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   27-MAR-2024, entry version 133.
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: Chromatin binding factor that binds to DNA sequence specific
CC       sites and regulates the 3D structure of chromatin (By similarity).
CC       Binds together strands of DNA, thus forming chromatin loops, and
CC       anchors DNA to cellular structures, such as the nuclear lamina (By
CC       similarity). 3Defines the boundaries between active and heterochromatic
CC       DNA via binding to chromatin insulators, thereby preventing interaction
CC       between promoter and nearby enhancers and silencers (By similarity).
CC       Plays a critical role in the epigenetic regulation (By similarity).
CC       Acts both as atranscriptional activator and a repressor of the MYC gene
CC       (PubMed:8246978). {ECO:0000250|UniProtKB:P49711,
CC       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.ENSGALP00000058125; -.
DR   iPTMnet; Q08705; -.
DR   PaxDb; 9031-ENSGALP00000002808; -.
DR   GeneID; 396274; -.
DR   KEGG; gga:396274; -.
DR   CTD; 10664; -.
DR   VEuPathDB; HostDB:geneid_396274; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q08705; -.
DR   PhylomeDB; Q08705; -.
DR   PRO; PR:Q08705; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23235:SF120; KRUEPPEL-LIKE FACTOR 15; 1.
DR   PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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
//