CTCF_RAT
ID CTCF_RAT Reviewed; 737 AA.
AC Q9R1D1;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=COP;
RA Jing L., Mikheev A.M., Lobanenkov V., Zarbl H.;
RT "Sequencing of rat CTCF (11-Zinc fingers protein) cDNA.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chromatin binding factor that binds to DNA sequence specific
CC sites. Involved in transcriptional regulation by binding to chromatin
CC insulators and preventing interaction between promoter and nearby
CC enhancers and silencers. Acts as transcriptional repressor binding to
CC promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK
CC and PIM1 promoters. Acts as a transcriptional activator of APP.
CC Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene
CC expression. Plays an essential role in oocyte and preimplantation
CC embryo development by activating or repressing transcription. Seems to
CC act as tumor suppressor. Plays a critical role in the epigenetic
CC regulation. Participates in the allele-specific gene expression at the
CC imprinted IGF2/H19 gene locus. On the maternal allele, binding within
CC the H19 imprinting control region (ICR) mediates maternally inherited
CC higher-order chromatin conformation to restrict enhancer access to
CC IGF2. Plays a critical role in gene silencing over considerable
CC distances in the genome. Preferentially interacts with unmethylated
CC DNA, preventing spreading of CpG methylation and maintaining
CC methylation-free zones. Inversely, binding to target sites is prevented
CC by CpG methylation. Plays an important role in chromatin remodeling.
CC Can dimerize when it is bound to different DNA sequences, mediating
CC long-range chromatin looping. Mediates interchromosomal association
CC between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a
CC common transcription factory. Causes local loss of histone acetylation
CC and gain of histone methylation in the beta-globin locus, without
CC affecting transcription. When bound to chromatin, it provides an anchor
CC point for nucleosomes positioning. Seems to be essential for homologous
CC X-chromosome pairing. May participate with Tsix in establishing a
CC regulatable epigenetic switch for X chromosome inactivation. May play a
CC role in preventing the propagation of stable methylation at the escape
CC genes from X-inactivation. Involved in sister chromatid cohesion.
CC Associates with both centromeres and chromosomal arms during metaphase
CC and required for cohesin localization to CTCF sites. Regulates
CC asynchronous replication of IGF2/H19. Plays a role in the recruitment
CC of CENPE to the pericentromeric/centromeric regions of the chromosome
CC during mitosis. {ECO:0000250|UniProtKB:P49711}.
CC -!- SUBUNIT: Interacts with CHD8. Interacts with LLPH. Interacts with
CC CENPE. {ECO:0000250|UniProtKB:P49711, ECO:0000250|UniProtKB:Q61164}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q61164}. Chromosome
CC {ECO:0000250|UniProtKB:P49711}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P49711}. Note=May translocate to the nucleolus
CC upon cell differentiation. Associates with both centromeres and
CC chromosomal arms during metaphase. Associates with the H19 ICR in
CC mitotic chromosomes. May be preferentially excluded from
CC heterochromatin during interphase. {ECO:0000250|UniProtKB:P49711}.
CC -!- PTM: Sumoylated on Lys-74 and Lys-699; sumoylation of CTCF contributes
CC to the repressive function of CTCF on the MYC P2 promoter.
CC {ECO:0000250|UniProtKB:Q61164}.
CC -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF133731; AAD27869.2; -; mRNA.
DR RefSeq; NP_114012.1; NM_031824.1.
DR AlphaFoldDB; Q9R1D1; -.
DR SMR; Q9R1D1; -.
DR STRING; 10116.ENSRNOP00000023851; -.
DR iPTMnet; Q9R1D1; -.
DR PhosphoSitePlus; Q9R1D1; -.
DR PaxDb; Q9R1D1; -.
DR PRIDE; Q9R1D1; -.
DR GeneID; 83726; -.
DR KEGG; rno:83726; -.
DR UCSC; RGD:621344; rat.
DR CTD; 10664; -.
DR RGD; 621344; Ctcf.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_002678_77_1_1; -.
DR InParanoid; Q9R1D1; -.
DR PhylomeDB; Q9R1D1; -.
DR PRO; PR:Q9R1D1; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q9R1D1; RN.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0001651; C:dense fibrillar component; IDA:RGD.
DR GO; GO:0001652; C:granular component; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0043035; F:chromatin insulator sequence binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0140588; P:chromatin looping; ISO:RGD.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0071514; P:genomic imprinting; ISO:RGD.
DR GO; GO:0010216; P:maintenance of DNA methylation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISO:RGD.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:RGD.
DR GO; GO:0035065; P:regulation of histone acetylation; ISO:RGD.
DR GO; GO:0031060; P:regulation of histone methylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Centromere; Chromatin regulator; Chromosome;
KW Chromosome partition; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..737
FT /note="Transcriptional repressor CTCF"
FT /id="PRO_0000047230"
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..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49711"
SQ SEQUENCE 737 AA; 83880 MW; B89A7AA7252DA7CE CRC64;
MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELPPQEDPS WQKDPDYQPP AKKTKKTKKS 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 IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
KMRSKKEDSS DSENAEPDLD DNEEEEEPAV EIEPEPEPQP QPQPQPQPQP VAPAPPPAKK
RRGRPPGRTN QPKQNQPTAI IQVEDQNTGA IENIIVEVKK EPDAEPAEGE EEEAQAAPAD
APNGDLTPEM ILSMMDR
