ID E7FH24_DANRE Unreviewed; 2555 AA.
AC E7FH24; A0A8M1PAN7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 8 {ECO:0000256|HAMAP-Rule:MF_03071};
DE Short=CHD-8 {ECO:0000256|HAMAP-Rule:MF_03071};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03071};
DE AltName: Full=ATP-dependent helicase CHD8 {ECO:0000256|HAMAP-Rule:MF_03071};
GN Name=chd8 {ECO:0000313|Ensembl:ENSDARP00000011455,
GN ECO:0000313|RefSeq:NP_001334600.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-6320};
GN Synonyms=CHD-8 {ECO:0000313|RefSeq:NP_001334600.1}, CHD8
GN {ECO:0000256|HAMAP-Rule:MF_03071}, si:ch211-10e2.6
GN {ECO:0000313|RefSeq:NP_001334600.1}, wu:fi45h08
GN {ECO:0000313|RefSeq:NP_001334600.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000011455};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000011455}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000011455};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=24240475;
RA Huang H.T., Kathrein K.L., Barton A., Gitlin Z., Huang Y.H., Ward T.P.,
RA Hofmann O., Dibiase A., Song A., Tyekucheva S., Hide W., Zhou Y., Zon L.I.;
RT "A network of epigenetic regulators guides developmental haematopoiesis in
RT vivo.";
RL Nat. Cell Biol. 15:1516-1525(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000011455, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000011455};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=24998929;
RA Bernier R., Golzio C., Xiong B., Stessman H.A., Coe B.P., Penn O.,
RA Witherspoon K., Gerdts J., Baker C., Vulto-van Silfhout A.T.,
RA Schuurs-Hoeijmakers J.H., Fichera M., Bosco P., Buono S., Alberti A.,
RA Failla P., Peeters H., Steyaert J., Vissers L.E.L.M., Francescatto L.,
RA Mefford H.C., Rosenfeld J.A., Bakken T., O'Roak B.J., Pawlus M., Moon R.,
RA Shendure J., Amaral D.G., Lein E., Rankin J., Romano C., de Vries B.B.A.,
RA Katsanis N., Eichler E.E.;
RT "Disruptive CHD8 mutations define a subtype of autism early in
RT development.";
RL Cell 158:263-276(2014).
RN [5] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=25294932;
RA Sugathan A., Biagioli M., Golzio C., Erdin S., Blumenthal I., Manavalan P.,
RA Ragavendran A., Brand H., Lucente D., Miles J., Sheridan S.D.,
RA Stortchevoi A., Kellis M., Haggarty S.J., Katsanis N., Gusella J.F.,
RA Talkowski M.E.;
RT "CHD8 regulates neurodevelopmental pathways associated with autism spectrum
RT disorder in neural progenitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4468-E4477(2014).
RN [6] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [7] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=27418670;
RA Asad Z., Pandey A., Babu A., Sun Y., Shevade K., Kapoor S., Ullah I.,
RA Ranjan S., Scaria V., Bajpai R., Sachidanandan C.;
RT "Rescue of neural crest-derived phenotypes in a zebrafish CHARGE model by
RT Sox10 downregulation.";
RL Hum. Mol. Genet. 25:3539-3554(2016).
RN [8] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=28119690;
RA Wan F., Hu C.B., Ma J.X., Gao K., Xiang L.X., Shao J.Z.;
RT "Characterization of gammadelta T Cells from Zebrafish Provides Insights
RT into Their Important Role in Adaptive Humoral Immunity.";
RL Front. Immunol. 7:675-675(2017).
RN [9] {ECO:0000313|RefSeq:NP_001334600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RX PubMed=29079199;
RA Kunkel G.R., Tracy J.A., Jalufka F.L., Lekven A.C.;
RT "CHD8short, a naturally-occurring truncated form of a chromatin remodeler
RT lacking the helicase domain, is a potent transcriptional coregulator.";
RL Gene 641:303-309(2018).
RN [10] {ECO:0000313|RefSeq:NP_001334600.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001334600.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: DNA helicase that acts as a chromatin remodeling factor and
CC regulates transcription. Acts as a transcription repressor by
CC remodeling chromatin structure and recruiting histone H1 to target
CC genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1
CC and preventing p53/TP53 transactivation activity. Acts as a negative
CC regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1)
CC activity. Negatively regulates CTNNB1-targeted gene expression by being
CC recruited specifically to the promoter regions of several CTNNB1
CC responsive genes. May also act as a transcription activator by
CC participating in efficient U6 RNA polymerase III transcription.
