CHD1_DROME
ID CHD1_DROME Reviewed; 1883 AA.
AC Q7KU24; Q24376; Q9VQJ9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1;
DE Short=CHD-1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase Chd1;
GN Name=Chd1; ORFNames=CG3733;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8692958; DOI=10.1073/pnas.93.14.7137;
RA Stokes D.G., Tartof K.D., Perry R.P.;
RT "CHD1 is concentrated in interbands and puffed regions of Drosophila
RT polytene chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7137-7142(1996).
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 SUBCELLULAR LOCATION, AND INTERACTION WITH SSRP1.
RX PubMed=10199952; DOI=10.1007/s004120050347;
RA Kelley D.E., Stokes D.G., Perry R.P.;
RT "CHD1 interacts with SSRP1 and depends on both its chromodomain and its
RT ATPase/helicase-like domain for proper association with chromatin.";
RL Chromosoma 108:10-25(1999).
RN [5]
RP FUNCTION.
RX PubMed=15643425; DOI=10.1038/nsmb884;
RA Lusser A., Urwin D.L., Kadonaga J.T.;
RT "Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly.";
RL Nat. Struct. Mol. Biol. 12:160-166(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17351630; DOI=10.1038/nsmb1217;
RA Eissenberg J.C., Lee M.G., Schneider J., Ilvarsonn A., Shiekhattar R.,
RA Shilatifard A.;
RT "The trithorax-group gene in Drosophila little imaginal discs encodes a
RT trimethylated histone H3 Lys4 demethylase.";
RL Nat. Struct. Mol. Biol. 14:344-346(2007).
RN [7]
RP FUNCTION.
RX PubMed=17717186; DOI=10.1126/science.1145339;
RA Konev A.Y., Tribus M., Park S.Y., Podhraski V., Lim C.Y., Emelyanov A.V.,
RA Vershilova E., Pirrotta V., Kadonaga J.T., Lusser A., Fyodorov D.V.;
RT "CHD1 motor protein is required for deposition of histone variant H3.3 into
RT chromatin in vivo.";
RL Science 317:1087-1090(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18202396; DOI=10.1534/genetics.107.079038;
RA McDaniel I.E., Lee J.M., Berger M.S., Hanagami C.K., Armstrong J.A.;
RT "Investigations of CHD1 function in transcription and development of
RT Drosophila melanogaster.";
RL Genetics 178:583-587(2008).
CC -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as
CC substrate recognition component of the transcription regulatory histone
CC acetylation (HAT) complex SAGA. Regulates polymerase II transcription.
CC Also required for efficient transcription by RNA polymerase I, and more
CC specifically the polymerase I transcription termination step. Regulates
CC negatively DNA replication. Not only involved in transcription-related
CC chromatin remodeling, but also required to maintain a specific
CC chromatin configuration across the genome (By similarity). Involved in
CC assembly of active chromatin. Required for maintaining open chromatin
CC and pluripotency in embryonic stem cells and is important for wing
CC development and fertility. Is essential for the incorporation of
CC histone H3.3 and assembly of paternal chromatin. Required for
CC replication-independent nucleosome assembly in the decondensing male
CC pronucleus. {ECO:0000250, ECO:0000269|PubMed:15643425,
CC ECO:0000269|PubMed:17717186, ECO:0000269|PubMed:18202396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the SAGA complex (By similarity). Interacts with
CC SSRP1. {ECO:0000250, ECO:0000269|PubMed:10199952}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8692958}. Chromosome
CC {ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:18202396,
CC ECO:0000269|PubMed:8692958}. Note=Colocalizes with elongating RNA
CC polymerase II (Pol II) on polytene chromosomes (PubMed:18202396).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; L77907; AAC37264.1; -; mRNA.
DR EMBL; AE014134; AAF51170.1; -; Genomic_DNA.
DR PIR; T13944; T13944.
DR RefSeq; NP_477197.1; NM_057849.5.
DR AlphaFoldDB; Q7KU24; -.
DR SMR; Q7KU24; -.
DR BioGRID; 59725; 8.
DR IntAct; Q7KU24; 5.
DR STRING; 7227.FBpp0297122; -.
DR PaxDb; Q7KU24; -.
DR PRIDE; Q7KU24; -.
DR EnsemblMetazoa; FBtr0077674; FBpp0077358; FBgn0250786.
DR GeneID; 33505; -.
DR KEGG; dme:Dmel_CG3733; -.
DR UCSC; CG3733-RA; d. melanogaster.
DR CTD; 1105; -.
DR FlyBase; FBgn0250786; Chd1.
DR VEuPathDB; VectorBase:FBgn0250786; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_8_1_1; -.
DR InParanoid; Q7KU24; -.
DR PhylomeDB; Q7KU24; -.
DR SignaLink; Q7KU24; -.
DR BioGRID-ORCS; 33505; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Chd1; fly.
DR GenomeRNAi; 33505; -.
DR PRO; PR:Q7KU24; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0250786; Expressed in egg cell and 26 other tissues.
DR ExpressionAtlas; Q7KU24; baseline and differential.
DR Genevisible; Q7KU24; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0035042; P:fertilization, exchange of chromosomal proteins; IMP:FlyBase.
