SYSGRKGYES EYHYGSDFGD SEEDKSDNED
DMLLTPSDDE SLEVANESES EFSVCSFNQN GVGRPPRPPS PEPVWLQEGR QYAALDLPDS
SEDLFIANTH VLRALSIYEV LRRFRHMVRL SPFRFEDLCA ALACEEQSAL LTEVHIMLLK
AILREEDAQG THFGPLDQKD TVNISLYLID SITWPEVLRS YVESDKTFDR NVFHILSHTE
YPYTGIDNRL EVLQFLSDQF LTSNSIRDVM LQEGPIHYDD HCRVCHRLGD LLCCETCPAV
YHLECVDPPM NDVPTEDWQC GLCRSHKVSG VVDCVLPQEK QGVLIRHDSL GVDRHGRKYW
FIARRIFIED QENFTCWYYS TTSKLKLLLS RLDAEELETR LHSQITERRD EIERQMKLTE
TLTNEHKHTK RSVIEIEQEA KNELLEKEVL DEDEKDGDAK SESQSIEGTK KQEECKMVTR
QKSNQLTNGT LHFKLGMEQG FKNYVNQYST NPIALNKPQR NEERDKRRHL SHKFSLTTAS
DFKWIGITMG TTDNMITTLR QTLINFESNI AASFLNINWV VNKKIWNAAV MNARRPSEFA
VVLLLFQASL KSVVFANVWH EQLGHTTLQR ITSAEREERK KLEKREKRER DDEEERNRLA
FNYIKYTLGL KHQVWKQKGE EYRVHGQWGW LWLSSSRRCG VRARRAQPLT HNRVYVHYTM
GEENDVNEII LVDPRTQRFM QQCESSNVDG QVCHYLPDQY KNVKVIEDVT EKIKGHIDVS
KALNAPGRTY YSKVARKSRL DDLLDRRLKL AEVEEQMASK IPSDMKPLLV SSQNNTANSK
QTFLEKRLLR LTEVQAKGGP ANVNLELVNS LAKQIQTVRL QFSQLNRFAK VFRCYTKECN
TNSNAVSQIT QNTCYSPLCL QKARAKKELL LLLRKAHTAG NGSKETVAAI LGAVKKPSIL
EQKLTEGKRE STQVAVDDSE EGKPAESEAP LDLLQDWEHA RAHAVPFSDS LLTECILVDQ
ECVTNTKIKQ EVNASSGCNT TPDSNTQDSD KIDYIESMDV CSNVEIESTE DSIVTGLNSG
NAEDVDMTPG WRRKRNQKSK KSYIGTKDVL DQTLDKDIPL NKQNRRFPIT ARPVKRECVK
KYERETFENG NERVYSTSSP RGRVYLLNDA AKLYEQAVKT EDKSTITKKP SYSRYPLISN
FLTHKKKRSL LVLPRFELLK LARLGGKSST NGFHHAAKNN TIWQYQCSRP LFRTCWSYRT
SNATSLSSLA LQLRILWSCL RWDDMIAKPP STDGKHQVTT DTEIVTLELL KLRHSGRYGE
KTSYLRRKVV IPLEMPKTVR EVTSIRSGLR KRKRAESPQP TEPQITEEWV DEDKLELWEI
KFMGEKQEKA RLSAVTRSVA SRQLEASGSN GSNTSTNGAL GVAGRVQLAP KLSEDVKEKM
EQQLKLQRAV HQQRKLVATG EITRSVTPVK GQVIGSRRVI VKNPDGTTRI IQQAVTQVSR
TGGANTAAAA ASPTVGGSTS TQSNPSTSTP HKVQIIRGPD GKVSVRGLNP GQQLVQMPDG
KLHVLTTTTS SNSAGQGNKM KVPIKPASTS SSPAISSAQT TTNPVTPVIK QIAVKHVTKN
SATQSIASSS RVALPLAQIK NKLLLAQQQQ QSTSSSPATS SSPVQKIVSK VVNTSTSGQT
LQQVFVQSGS KLVVGQNAQG QKVIISTSAA QQQGTSPVQQ QQLVQSQPIQ QSPQQISMTQ
VGNQPTQKVI QQIVNTSNVQ QQIVVGGQRI ILSPGQTIVT QRNVPQSQAL QMVQQQIQTQ
QQQQQHHVVQ PQQQFVVQSN QIVQSSPSAQ TKLVKQLVVQ QQSQQTIEEK TQITTTDSNE
TGTQQVLVPN STLAQQLAQG KLQVATVNGQ QVIVKPLGNN QAQIVAHIKH QGDGNAHIVT
SNSATAVPQA NPQTSPVKQQ ALPPQSPQQV VVQQQQIHQQ SPTNFESGVT PITQQPVLTQ
AVQAPAQQQA LSVEESLLQN QPPGTVIKCV TAQVLQTEHG PRIVLQGLVG NDFTAQQLQL
VQTQVKQQLM KAQESNGKLG VLGPTKIYLA VQPENAVQSQ PPPLTPVHQS AAHQQTNNIE
IDADTLATTY EANSTIKDIA INNGDDQENS KCAETENSNI TTNESFAGTS SLLEGSEHDE
PTNLAGLDIS ETDLENKQNE SFVVTRGYIQ KSISNALKQG NLSPELEEKL VCMQKQQENA
NSTNEWETCS RGSVNEEALT PSRQTDDTEW KIRTSLRRPN AMTTSSQFNR ILKKNRSKND
EVAELGEQKQ SQLERHKELL KKNILRKRSL LERNLQSEIH EDVKTKVQRH VRPLSNASPD
EQSENERSGE PNLDFKRTEV QNPRHGAGRP KKLTRKKEKL YCICRTPYDD TKFYVGCDLC
SNWFHGDCVS ITEEASKKLS EFICIDCKRA RETQQLYCSC RQPYDESQFY ICCDKCQDWF
HGRCVGILQS EAEFIDEYVC PECQRKNDAN AANMKKLTSN DVEELKNLIK QMQLHKSAWP
FMEPVDPKEA PDYYKVIKEP MDLKRMEIKL ESNTYTKLSE FIGDMTKIFD NCRYYNPKES
SFYKCAEALE SYFVQKIKNF RENVFDQRT
