ID   T7L1D_XENLA             Reviewed;         550 AA.
AC   P70064;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Transcription factor 7-like 1-D;
DE   AltName: Full=HMG box transcription factor 3-D;
DE            Short=TCF-3-D;
DE            Short=xTcf-3d;
GN   Name=tcf7l1-d; Synonyms=tcf3d;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8756721; DOI=10.1016/s0092-8674(00)80112-9;
RA   Molenaar M., van de Wetering M., Peterson-Maduro J., Godsave S.,
RA   Korinkek V., Roose J., Destree O., Clevers H.;
RT   "XTcf-3 transcription factor mediates beta-catenin-induced axis formation
RT   in Xenopus embryos.";
RL   Cell 86:391-399(1996).
CC   -!- FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and
CC       acts as a repressor in the absence of ctnnb1-A and possibly ctnnb1-B,
CC       and as an activator in the presence of these proteins. Required early
CC       in development for the establishment of the dorsal body axis in
CC       response to maternal Wnt signaling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with csnk1e, ctnnb1-A, ctbp-B, dact1-A and gsk3b.
CC       May interact with ase and tle4-A (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- PTM: Phosphorylated. Phosphorylation by csnk1e promotes binding to
CC       ctnnb1-A while phosphorylation by gsk3b may reverse this effect (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR   EMBL; X99310; CAA67688.1; -; mRNA.
DR   RefSeq; NP_001165165.1; NM_001171694.1.
DR   GeneID; 100329123; -.
DR   CTD; 100329123; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013558; CTNNB1-bd_N.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR024940; TCF/LEF.
DR   InterPro; IPR028778; Tcf7l1.
DR   PANTHER; PTHR10373; PTHR10373; 1.
DR   PANTHER; PTHR10373:SF25; PTHR10373:SF25; 1.
DR   Pfam; PF08347; CTNNB1_binding; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Wnt signaling pathway.
FT   CHAIN           1..550
FT                   /note="Transcription factor 7-like 1-D"
FT                   /id="PRO_0000048619"
FT   DNA_BIND        323..391
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..61
FT                   /note="Interaction with CTNNB1-A"
FT                   /evidence="ECO:0000250"
FT   REGION          109..311
FT                   /note="Interaction with AES and TLE4-A"
FT                   /evidence="ECO:0000250"
FT   REGION          173..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..550
FT                   /note="Interaction with CTBP-B"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        15..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  60063 MW;  C7D9D361DE4D3268 CRC64;
     MPQLNSGXGD ELGANDELIR FKDEGEQEEK SPGEGSAEGD LADVKSSLVN ESENHSSDSD
     SEVERRPPPR ETFEKPRDYL SEAFRRQQDA AFFKGPPYAG YPFLMIPDLG GITCPMVPSH
     PALAYLQMKW PLLDSPSTAG LKDARSPSPA HLSNKVPVVQ HPHHMHPLTP LITYSNEHFS
     PGTPPGHLSP EIDPKTGIPR PPHPSELSPY YPLSPGAVGQ IPHPLGWLVP QQGQPMYSIP
     PGGFRHPYPA LAMNASMSSL VSSRFSPHMV PPPHHSLHTS GIPHPAIVSP IVKQEPSSGN
     ISPNLSMKSN VVVKKEEEKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES AAINQILGRR
     WHSLSREEQA KYYELARKER QLHSQLYPSW SARDNYGKKK KRKREKQSPE MENYTKTKKM
     CVQHFPSDKS CDSPASSHGS MLDSPATPSA ALASPREPAA THSEEAQPLS LTTKPEARAL
     SHSAAFLASK SPSSSSLSGH LPSPVGSPLL SRPIPLTSSI LSPPGVFPPA LQALPLLQAQ
     PLPLVARSSD