CC {ECO:0000256|HAMAP-Rule:MF_03071}.
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 Evidence={ECO:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP-
CC Rule:MF_03071};
CC -!- SUBUNIT: Component of some MLL1/MLL complex. {ECO:0000256|HAMAP-
CC Rule:MF_03071}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03071}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03071}.
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DR EMBL; AL928674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001334600.1; NM_001347671.1.
DR PeptideAtlas; E7FH24; -.
DR Ensembl; ENSDART00000013676; ENSDARP00000011455; ENSDARG00000075543.
DR Ensembl; ENSDART00000013676.9; ENSDARP00000011455.9; ENSDARG00000075543.5.
DR GeneID; 568214; -.
DR KEGG; dre:568214; -.
DR AGR; ZFIN:ZDB-GENE-030131-6320; -.
DR CTD; 57680; -.
DR ZFIN; ZDB-GENE-030131-6320; chd8.
DR OMA; CEWASME; -.
DR OrthoDB; 22878at2759; -.
DR Proteomes; UP000000437; Alternate scaffold 2.
DR Proteomes; UP000000437; Chromosome 2.
DR Bgee; ENSDARG00000075543; Expressed in blastula and 22 other cell types or tissues.
DR GO; GO:0071339; C:MLL1 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR CDD; cd18060; DEXHc_CHD8; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 3.40.5.120; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR HAMAP; MF_03071; CHD8; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR034724; CHD8.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR46850:SF2; -; 1.
DR PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 2.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; BRK domain-like; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03071};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03071};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Helicase {ECO:0000256|HAMAP-Rule:MF_03071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03071};
KW Proteomics identification {ECO:0007829|PeptideAtlas:E7FH24};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_03071};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_03071};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_03071};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_03071};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|HAMAP-
KW Rule:MF_03071}.
FT DOMAIN 718..785
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 800..866
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 899..1073
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1214..1365
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 333..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2129..2213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2512..2555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2167..2185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2555 AA; 283766 MW; 6CB34D927B587581 CRC64;
