CTCF_CHICK
ID CTCF_CHICK Reviewed; 728 AA.
AC Q08705;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcriptional repressor CTCF;
DE AltName: Full=11-zinc finger protein;
DE AltName: Full=CCCTC-binding factor;
DE AltName: Full=CTCFL paralog;
GN Name=CTCF;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8246978; DOI=10.1128/mcb.13.12.7612-7624.1993;
RA Klenova E.M., Nicolas R.H., Paterson H.F., Carne A.F., Heath C.M.,
RA Goodwin G.H., Neiman P.E., Lobanenkov V.V.;
RT "CTCF, a conserved nuclear factor required for optimal transcriptional
RT activity of the chicken c-myc gene, is an 11-Zn-finger protein
RT differentially expressed in multiple forms.";
RL Mol. Cell. Biol. 13:7612-7624(1993).
CC -!- FUNCTION: Acts as both a transcriptional activator and repressor of the
CC MYC gene. {ECO:0000269|PubMed:8246978}.
CC -!- INTERACTION:
CC Q08705; P67809: YBX1; Xeno; NbExp=2; IntAct=EBI-932806, EBI-354065;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8246978}.
CC -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; Z22605; CAA80319.1; -; mRNA.
DR PIR; A54603; A54603.
DR RefSeq; NP_990663.2; NM_205332.5.
DR AlphaFoldDB; Q08705; -.
DR SMR; Q08705; -.
DR IntAct; Q08705; 3.
DR STRING; 9031.ENSGALP00000002808; -.
DR iPTMnet; Q08705; -.
DR PaxDb; Q08705; -.
DR GeneID; 396274; -.
DR KEGG; gga:396274; -.
DR CTD; 10664; -.
DR VEuPathDB; HostDB:geneid_396274; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q08705; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q08705; -.
DR PRO; PR:Q08705; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="Transcriptional repressor CTCF"
FT /id="PRO_0000047227"
FT ZN_FING 266..288
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..345
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..430
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..460
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..546
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 555..577
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 180..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 82828 MW; 6F58E25CFDAE17C8 CRC64;
MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEDEACHI APNQADGGEV VQDVNSGVQM
VMMEHLDPTL LQMKTEVMEG AVPQETEATV DDTQIITLQV VNMEEQPINL GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKGGLQEG EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELQPQEDPN WQKDPDYQPP AKKTKKNKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
ALIQHQKSHK NEKRFKCDQC DYACRQERHM VMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCSGL DGGEGENGGE TKKGKRGRKR
KMRSKKEDSS DSEENAEPDL DDNEDEEETA VEIEAEPEVS AEAPAPPPSK KRRGRPPGKA
ATQTKQSQPA AIIQVEDQNT GEIENIIVEV KKEPDAETVE EEEEAQPAVV EAPNGDLTPE
MILSMMDR