DR GO; GO:0043486; P:histone exchange; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR025260; DUF4208.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF13907; DUF4208; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1883
FT /note="Chromodomain-helicase-DNA-binding protein 1"
FT /id="PRO_0000388773"
FT DOMAIN 318..414
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 439..501
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 540..710
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 840..991
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 661..664
FT /note="DEAH box"
FT COMPBIAS 27..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 730
FT /note="Y -> H (in Ref. 1; AAC37264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1448
FT /note="T -> N (in Ref. 1; AAC37264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1745
FT /note="R -> S (in Ref. 1; AAC37264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1804
FT /note="S -> I (in Ref. 1; AAC37264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1883 AA; 211828 MW; 226F2CA8996F6F17 CRC64;
MSQALNESAN SIGSDEQDDT REEANGTDHS GSGSGSGSSG SDSDSDSSSG NSSDGRSSPE
PEDKSLSVAG FPPTAAAAQA DSKTNGFTDD QEDSSSDGSS GSDSDSDAEG PSDQRNQSIN
NANTSSSLPK PEQNEEEDNE TEAGQQQPAS DASADESSDS SANVSPTSSS SSSEEEEEDY
RPKRTRQARK PPTAAEKSKK APAPKNKKKT WDSDESDESE DSDDEVSTAQ KRKPAATTSR
SKLAQQQQRR RVKPFSSEDS DDDDASKRCA TRRKGAAVSY KEASEDEATD SEDLLEFEYD
ESQAATTAAT AEEEEKCETI ERILAQRAGK RGCTGNQTTI YAIEENGFDP HAGFDEKQTP
DAETEAQFLI KWKGWSYIHN TWESEATLRD MKAKGMKKLD NFIKKEKEQA YWRRYAGPED
IDYFECQLEL QHELLKSYNN VDRIIAKGSK PDDGTEEYLC KWQSLPYAES TWEDAALVLR
KWQRCAEQFN DRESSKCTPS RHCRVIKYRP KFSRIKNQPE FLSSGLTLRD YQMDGLNWLL
HSWCKENSVI LADEMGLGKT IQTICFLYSL FKIHHLYGPF LCVVPLSTMT AWQREFDLWA
PDMNVVTYLG DIKSRELIQQ YEWQFESSKR LKFNCILTTY EIVLKDKQFL GTLQWAALLV
DEAHRLKNDD SLLYKSLKEF DTNHRLLITG TPLQNSLKEL WALLHFIMPD KFDTWENFEV
QHGNAEDKGY TRLHQQLEPY ILRRVKKDVE KSLPAKVEQI LRVEMTSLQK QYYKWILTKN
FDALRKGKRG STSTFLNIVI ELKKCCNHAA LIRPSEFELM GLQQDEALQT LLKGSGKLVL
LDKLLCRLKE TGHRVLIFSQ MVRMLDVLAD YLQKRHFPFQ RLDGSIKGEM RRQALDHFNA
EGSQDFCFLL STRAGGLGIN LATADTVIIF DSDWNPQNDL QAQARAHRIG QKNQVNIYRL
VTARSVEEQI VERAKQKMVL DHLVIQRMDT TGRTVLDKSG NGHSSNSNPF NKDDLSAILK
FGAEELFKDE QEHDDDLVCD IDEILRRAET RNEDPEMPAD DLLSAFKVAS IAAFEEEPSD
SVSKQDQNAA GEEDDSKDWD DIIPEGFRKA IDDQERAKEM EDLYLPPRRK TAANQNEGKR
GAGKGGKGKQ QADDSGGDSD YELGSDGSGD DGRPRKRGRP TMKEKITGFT DAELRRFIRS
YKKFPAPLHR MEAIACDAEL QEKPLAELKR LGEMLHDRCV QFLHEHKEEE SKTAATDETP
GAKQRRARAT FSVKLGGVSF NAKKLLACEQ ELQPLNEIMP SMPEERQQWS FNIKTRAPVF
DVDWGIEEDT KLLCGIYQYG IGSWEQMKLD PTLKLTDKIL LNDTRKPQAK QLQTRAEYLL
KIIKKNVELT KGGQRRQRRP RASRANDAKA ASQSASSTID AKPHDGEDAA GDARTVAESS
NSQVDPSTAS PHNAPATEQH GDPAKKAKKS KARSKKTSAS DNNGNKPMHF TANNEPRALE
VLGDLDPSIF NECKEKMRPV KKALKALDQP DVSLSDQDQL QHTRDCLLQI GKQIDVCLNP
YAETEKKEWR SNLWYFVSKF TELDAKRLFK IYKHALKQKA GGDGEAKGKD KGSSGSPAKS
KPNGVTTEEK EKERDRSGGK KKKKDKDKER SGQARYPETG IPTSGRYADP PLKRKRDEND
ADASSGLAGA PGGGIGDNLK SMSFKRLNMD RHEDRKKHHR GPDYYGGSGP PMGSGSYEGG
SNSRRQGPTS PSTPRTGRGG YDPPPAPSGY TPEMERWQSR DRYSQDYKRD RYDGYGRSGG
GQGSYHRERD RRPEKRRYPS GLPPHPYSSH YLPPNYYGLP NGAVPGLPPP SSVYRSDPRG
YPVMPRDYPA DYRRSDYERR TQT