MADPIMDLFD DTPLFNLDSL PEDAFSQGSS DPVEEALKLA LGQVDPPTDP IPDPGVPILS
DVVTDPALIP TPVSVPLQNL QTQQLSQIPH EVSVASAPIS IQPSLSVASN SSGAATVLLS
SSLGVPVSGA QVTPQQQTQQ ITAVTQQAAG QHAPKIVILK GPQGQTQVLQ GVTGATGSPG
KVTLARVLTG TPLRPGMAVV SGGTVLNATS PAQGQVKVGT GVQRLVQTAN GPMKQVLLTS
VPQTQSQVQT QPVQVQIPVQ TQLQSPSQPQ QLQAQIQAQT QVALQTQAQT QTPTSPAAAG
IRPQSVTLSA VPQQGEAKRI TLVLQQPSQG GAAQAGTVTV GGTAGSGQQG QQPRLVLGSL
PGKLVLQGDQ LAALAQAKAG QTGAQAKVLT IQLQVQQQPN QQGAKFQLVS GAANAGGSPQ
VVQISQGQGG QRLAVPLKLL LQPQSNTVSS AGGAVSVVKV INTSAAGSTS GTTTTAASSG
VRLAKIQEPV RRVETLCKQE KANRIVAEAI ARAKARGERN IPRVLNQDEL PAGQTSADLE
GAGGATGAKK KGGGGVGGGG GGSKKKSPSA GGAKMVVGGD KKSKAKTPVI PGGGSKSKSK
TKLNTITLVG KKRKRNPSSD HSDVDLSPPV SPRTLEEEMS QKRRSNRQVK RKKYTEDLDI
KITDDEDELD ADVDVTTTPM PAVGHVQPLG AELPPELDGD GLPSMQFFVE NPSEEDAAIV
DKILSMRVTK KEVCPGQYTN VEEFFVKYKN YSYMHCEWAS LEQLERDKRI HQKLKRFKTK
QAQMRNLFQE DEEPFNPDYV EVDRILDESH SVDKDNGEPV VYYLVKWCSL PYEDATWELK
EDVDEGKVEE FRKIESRQPR LKRTPRPAAS AWKKLDESTE YKNGNQLREY QLEGVNWLLF
NWYNRQNCIL ADEMGLGKTI QSIALLSEMF SAGVQSPFMI IAPLSTITNW EREFSNWTDM
NAIVYHGSLA SRQMIQQYEM YCKDDKGHLI PGAYKFDALI TTFEMILSDC PELREISWRC
VVIDEAHRLK NRNCKLLDSL KMLEIEHKVL LTGTPLQNTV EELFSLLHFL EPAQFPSEIE
FLREFGDLKT EEQVQKLQSI LKPMMLRRLK EDVEKNLAPK QETIIEVELT DVQKKYYRAI
LERNFSFLSM GATQNSNVPN LLNTMMELRK CCNHPYLITG AEEKIVSELR EVYDPLAPDF
HLQALVRSAG KLVLLDKLLP RLKAGGHKVL IFSQMVRCLD ILEDYLIHKR YLYERIDGRV
RGNLRQAAID RFSKPDSDRF VFLLCTRAGG LGINLTAADT CVIFDSDWNP QNDLQAQARC
HRIGQSKAVK VYRLITRNSY EREMLDKASL KLGLDRAVLQ SMSGNKESSV NGIQQFSKKE
IEDLLRKGAY AAIMDENDEG SRFCEEDIDQ ILQRRATTIT IESEGKGSTF SKASFVASEN
RTDIALDDPE FWQKWAKKAD IDMDSLNRKN TLVIDTPRVR KQTRQFSSLR GEGGDLSDLD
SDDDYPPHNS RQSRASRRSD RHSGGGYGRT DCFRVEKHLL VYGWGRWRDI LSHARCKRRL
SERDVETICR VILVFCLIHY RGDENIKSFI WELITPPENG REPQALLNHS GLSIPVPRGR
KGKRVKAQSS FDVQKVEWIR KYNPDSLLLD DSYRKHLKHQ CNKVLLRVRM LYYLKQEVIG
EHADSVLSGA DARDIDIWLP EMEQQDVPSG WWDAEADRCL LIGVYKHGYE MYTTMRADPC
LCFVERCGRP NEQDINAEQQ AADPELGEGG DYDKYSEDPE FKPATRHAKE MYEEGDSVNA
DGEICVEDRS APMQVEGPSS GSSDLCYWPT SSSLTARLRR LITAYQRSYR REQLKIEAAE
KGDRRRRRCE QATKLKEIAR QERQQRWTRR EECDFYRVVS TFGVERIKKE TDAPEGDEHH
MDWNRFRSFA RLDKKTDESL TRYFKCFMSM CRKVCHIRPG RGDESQDMSQ SLAPITEERA
SRTLYRVTLL CRLRERVLPH PSLEERLSLA PQTSDLPSWW SIPKHDHELL LAAARHGVSR
TELSIFSDPL YSFSQSRLDY LQNQQAQAAA QIHAFSQSQD PAGIKEEGLE DESRLLGVEA
LCPSDSPAML LSHSDSKVGI QAGWVWKKSK NNGPSERKLG GGGGGASDSD SDSDSGSSSS
SRHSGSSDDS GDSDVEREQA AALKMCDGDE ENSILSLTPS QEGAPPESLT DPLRVDWPKD
RILINRIENL CSLVITGHWP SGRRYISDIQ LNTVSDEHEL GDDLGYSRVA RKINSTLSAE
ALEGQESEFT VKLLKEEGLK LTFSKQALMP NGEGSARKKR KDHELEDAEG VLHAPRRRDL
PNWLKENPDY EVEGDMLELL VNRTKRKRRR KRVEKGAALT GSERVKVIDI RTGKKFAGVF
GPALQDLREH LEENPDHAVA PEWSETVRHS GFLPEILFHR LLSPHASIPK KSRHYLHTPS
LQTDDPLLGG GEGEMLVSDG AYMMDDEDLE DGGHLTSSHH FLTPAYDVKM EPSALDMDGG
DSLSQGGYDS SDREAILDDV IMAPKHSDTS SSSED
//
