TF7L1_XENTR
ID TF7L1_XENTR Reviewed; 553 AA.
AC Q6GL68;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transcription factor 7-like 1;
DE AltName: Full=HMG box transcription factor 3;
DE Short=TCF-3;
GN Name=tcf7l1; Synonyms=tcf3;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and
CC acts as a repressor in the absence of ctnnb1, and as an activator in
CC its presence. Required early in development for the establishment of
CC the dorsal body axis in response to maternal Wnt signaling (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with csnk1e, ctnnb1, ctbp, dact1 and gsk3b. May
CC interact with ase and tle4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- PTM: Phosphorylated. Phosphorylation by csnk1e promotes binding to
CC ctnnb1 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; BC074638; AAH74638.1; -; mRNA.
DR RefSeq; NP_001005640.1; NM_001005640.1.
DR AlphaFoldDB; Q6GL68; -.
DR SMR; Q6GL68; -.
DR STRING; 8364.ENSXETP00000045614; -.
DR PaxDb; Q6GL68; -.
DR DNASU; 448107; -.
DR GeneID; 448107; -.
DR KEGG; xtr:448107; -.
DR CTD; 83439; -.
DR Xenbase; XB-GENE-1031985; tcf7l1.
DR eggNOG; KOG3248; Eukaryota.
DR HOGENOM; CLU_013229_4_0_1; -.
DR InParanoid; Q6GL68; -.
DR OMA; HPLSWLV; -.
DR OrthoDB; 807716at2759; -.
DR PhylomeDB; Q6GL68; -.
DR TreeFam; TF318448; -.
DR Reactome; R-XTR-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-XTR-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-XTR-4086398; Ca2+ pathway.
DR Reactome; R-XTR-4641265; Repression of WNT target genes.
DR Reactome; R-XTR-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-XTR-8951430; RUNX3 regulates WNT signaling.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000019015; Expressed in gastrula and 14 other tissues.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..553
FT /note="Transcription factor 7-like 1"
FT /id="PRO_0000048620"
FT DNA_BIND 324..392
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..61
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 109..312
FT /note="Interaction with AES and TLE4"
FT /evidence="ECO:0000250"
FT REGION 183..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..553
FT /note="Interaction with CTBP"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60081 MW; 26B849B47470AE34 CRC64;
MPQLNSGGGD ELGANDELIR FKDEGEQEEK SPGEGSAEGD LADVKSSLVN ESENHSSDSD
SEVERRPPPR ETFEKPRDYL SEAFRRQQDA AFFKGPPYAG YPFLMIPDLG GHYLPNGALS
PSARTYLQMK WPLLDSPSTA GLKDARSPSP AHLSNKVPVV QHPHHMHPLT PLITYSNEHF
SPGTPPGHLS PEIDPKTGIP RPPHPSELSP YYPLSPGAVG QIPHPLGWLV PQQGQPMYSI
PPGGFRHPYP ALAMNASMSS LVSSRFSPHM VPPPHHGLHT SGIPHPAIVS PIVKQEPSSG
NISPNLITKP SVVVKKEEEK KPHIKKPLNA FMLYMKEMRA KVVAECTLKE SAAINQILGR
RWHSLSREEQ AKYYELARKE RQLHSQLYPT WSARDNYGKR KKRKRDKQSP EMEITKTKKM
CVQHLPADKS CDSPASSHGS MLDSPATPSA ALASPAAPAA THSEQAQPLS LTTKPEARAQ
LSLSHSAAFL ASKSPPSSSL SGSLSSPVGS PLLSRPIPLT SSILSPPCVF PSALQALPLL
QAQPLSLVTK SSD
