ID A0A3B4CVH4_PYGNA Unreviewed; 2564 AA.
AC A0A3B4CVH4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:0000256|HAMAP-Rule:MF_03071};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000015390.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000015390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017572566.1; XM_017717077.1.
DR STRING; 42514.ENSPNAP00000015390; -.
DR Ensembl; ENSPNAT00000023607.1; ENSPNAP00000015390.1; ENSPNAG00000003683.1.
DR GeneID; 108438943; -.
DR CTD; 57680; -.
DR GeneTree; ENSGT00940000153649; -.
DR OMA; CEWASME; -.
DR OrthoDB; 22878at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0071339; C:MLL1 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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: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; 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; 2.
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; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR PANTHER; PTHR46850:SF3; DNA HELICASE; 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 3: Inferred from homology;
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 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 727..794
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 809..875
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 908..1082
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1223..1374
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2067..2092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2200..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2463..2482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2526..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2130..2152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2200..2215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2325..2343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2564 AA; 285028 MW; DB070B3493E55761 CRC64;
MADPIMDLFD DTPLFNLDSL PDDAFTQGSS DPVEEALKLA LGQVDPPVDP APDTNVPILS
DPTPDPTPAP APAVPSVLVQ TQQPTQVSLT QAVSVASAPV SIQAVPQSSL PIASSSGAST
AVLLSSPLTV PVSGAQVTTQ QLQPQQLTAV TQQTAGQAAP KIVILKGPQG QAQVLQSVTG
NAGSPGKLTI ARVLTGTPLR PGMSIVSGGT VLNAAQPAQG QVKVGTGVQE LVQSPNGPVK
QVLMASLPHT QSQVQIPAQA RLTQTQVPQL QLQTQAQPAQ VQTQVHVQPQ TQAQAQVTPT
AGSTAAVRPQ GVTLSTVPQQ GEAKRITLVL QQPSQGGTAQ AGAVTLGTTQ ASGPGQQGQQ
PRLVLGSLPG KLVLQGGQLA ALTQARAGQT GAQPKVLTIQ LQVQQQPNQQ GAKFQLVSGT
PNASGSPQVV QISQGQGGQR VAVPLKLLLQ PQTSSASGAG GAVSVVKVIN TSAGSAASSG
TAAASTGIRV AKAQEPLRKV ETLCKQEKAN RIVAEAIARA KARGERNIPR VLNQDELPTG
QTSADLEGAA TPIGAKKKSG GGSKKKSPTS AVTGKAVASG EKKVKVKPAG SVVAGGAGGG
SSKSKSKAKP NTITLVGLKK RKRNASSDHS DGELSPPASP RTQEEDLSQM RRSNRQVKRK
KYTEDLDIKI TDDEDEPDED VDVTTPAVLP AGHSQSTGLE LQEQDADGLP VSSMQFFVEN
PSEEDAAIVD KILSMRLTKK ELCPGQYITV EEFFVKYKNY SYLHCEWASM EQLERDKRIH
QKLKRFKTKQ AQMRHIFHED EEPFNPDYVE VDRILDESIS VDKDNGEPVV YYLVKWCSLP
YEDATWELKE DVDEGKVEEF RKIQSRQPRL KRTPRPPAGS WKKLDQSREY RNGNTLREYQ
LEGVNWLLFN WYNRQNCILA DEMGLGKTIQ SIALLSEVFA VGVQGPFLII APLSTITNWE
REFSTWTEMN AIVYHGSLAS RQMIQQYEMY CKDDKGHLIP GAYKFDALIT TFEMVLSDCP
ELREIYWRCV IIDEAHRLKN RNCKLLDSLK MLNLEHKVLL TGTPLQNTVE ELFSLLHFLE
PAQFPSETEF LREFGDLKTE EQVQKLQAIL KPMMLRRLKE DVEKNLAPKQ ETIIEVELTD
VQKKYYRAIL ERNFSFLSLG ANSNSNVPNL LNTMMELRKC CNHPYLITGA EEKIVAELRE
RYDPMAPDFH LQALVRSAGK LVLLDKLLPR LKAGGHKVLI FSQMVRCLDI LEDYLIHKRY
LYERIDGRVR GNLRQAAIDR FSKSDSDRFV FLLCTRAGGL GINLTAADTC VIFDSDWNPQ
NDLQAQARCH RIGQSKAVKV YRLITRNSYE REMLDKASLK LGLDRAVLQS MSGSKESNVN
GIQQFSKKEI EDLLRKGAYA AIMDENDEGS RFCEEDIDQI LQRRATTITI ESEGKGSTFS
KASFVASENR TDIALDDPEF WQKWAKKADI DLDSINRKNT LVIDTPRVRK QTRQFSSLRG
EGGDISDLDS DEEYPPHNSR QARASRRSER QAGGGYGRTD CFRVEKHLLI YGWGRWRDIL
CHARCKRRLG EKDVETICRV ILVFCLLHYR GDENIKSFIW ELITPPENGQ EPNTLLNHSG
LSIPVPRGRK GKRVKAQSSF DIQKVEWIRK YNPDTLLLDD SYRKHLKHQC NKVLLRVRML
YYLKQEVIGD HADSVLRGAD SRDIDIWLPE MEQQDVPSAW WDAEADRCLL IGVFKHGYEM
YTTMRADPCL CFVERCGRPD DQDIKAEQHS ADPDLGDGAD YDKYSEDPEF KPVMRHSKDI
FGEADLRNAD EICVDDLTNP VPPEVQSSST TWPTSSSLTA RLRRLITAYQ RSYRREQLKI
EAAEKGDRRR RRCEQATKLK EIARQERQQR WTRREECDFY RVVSTFGVER IKTEGETQMG
DETKLDWTRF RTFARLDKKT DESLSRYFRC FVAMCRRVCH LRPARGEESQ DMSQSLAPIT
EERASRTLYR ISLLCRLRER ILPHPSLEER LQLAPSSSDL PTWWSIPQHD HELLLGASRH
GVSRTEQSIF SDPQFSFNQA RQDYLQNQQN RQEPAVQIQT HNQPPEKTSI KEERLEDEVR
LLGMESICQS DSLATPISFS DGKGRGQFAW GWKKSRERGS KGRERKEGDG AGGQPSDSDS
DSDSGSSTSS HCSASSDESG DSDAEREQAA LKMCDVDEEN STLSFTPSQD GAPPESLNDS
HRVDWPKDRV LINRIDNLCT LVLTGHWLSG RRYTSDPHLT LASDEHGLGD DLGYARVSRR
GNSALPGEAA DGQDTEFTVK LLKEEGLKLT FSKQALLPNG SAGEASGRRR RKDQELAESG
GVLHAPRKRD LPNWLKENPD YEVEGDMLEL LVNRTKRKRR KKKIEKEAAL TGNERIKVID
MRTGKKYGGI YGPALQDLKD YLEENPDHAV APEWADAVRN SGFLPESFFH RLLSLHASFP
KKSHHYLSTP STQPDPLLGG GEGETLVSDG AYMMDDEDLD AGDLTSSHHF LTPAYDVKME
AGSLDMDGGD GLSQGGYDSS DREAILDDVI MAPKNSDSSS SSED
//
