T7L1C_XENLA
ID T7L1C_XENLA Reviewed; 550 AA.
AC P70063;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Transcription factor 7-like 1-C;
DE AltName: Full=HMG box transcription factor 3-C;
DE Short=TCF-3-C;
DE Short=xTcf-3c;
GN Name=tcf7l1-c; Synonyms=tcf3c;
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; X99309; CAA67687.1; -; mRNA.
DR RefSeq; NP_001165163.1; NM_001171692.1.
DR AlphaFoldDB; P70063; -.
DR SMR; P70063; -.
DR GeneID; 397969; -.
DR CTD; 397969; -.
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-C"
FT /id="PRO_0000048618"
FT DNA_BIND 323..391
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..60
FT /note="Interaction with CTNNB1-A"
FT /evidence="ECO:0000250"
FT REGION 108..311
FT /note="Interaction with AES and TLE4-A"
FT /evidence="ECO:0000250"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..473
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..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 60006 MW; E0098A583BC98037 CRC64;
MPQLNSGGGD ELGANDELIR FKDEGEQEEK SPGEGSAEDL ADVKSSLVNE SENHSSDSDS
EVERRPPPRE TFEKPRDYLS EAFRRQQDAA FFKGPPYAGY PFLMIPDLGG ITCPMVPSHP
ASRAYLQMKW PLLDSPSTAG LKDARSPSPA HLSNKVPVVQ HPHHMHPLTP LITYSNEHFS
PGTPPGHLSP EIDPKTGIPR PPHPSELSPY YPLSPGAVGQ IPHRLGWLVP QQGQPMYSIP
PGGFRHPYPA LAMNASMSSL VSSRFSPHMV PPPHHSLHTS GIPHPAIVSP IVKQEPSSGN
ISPNLSRKSN VVVKKEEEKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES AAINQILGRR
WHSLSREEQA KYYELARKER QLHSQLYPSW SARDNYGKKK KRKREKQSPE MENYTKTKKM
CVQHFPSDKS CDSPASSHGS MLDSPATPSA ALASPAAPAA THSEQAQPLS LTTKPEARAL
SHSAAFLASK SPSSSSLSGH LPSPVGASLL SRPIPLTSSI LSPPGVFPSA LQALPLLQAQ
PLSLVTRSSD