CHD8_DANRE
ID CHD8_DANRE Reviewed; 2511 AA.
AC B0R0I6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE Short=CHD-8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03071};
DE AltName: Full=ATP-dependent helicase CHD8 {ECO:0000255|HAMAP-Rule:MF_03071};
GN Name=chd8 {ECO:0000255|HAMAP-Rule:MF_03071};
GN ORFNames=si:ch211-10e2.6, wu:fi45h08;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., 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).
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:0000255|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:0000255|HAMAP-Rule:MF_03071};
CC -!- SUBUNIT: Component of some MLL1/MLL complex. {ECO:0000255|HAMAP-
CC Rule:MF_03071}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03071}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAQ13521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL928674; CAQ13521.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0R0I6; -.
DR SMR; B0R0I6; -.
DR STRING; 7955.ENSDARP00000122217; -.
DR PaxDb; B0R0I6; -.
DR PeptideAtlas; B0R0I6; -.
DR PRIDE; B0R0I6; -.
DR ZFIN; ZDB-GENE-030131-6320; chd8.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; B0R0I6; -.
DR PhylomeDB; B0R0I6; -.
DR Reactome; R-DRE-3769402; Deactivation of the beta-catenin transactivating complex.
DR PRO; PR:B0R0I6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0002039; F:p53 binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007420; P:brain development; IMP:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; IBA:GO_Central.
DR GO; GO:0048484; P:enteric nervous system development; IMP:GO_Central.
DR GO; GO:0030900; P:forebrain development; IMP:GO_Central.
DR GO; GO:0060322; P:head development; IMP:ZFIN.
DR GO; GO:0030901; P:midbrain development; IMP:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:UniProtKB-UniRule.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.40.5.120; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF160481; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..2511
FT /note="Chromodomain-helicase-DNA-binding protein 8"
FT /id="PRO_0000367312"
FT DOMAIN 680..745
FT /note="Chromo 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 760..826
FT /note="Chromo 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 859..1033
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 1174..1330
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT REGION 484..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2468..2511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 984..987
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT COMPBIAS 598..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2105..2123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2124..2142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 872..879
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
SQ SEQUENCE 2511 AA; 279712 MW; E81C33399E45322E 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 VPQQVRFVLG SLPGKLVLQG DQLAALAQAK AGQTGAQAKV LTIQLQVQQQ
PNQQGAKFQL VSGAANAGGS PQVVQISQGQ GGQRLAVPLK LLLQPQSNTV SSAGGAVSVV
KVINTSAAGS TSGTTTTAAS SGVRLAKIQE PVRRVETLCK QEKANRIVAE AIARAKARGE
RNIPRVLNQD ELPAGQTSAD LEGAGGATGA KKKGGGGVGG GGGGSKKKSP SAGGAKMVVG
GDKKSKAKTP VIPGGGSKSK SKTKLNTITL VGKKRKRNPS SDHSDVDLSP PVSPRTLEEE
MSQKRRSNRQ VKRKKYTEDL DIKITDDEDE LDADVDVTTT PMPAVGHVQP LGAELPPELD
GDGLPSMQFF VENPSEEDAA IVDKILSMRV TKKEARQYTN 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
SMSGNKESSI QQFSKKEIED LLRKGAYAAI MDENDEGSRF CEEDIDQILQ RRATTITIES
EGKGSTFSKA SFVASENRTD IALDDPEFWQ KWAKKADIDM DSLNRKNTLV IDTPRVRKQT
RQFSSLRGEG GDLSDLDSDD DYPPHNSRQS RASRRSDRHS GGGYGRTDCF RVEKHLLVYG
WGRWRDILSH ARCKRRLSER DVETICRVIL VFCLIHYRGD ENIKSFIWEL ITPPENGREP
QALLNHSGLS IPVPRGRKGK RVKAQSSFDV QKVEWIRKYN PDSLLLDDSY RKHLKHQCNK
VLLRVRMLYY LKQEVIGEHA DSVLSGADAR DIDIWLPEME QQDVPSGWWD AEADRCLLIG
VYKHGYEMYT TMRADPCLCF VERCGRPNEQ DINAEQQAAD PELGEGGDYD KYSEDPEFKP
ATRHAKEMYE EGDSVNADGE ICVEDRSAPM QVEGPSSGSS DLCYWPTSSS LTARLRRLIT
AYQRSYRREQ LKIEAAEKGD RRRRRCEQAT KLKEIARQER QQRWTRREEC DFYRVVSTFG
VERIKKETDA PEGDEHHMDW NRFRSFARLD KKTDESLTRY FKCFMSMCRK VCHIRPGRGD
ESQDMSQSLA PITEERASRT LYRVTLLCRL RERVLPHPSL EERLSLAPQT SDLPSWWSIP
KHDHELLLAA ARHGVSRTEL SIFSDPLYSF SQSRLDYLQN QQAQAAAQIH AFSQSQDPAG
IKEEGLEDES RLLGVEALCP SDSPAMLLSH SDSKVGIQAG WVWKKSKNNG PSERKLGGGG
GGASDSDSDS DSGSSSSSRH SGSSDDSGDS DVEREQAALK MCDGDEENSI LSLTPSQEGA
PPESLTDPLR VDWPKDRILI NRIENLCSLV ITGHWPSGRR YISDIQLNTV SDEHELGDDL
GYSRVARKIN STLSAEALEG QESEFTVKLL KEEGLKLTFS KQALMPNGEG SARKKRKDHE
LEDAEGVLHA PRRRDLPNWL KENPDYEVEG DMLELLVNRT KRKRRRKRVE KGAALTGSER
VKVIDIRTGK KFAGVFGPAL QDLREHLEEN PDHAVAPEWS ETVRHSGFLP EILFHRLLSP
HASIPKKSRH YLHTPSLQTD DPLLGGGEGE MLVSDGAYMM DDEDLEDGGH LTSSHHFLTP
AYDVKMEPSA LDMDGGDSLS QGGYDSSDRE AILDDVIMAP KHSDTSSSSE D
