CTCFL_MOUSE
ID CTCFL_MOUSE Reviewed; 636 AA.
AC A2APF3; B9EKP6; Q3Y6S0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transcriptional repressor CTCFL;
DE AltName: Full=Brother of the regulator of imprinted sites;
DE AltName: Full=CCCTC-binding factor;
DE AltName: Full=CTCF paralog;
DE AltName: Full=CTCF-like protein;
GN Name=Ctcfl; Synonyms=Boris;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=12011441; DOI=10.1073/pnas.092123699;
RA Loukinov D.I., Pugacheva E., Vatolin S., Pack S.D., Moon H., Chernukhin I.,
RA Mannan P., Larsson E., Kanduri C., Vostrov A.A., Cui H., Niemitz E.L.,
RA Rasko J.E.J., Docquier F.M., Kistler M., Breen J.J., Zhuang Z.,
RA Quitschke W.W., Renkawitz R., Klenova E.M., Feinberg A.P., Ohlsson R.,
RA Morse H.C. III, Lobanenkov V.V.;
RT "BORIS, a novel male germ-line-specific protein associated with epigenetic
RT reprogramming events, shares the same 11-zinc-finger domain with CTCF, the
RT insulator protein involved in reading imprinting marks in the soma.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6806-6811(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DNA-BINDING, AND INTERACTION WITH HISTONE AND PRMT7.
RX PubMed=17048991; DOI=10.1371/journal.pbio.0040355;
RA Jelinic P., Stehle J.-C., Shaw P.;
RT "The testis-specific factor CTCFL cooperates with the protein
RT methyltransferase PRMT7 in H19 imprinting control region methylation.";
RL PLoS Biol. 4:E355-E355(2006).
CC -!- FUNCTION: Testis-specific DNA binding protein responsible for insulator
CC function, nuclear architecture and transcriptional control, which
CC probably acts by recruiting epigenetic chromatin modifiers. Plays a key
CC role in gene imprinting in male germline, by participating in the
CC establishment of differential methylation at the IGF2/H19 imprinted
CC control region (ICR). Directly binds the unmethylated H19 ICR and
CC recruits the PRMT7 methyltransferase, leading to methylate histone H4
CC 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA
CC methyltransferases at these sites. Seems to act as tumor suppressor. In
CC association with DNMT1 and DNMT3B, involved in activation of BAG1 gene
CC expression by binding to its promoter. Required for dimethylation of H3
CC lysine 4 (H3K4me2) of MYC and BRCA1 promoters.
CC {ECO:0000269|PubMed:17048991}.
CC -!- SUBUNIT: Interacts with histones, PRMT7 and SETD1A. Interacts (via N-
CC terminus) with BAG6/BAT3 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC A2APF3; Q922X9: Prmt7; NbExp=3; IntAct=EBI-11566304, EBI-15606508;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:17048991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2APF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2APF3-2; Sequence=VSP_037281;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17048991}.
CC -!- DEVELOPMENTAL STAGE: Not detected at 13.5 dpc. Detected in mitotically
CC arrested gonocytes of 14.5 dpc embryos. From 17.5 dpc to newborn, it is
CC expressed in some centrally located gonocytes and cells present at the
CC periphery of the developing seminiferous tubules. Present in nuclei of
CC spermatogonia from 15 days after birth to adulthood.
CC {ECO:0000269|PubMed:17048991}.
CC -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; DQ153171; AAZ79234.1; -; mRNA.
DR EMBL; AL837509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151026; AAI51027.1; -; mRNA.
DR CCDS; CCDS38349.1; -. [A2APF3-1]
DR RefSeq; NP_001074856.1; NM_001081387.2. [A2APF3-1]
DR RefSeq; XP_017174657.1; XM_017319168.1.
DR AlphaFoldDB; A2APF3; -.
DR SMR; A2APF3; -.
DR BioGRID; 576678; 26.
DR DIP; DIP-29209N; -.
