ID H2M9G6_ORYLA Unreviewed; 2553 AA.
AC H2M9G6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
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:ENSORLP00000015149.2};
GN Synonyms=CHD8 {ECO:0000256|HAMAP-Rule:MF_03071};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000015149.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000015149.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015149.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000015149.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015149.2};
RG Ensembl;
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 STRING; 8090.ENSORLP00000015149; -.
DR Ensembl; ENSORLT00000015150.2; ENSORLP00000015149.2; ENSORLG00000012103.2.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000153649; -.
DR HOGENOM; CLU_000315_5_2_1; -.
DR InParanoid; H2M9G6; -.
DR TreeFam; TF313572; -.
DR Proteomes; UP000001038; Chromosome 17.
DR Bgee; ENSORLG00000012103; Expressed in blastula and 14 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 DNA-templated transcription; IBA:GO_Central.
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; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000001038};
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 721..788
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 803..869
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 902..1076
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1217..1368
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2062..2082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2120..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2300..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2449..2478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2502..2532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2153..2168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2450..2466
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2553 AA; 284913 MW; 3C75FB3227795ED0 CRC64;
MADPIMDLLE DTPLFNLDGL PDDTFSQGSS DPVEEALKLA LGQVDPPMDA EPTPDLAVTS
SLGVPVAASA FLDPASVQVS AQPVPVAQTV SVAAVPTMTP ATVDAVPQVQ AQAPMPITSN
SSRPSSGTVL LGSPLTVSSP SATSATTQQL TQIAHQLTPQ QLAAITQQGA GKIVILKGPQ
GQAQVLQTVS GTTAQTSGKV IRVLSGTPLK PGMSILQGGT ILNQASPGQA QVKQVQQTQG
QPVQVQIAAQ AQVAQGQTTV QVQPQVQAAQ IQVQPQSQAA QIQVQAQGQV QLQQPLQAQT
PGGEAKRITL VLQQPSQTMS ATPMGQQQVT QVQATAAGQQ QQQAPARLVL GQLPGGKLVL
QGSQLAALTQ ARAAGQAGGQ PKVLTLQLQV QQQPNQQGGV KYQLVSGAGN AGGPQVLQIS
QGQGGQRVAV PLKMLLQPQT SSASSAGGTV SVVKVINASS TATSSTTSTP SQAIRISKAP
GEPASVRRVE ILCKQEKANR IVAEAIARAK ARGEKNLPRV LNQDELPNTQ SSPEIGGTIT
VVSTKKKSSG GGSKKKSPLS GGPGFKTPAG GDKKGKVKMV GGTISIAGGA VLPGVGNKSK
SKAKTNTITL VGAKKRKRNA SSDHSDGELS PPSPVALDDD MIMKRRSNRV VKRKKYTEDL
DIKITDDEDE QEDVDVITTA AAVASISGGT VAQLKPEVEL DVDGQPSMQF FVENPSEEDA
AIVDKVLSMR ITKKEVVPGQ YTNAEEFFVK YKNYSYLHCE WATLEQLEKD KRIHQKIKRF
KAKHAQMRHF FQEDEEPFNP DYVEVDRILD VSHSVDKDNG EPVIYYLVKW CSLPYEDATW
ELKEDVDEGK VKEFSRIHNR QPCLKRTPRP PASSWKKLEE TREYKNGNIL REYQLEGVNW
LLFNWYNRQN CILADEMGLG KTIQSIALLS EVYTAGIQGP FLVIAPLSTI TNWEREFCTW
TQMNAIVYHG SLASRQMIQQ YEMYCKDDKG HLIPGAYKFD ALITTFEMVL SDCPELREIS
WRCVIIDEAH RLKNRNCKLL DSLKMLDLEH KVLLTGTPLQ NTVEELFSLL HFLEPAQFPS
EIEFLRDFGD LKTEEQVQKL QAILKPMMLR RLKEDVEKNL APKQETIIEV ELTDVQKKYY
RAILERNFSF LSLGANSNSN VPNLLNTMME LRKCCNHPYL INGAEEKIVA ELREVYDPLA
PDFHLQALIR SAGKLVLLDK LLPRLKAGGH KVLIFSQMVR CLDILEDYLI NKRYLYERID
GRVRGNLRQA AIDRFSKPDS DRFVFLLCTR AGGLGINLTA ADTCVIFDSD WNPQNDLQAQ
ARCHRIGQSK AVKVYRLITR NSYEREMLDK ASLKLGLDRA VLQSMSGNKE SNNNGQIQQF
SKKEIEDLLR KGAYAAIMDE NDEGSRFCEE DIDQILQRRA TTITIESEGK GSTFSKASFV
ASENRNDIAL DDPEFWQKWA KRADIDMDSI NQKNTLVIDT PRIRKQTRQY SSLRGEGGDL
SDLDSDEEYP PANSRHSRSS RRADRHSGGG YGRTDCFRVE KHLLVYGWGR WRDILLHARC
KRRLSERDVE TICRVILVFC LIHYRGDENI KSFIWELITP PENGREPQTL LNHSGLSIPV
PRGRKGKRVK AQSTFDIQKV EWIRKYNPDT LLLDDSYRKH LKHQCNKVLL RVRMLYYLKQ
EVIGEHAEAV LKGADIRDVD IWMPEMEQQE VPAAWWDSDA DRSLLAGVFK HGYEMYTTMR
ADPQLCFVER VGRPDDKAID AEQHTGDTEM GDEADFDKYS EDPEFKPASR HTKELFEEAD
SMNVEDEISV EDKIGPPVIE SAPSQSGACD WPSSSSLTAR LRRLITAYQR SYRQEQLKME
AEAKGDRRRR RCEQASKLKE IARQERQQRW TRREECDFYR VVSTFGVEKI KKEPGLPESS
DAEFDWTRFR TFARLDKKTD ESLSRYFRSF VAMCRRVCHL RPAHGEDQSQ PPQTVAPITE
ERASRTLYRI SLLRRLRERV LPHPCLEERL RLARPSSELP AWWKIPEHDH QLMFAASVHG
VSRTELSIFP DPQFTFSSAR EEFIQSQQAT PPPPPPPPPI MTLIQPRAEV DLSGLKEEGS
DHSAHLLGGE ACAELQTTPL SHHSGKVQGQ SWGFKRSRER GERRKGEGGS DSDSDSDSGS
SSSDRSGSSD DSAESEEEVE GGAMKVRDMD EENSLLSMTP SQDGLPPPDP IRVDWPKDRV
LINRLDNLCN LVLSGQWPSG RRYLPEAQLN LSSEVTGEEL AFSRMIRKPP CTPSVLGPDG
EDGEFTVKLL KEEGLKLTFS KQALMPNGSG GESSSRKKRK DQELSDMDGL HNSLERAPRR
RDPPTWLKEN PEYEVEGDML ELLVNKSKRK RRRRADKALT GTEKIKIINM MTGKKVGAAF
CPMLQELRVY LEENPDAAVS PEWSETVRKS GYLPESFFHR LLAEHSEIPK KSRRHHHHHH
HHHHHYHTPE PVSEDPNLDG VEEETLVSDG AYMMDEEDLE TSHNFLSGPD FDVKMEGGDS
LSQGDYDSSD QEALLEDVII AQKDSDSSSS SED
//
