CHD8_XENTR
ID CHD8_XENTR Reviewed; 2184 AA.
AC B5DE69;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
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};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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=AAI68549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC168549; AAI68549.1; ALT_INIT; mRNA.
DR RefSeq; NP_001131089.2; NM_001137617.2.
DR AlphaFoldDB; B5DE69; -.
DR SMR; B5DE69; -.
DR STRING; 8364.ENSXETP00000031524; -.
DR PRIDE; B5DE69; -.
DR Ensembl; ENSXETT00000089319; ENSXETP00000072752; ENSXETG00000017194.
DR GeneID; 100192376; -.
DR KEGG; xtr:100192376; -.
DR CTD; 57680; -.
DR Xenbase; XB-GENE-966847; chd8.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; B5DE69; -.
DR OrthoDB; 7181at2759; -.
DR Reactome; R-XTR-3769402; Deactivation of the beta-catenin transactivating complex.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017194; Expressed in blastula and 12 other tissues.
DR ExpressionAtlas; B5DE69; differential.
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; IBA: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: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: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; -; 1.
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; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
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 2: Evidence at transcript level;
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..2184
FT /note="Chromodomain-helicase-DNA-binding protein 8"
FT /id="PRO_0000367313"
FT DOMAIN 586..653
FT /note="Chromo 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 668..734
FT /note="Chromo 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 767..941
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 1081..1252
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT REGION 379..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 892..895
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT COMPBIAS 433..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 780..787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
SQ SEQUENCE 2184 AA; 246687 MW; 08867A829AD6919D CRC64;
MADPIMDLFD DPNLFGLDSL TGDSFGRDGP DTIDDALGLG NVLGPLEPIT DRVGLPGADV
GNNEVKQQTE SQVLPDNPAL MSATEIMQPI QLPTNQETLN QGNPFMGASN AGAPKIMILK
APAGMTVGAC PVTQIQTLTP HQAANGGKVA FAKVLTGTPL RPGVSIVSGN TVLAKMPSTG
VAGQVGAVRP VRQLLLQPVR ASAAPGSSES NTGIKPAITL TSAPQQGDPK RITLVLQQPS
QVGATAQQGQ RHVVLGGLPG KIVLQGNQLA ALTQAKTPQG QPAKVVTIQL QVQQQPGAAG
QTPQKFQIVQ QAPGGVAIAP SGQHTHMLNQ QGVQRLSVPL KVVLQPQAGS SQGTAQGLSV
VKVLNASEVA NLTASQTVVK TSTGGGESRK LDSQKKQEKA NRIVAEAIAR ARARGEQNIP
RVLNEDELPS VNPEDDDGSR RKRKKKKGET SDRSKDEKPK KVKGSGSLRS RSKGKPSTIT
PIVGKKRKRN PSSDNSDAEI MASQASPAED EDSVQKRRSN RQVKRKKYTE DLDIKITDDE
DDEEVDVTGP VKTEPVLLPE PMPLPDSEAV PSMQFFVENP SEEDAAIVDK ILSMRLAKKE
LPTGEYVEVE EYFVKYKNYS YLHCEWATIE QLERDKRIHQ KLKRFKTKMT QMQHFLQEDE
ESFNPDYVEV DRILDESHST DKDNGEPVVY YLVKWCSLPY EDSTWELKED VDDGKIEEFK
RIEARQPNLK RVARPAATSW KKLELSREYQ NGNQLREYQL EGVNWLLFNW YNRQNCILAD
EMGLGKTIQS ITFLQEVYNV GIRGPFLVIA PLSTITNWER EFGSWTQMNT IVYHGSLASR
QMIQQYEMYC KDSKGRLIPG AYKFDALITT FEMVLSDCPE LREIEWRCVI IDEAHRLKNR
NCKLLDSLKH MDLEHKVLLT GTPLQNTVEE LFSLLHFLEP TQFSSEAEFL KDFGDLKTEE
QVQKLQAILK PMMLRRLKED VEKNLAPKQE TIIEVELTNI QKKYYRAILE KNFSFLTKGA
SQSNTPNLLN TMMELRKCCN HPYLITGAEE KIISEFREAT PVVPPDFHVQ AMVRSSGKLV
LIDKLLPKLR AGGHKVLIFS QMVRCLDILE DYLIQRRYLY ERIDGRVRGN MRQAAIDRFS
RPDSDRFVFL LCTRAGGLGI NLTAADTCII FDSDWNPQND LQAQARCHRI GQSKAVKIYR
LITRNSYERE MFDKASLKLG LDKAVLQSMS GRDNHLSGPI QQFTKKEIED LLRKGAYAAI
MDEDDEGSKF CEEDIDQILL RRTTTITIES EGKGSTFSKA SFVASENRTD ISLDDPNFWQ
KWAKKADLDL DLLSSKNTLV IDTPRIRKQT RHFTNKDDDM VEFSDLESDD DDRPKARRQD
RKHGYGRTDC FRVEKHLLVY GWGRWRDILT HGRFKRGMNE RDVEKICRAI LVYCLLHYRG
DENIKSFIWD LITPAENGKT KQLQNHSGLS IPVPRGRKGK KVKSQSSFDI HKADWIHKYN
PDTLFQDEGY KKHLKHQCNK VLLRVRMLYF LRQEVIGNQA MKVLSGVEAR QIDIWFPQVD
QVEVPSRWWD READKSLLIG VFKHGYEKYN TMRADPALCF LEKVGGPDEQ AIAAEHHAQD
FSELPDGGDF DRDIEDPEYK PLHAQKDPED EIDSLMMDEE ISVVDGEEAT AMPSGMLWPP
GSALTARLRR LITAYQRSYK REQLKLEAEE RGDKRRKRCE AAFKLKEIAR REKQQRWTRR
EACDFFRVLS SFGVEYDPDT QLYDWQRFRG LARLDKKTDE SLLKYFHGFV AMCRQVCRLP
PAAGDEPPDP SLFIEPISEE RASRALFRLD LLRRVREQVL CHPLLIPRLS LCRPDPELPE
WWESGRHDNE LLQGAARYGL SRTDLTILQD HAFSFLRCQI SYFQSRGISG HSRPSTPTTA
PSVPTERQPS HLASLSSSVS CSPAPRRSSS CSSSSHSSNS EDSSDESNGV KVKPNAGLSH
ARLYDEESRL SLTASPADLT TEDSIQTALE TPHSTDWPKD RVLICRIEQV CSAVLTGKWS
SPRRLSDPPS DSPDSLPPTP EQQSPAHFTQ IRPAPDPKEF TIQIKSEEGL KIKFQKHKFM
GNGALDSAPH TQKKKSKKKM DLDMDTRIPV VNQKDGTLLL GEEAPLRCQL PEWLHRNPDF
MVDPRFIAVS GYWIPYINRG KHFL