DR IntAct; A2APF3; 5.
DR STRING; 10090.ENSMUSP00000091845; -.
DR iPTMnet; A2APF3; -.
DR PhosphoSitePlus; A2APF3; -.
DR MaxQB; A2APF3; -.
DR PaxDb; A2APF3; -.
DR PeptideAtlas; A2APF3; -.
DR PRIDE; A2APF3; -.
DR ProteomicsDB; 277914; -. [A2APF3-1]
DR ProteomicsDB; 277915; -. [A2APF3-2]
DR Antibodypedia; 744; 271 antibodies from 33 providers.
DR DNASU; 664799; -.
DR Ensembl; ENSMUST00000094287; ENSMUSP00000091845; ENSMUSG00000070495. [A2APF3-1]
DR Ensembl; ENSMUST00000179693; ENSMUSP00000135932; ENSMUSG00000070495. [A2APF3-1]
DR GeneID; 664799; -.
DR KEGG; mmu:664799; -.
DR UCSC; uc008odi.1; mouse. [A2APF3-1]
DR UCSC; uc012cks.1; mouse. [A2APF3-2]
DR CTD; 140690; -.
DR MGI; MGI:3652571; Ctcfl.
DR VEuPathDB; HostDB:ENSMUSG00000070495; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161524; -.
DR HOGENOM; CLU_002678_77_1_1; -.
DR InParanoid; A2APF3; -.
DR OMA; LTCEMIF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A2APF3; -.
DR TreeFam; TF106430; -.
DR BioGRID-ORCS; 664799; 2 hits in 75 CRISPR screens.
DR PRO; PR:A2APF3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2APF3; protein.
DR Bgee; ENSMUSG00000070495; Expressed in dorsal root ganglion and 30 other tissues.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
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:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IDA:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IDA:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; ISO:MGI.
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; 3.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Tumor suppressor; Zinc;
KW Zinc-finger.
FT CHAIN 1..636
FT /note="Transcriptional repressor CTCFL"
FT /id="PRO_0000373924"
FT ZN_FING 257..279
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..336
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..421
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..451
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..537
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..572
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 17..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 598
FT /note="E -> EDVATQESATS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037281"
FT CONFLICT 629
FT /note="I -> M (in Ref. 1; AAZ79234 and 3; AAI51027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 73108 MW; BECF76F0C84FA7F0 CRC64;
MAAAEVPVPS GYFTQIKEQK LKPGDLEEEK EEDGVQRVEA QEGVVKEVEA ENSCLLLEAR
APVESDRRIL TLQTVHLESQ DVHLQGLGWL SVPHSEELSG TVPEAEGILQ LPSVLWLDPE
PQLSLQHCVT VSIPEELYPP EELQRIHFHL LRENVLMAEE NPELTPDLDE STALKKPEED
EKDQLPPQGE TDKREERLLL LEMKPKEGKD DEIVLTISHL SLEEQQDPPA ANQTSVPGAK
AAKPKRRRQT KGKPQSFQCD TCPFTSSKLS TFNRHIKIHS NERPHLCHLC LKAFRTVTLL
RNHVNTHTGT RPHKCRDCDM AFVTSGELVR HRRYKHTYEK PFKCSLCKYA SVEASKMKRH
IRSHTGERPF QCCQCAYASR DSYKLKRHMR THSGEKPYEC PTCHVRFTQS GTMKIHIAQK
HGENVPKYEC PHCATIIARK SDLRVHLRNL HSQSPEEMKC RYCPAGFHER YALIQHQRTH
KNEKKFKCKQ CDYACKQERC LKAHMRMHTG EKPFSCLACN KHFRQKQLLT VHLRKYHDPN
FVPNLHLCLK CDKRFSRWSN LQRHRKKCDP EHETLAPNKD RRPVTRTQAS EGEAGHKEGE
PQCPGEQALG HQGEAAGSQS PDHGLTCEII FNMMDK
