CHD3_CAEEL
ID CHD3_CAEEL Reviewed; 1787 AA.
AC Q22516; Q18794;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 3 homolog;
DE Short=CHD-3;
DE EC=3.6.4.12;
GN Name=chd-3; ORFNames=T14G8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11076750; DOI=10.1242/dev.127.24.5277;
RA von Zelewsky T., Palladino F., Brunschwig K., Tobler H., Hajnal A.,
RA Mueller F.;
RT "The C. elegans Mi-2 chromatin-remodelling proteins function in vulval cell
RT fate determination.";
RL Development 127:5277-5284(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21060680; DOI=10.1371/journal.pone.0013681;
RA Passannante M., Marti C.O., Pfefferli C., Moroni P.S., Kaeser-Pebernard S.,
RA Puoti A., Hunziker P., Wicky C., Muller F.;
RT "Different Mi-2 complexes for various developmental functions in
RT Caenorhabditis elegans.";
RL PLoS ONE 5:E13681-E13695(2010).
CC -!- FUNCTION: Chromatin-remodeling protein that has a role in notch
CC signaling-dependent vulval cell fate determination. May also have a
CC role in pharyngeal precursor cell specification.
CC {ECO:0000269|PubMed:11076750, ECO:0000269|PubMed:21060680}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the head and vulva.
CC {ECO:0000269|PubMed:21060680}.
CC -!- DEVELOPMENTAL STAGE: Detected around the 20 cell stage after the onset
CC of zygotic transcription. Also expressed in adults.
CC {ECO:0000269|PubMed:21060680}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF308444; AAG29837.1; -; mRNA.
DR EMBL; Z67884; CAA91810.1; -; Genomic_DNA.
DR EMBL; Z67881; CAA91810.1; JOINED; Genomic_DNA.
DR PIR; T20160; T20160.
DR RefSeq; NP_510140.1; NM_077739.4.
DR AlphaFoldDB; Q22516; -.
DR SMR; Q22516; -.
DR BioGRID; 46325; 4.
DR STRING; 6239.T14G8.1; -.
DR iPTMnet; Q22516; -.
DR EPD; Q22516; -.
DR PaxDb; Q22516; -.
DR PeptideAtlas; Q22516; -.
DR PRIDE; Q22516; -.
DR EnsemblMetazoa; T14G8.1.1; T14G8.1.1; WBGene00000482.
DR GeneID; 181421; -.
DR KEGG; cel:CELE_T14G8.1; -.
DR UCSC; T14G8.1; c. elegans.
DR CTD; 181421; -.
DR WormBase; T14G8.1; CE03657; WBGene00000482; chd-3.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000169383; -.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; Q22516; -.
DR OMA; MEQPPEG; -.
DR OrthoDB; 54215at2759; -.
DR PhylomeDB; Q22516; -.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR PRO; PR:Q22516; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000482; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; ISS:WormBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromatin regulator; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..1787
FT /note="Chromodomain-helicase-DNA-binding protein 3 homolog"
FT /id="PRO_0000080234"
FT DOMAIN 373..476
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 501..583
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 628..812
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 944..1107
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 265..312
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 328..375
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1754..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 763..766
FT /note="DEAH box"
FT COMPBIAS 9..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 641..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1787 AA; 205255 MW; 1EFCE1FFECE59740 CRC64;
MSDDQHESID GDETMEEDSM LAEGHEDGEE DVGEDEEEVE TEESQGVPTT SEKKKPPPKK
KKGGKKSSKK KNNCDYPDPY KSTSAEISAA IGLTDVDVDY EQEEFQSITN LKNFSSLVKP
YILKVNPGTN VTKMYPLFQV KYKEFQDHMT AHGKSIQKQQ RAKFVPVPVP VTPQEKIIPQ
KTRSSARRKR RDGSDGEGGG HDSDQEFEAL IKQHEKQQDE AEKGKEEARI NRAAAKVDKR
KAALESARAS KRARKEQGVV EENHQENCEV CNQDGELMLC DTCTRAYHVA CIDENMEQPP
EGDWSCPHCE EHGPDVLIVE EEPAKANMDY CRICKETSNI LLCDTCPSSY HAYCIDPPLT
EIPEGEWSCP RCIIPEPAQR IEKILSWRWK EISYPEPLEC KEGEEASKDD VFLKPPRKME
PRREREFFVK WKYLAYWQCE WLSETLMDVY FTALVRMYWR KVDSENPPIF EESTLSRHHS
DHDPYKLRER FYQYGVKPEW MQIHRIINHL SYAKSQQDYL VKWKELSYEH ATWERDDTDI
ANYEDAIIKY WHHRERMLND EVPRNVQKMI AKQREAKGLG PKEDEVTSRR KKREKIDILK
KYEVQPDFIS ETGGNLHPYQ LEGINWLRHC WSNGTDAILA DEMGLGKTVQ SLTFLYTLMK
EGHTKGPFLI AAPLSTIINW EREAELWCPD FYVVTYVGDR ESRMVIREHE FSFVDGAVRG
GPKVSKIKTL ENLKFHVLLT SYECINMDKA ILSSIDWAAL VVDEAHRLKN NQSTFFKNLR
EYNIQYRVLL TGTPLQNNLE ELFHLLNFLA PDRFNQLESF TAEFSEISKE DQIEKLHNLL
GPHMLRRLKA DVLTGMPSKQ ELIVRVELSA MQKKYYKNIL TRNFDALNVK NGGTQMSLIN
IIMELKKCCN HPYLFMKACL EAPKLKNGMY EGSALIKNAG KFVLLQKMLR KLKDGGHRVL
IFSQMTMMLD ILEDFCDVEG YKYERIDGSI TGQQRQDAID RYNAPGAKQF VFLLSTRAGG
LGINLATADT VIIYDSDWNP HNDIQAFSRA HRLGQKHKVM IYRFVTKGSV EERITSVAKK
KMLLTHLVVR AGLGAKDGKS MSKTELDDVL RWGTEELFKE EEAPVEGADG EGTSSKKPNE
QEIVWDDAAV DFLLDRNKEE EGQDGEKKEH WTNEYLSSFK VATYNTKEAD DADDDEDETE
VIKEGTEEQD PNYWEKLLKH HYEQDQETEL QKLGKGKRVR RQVNYASENM GQDWSAQNNQ
QQEEDDGSEY GSDNGELLQT DEDYEERRRR REERSEKLPP LLAKVNGQIE VLGFNPRQRK
AFYNAVMRWG MPPQDLTQSS WQVRDLRNKS EKVFKAYSSL FMRHLCEPVV DNSDSFMDGV
PREGLNRQAV LSRIGLMSIL RKKVQEFEKF NGEWSMPETR EKMLATAAQA SVSNLPGMIK
IKEEPIDIDE TPMDVDQSNI TKTEELASEV KVEEEPKAPR LPYKFNICDG GYTELHSLWI
NEEKVARNGK EYEIWHRRHD FWLLAAVAVY GYGRYQINFQ DIMNDPKFSI VNEPFKQTGA
DPATNFADVK NKFLARRFKL LEQSLVIEEQ LRRAAHINKQ QSPDQVGQLA QHFSELEHTA
DAHVNIARES NNGNRNANAI LHKCLAQLDD LLSDLKTDVA RLPATISQVR PVTERLQMSE
RQILSRLVVA KDPDAAPSKP ALPPSGPFIT PLFNQNFTTI QPKFPSLFDC NLSPDDEPID
IEGSISAAVA EASRASSIAA TKDEPMDTSD KDIPSTSAAA GSSYPRY
