T7L1A_XENLA
ID T7L1A_XENLA Reviewed; 554 AA.
AC P70062;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transcription factor 7-like 1-A;
DE AltName: Full=HMG box transcription factor 3-A;
DE Short=TCF-3-A;
DE Short=xTcf-3;
GN Name=tcf7l1-a; Synonyms=tcf3, tcf3a;
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], FUNCTION, DNA-BINDING, AND SUBCELLULAR
RP LOCATION.
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).
RN [2]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH CTNNB1-A.
RX PubMed=9308964; DOI=10.1101/gad.11.18.2359;
RA Brannon M., Gomperts M., Sumoy L., Moon R.T., Kimelman D.;
RT "A beta-catenin/XTcf-3 complex binds to the siamois promoter to regulate
RT dorsal axis specification in Xenopus.";
RL Genes Dev. 11:2359-2370(1997).
RN [3]
RP FUNCTION, AND INTERACTION WITH AES AND TLE4-A.
RX PubMed=9783587; DOI=10.1038/26989;
RA Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P.,
RA van de Wetering M., Destree O., Clevers H.;
RT "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT transcriptional repressors.";
RL Nature 395:608-612(1998).
RN [4]
RP FUNCTION, INTERACTION WITH CTBP-B, AND MUTAGENESIS OF 469-PRO-LEU-470 AND
RP 545-PRO-LEU-546.
RX PubMed=10375506; DOI=10.1242/dev.126.14.3159;
RA Brannon M., Brown J.D., Bates R., Kimelman D., Moon R.T.;
RT "XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus
RT development.";
RL Development 126:3159-3170(1999).
RN [5]
RP FUNCTION.
RX PubMed=10495268; DOI=10.1016/s0925-4773(99)00136-7;
RA McGrew L.L., Takemaru K., Bates R., Moon R.T.;
RT "Direct regulation of the Xenopus engrailed-2 promoter by the Wnt signaling
RT pathway, and a molecular screen for Wnt-responsive genes, confirm a role
RT for Wnt signaling during neural patterning in Xenopus.";
RL Mech. Dev. 87:21-32(1999).
RN [6]
RP FUNCTION.
RX PubMed=10559484; DOI=10.1016/s0925-4773(99)00210-5;
RA Marikawa Y., Elinson R.P.;
RT "Relationship of vegetal cortical dorsal factors in the Xenopus egg with
RT the Wnt/beta-catenin signaling pathway.";
RL Mech. Dev. 89:93-102(1999).
RN [7]
RP FUNCTION.
RX PubMed=11493528; DOI=10.1242/dev.128.11.2063;
RA Hamilton F.S., Wheeler G.N., Hoppler S.;
RT "Difference in XTcf-3 dependency accounts for change in response to beta-
RT catenin-mediated Wnt signalling in Xenopus blastula.";
RL Development 128:2063-2073(2001).
RN [8]
RP FUNCTION.
RX PubMed=11356018; DOI=10.1006/dbio.2001.0253;
RA Darken R.S., Wilson P.A.;
RT "Axis induction by wnt signaling: target promoter responsiveness regulates
RT competence.";
RL Dev. Biol. 234:42-54(2001).
RN [9]
RP FUNCTION, INTERACTION WITH CSNK1E; CTNNB1-A AND GSK3B, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RX PubMed=11524435; DOI=10.1083/jcb.200102074;
RA Lee E., Salic A., Kirschner M.W.;
RT "Physiological regulation of beta-catenin stability by Tcf3 and
RT CK1epsilon.";
RL J. Cell Biol. 154:983-993(2001).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=11238923; DOI=10.1128/mcb.21.5.1866-1873.2001;
RA Snider L., Thirlwell H., Miller J.R., Moon R.T., Groudine M.,
RA Tapscott S.J.;
RT "Inhibition of Tcf3 binding by I-mfa domain proteins.";
RL Mol. Cell. Biol. 21:1866-1873(2001).
RN [11]
RP FUNCTION.
RX PubMed=12445388; DOI=10.1016/s0960-9822(02)01280-0;
RA Roeel G., Hamilton F.S., Gent Y., Bain A.A., Destree O., Hoppler S.;
RT "Lef-1 and Tcf-3 transcription factors mediate tissue-specific Wnt
RT signaling during Xenopus development.";
RL Curr. Biol. 12:1941-1945(2002).
RN [12]
RP FUNCTION.
RX PubMed=12163405; DOI=10.1242/dev.129.17.4015;
RA Houston D.W., Kofron M., Resnik E., Langland R., Destree O., Wylie C.,
RA Heasman J.;
RT "Repression of organizer genes in dorsal and ventral Xenopus cells mediated
RT by maternal XTcf3.";
RL Development 129:4015-4025(2002).
RN [13]
RP FUNCTION.
RX PubMed=11934150;
RA Rex M., Hilton E., Old R.W.;
RT "Multiple interactions between maternally-activated signalling pathways
RT control Xenopus nodal-related genes.";
RL Int. J. Dev. Biol. 46:217-226(2002).
RN [14]
RP DNA-BINDING.
RX PubMed=12049769; DOI=10.1016/s0925-4773(02)00121-1;
RA Yang J., Mei W., Otto A., Xiao L., Tao Q., Geng X., Rupp R.A.W., Ding X.;
RT "Repression through a distal TCF-3 binding site restricts Xenopus myf-5
RT expression in gastrula mesoderm.";
RL Mech. Dev. 115:79-89(2002).
RN [15]
RP FUNCTION.
RX PubMed=14568102; DOI=10.1016/j.mod.2003.08.004;
RA Hilton E., Rex M., Old R.;
RT "VegT activation of the early zygotic gene Xnr5 requires lifting of Tcf-
RT mediated repression in the Xenopus blastula.";
RL Mech. Dev. 120:1127-1138(2003).
RN [16]
RP FUNCTION, AND INTERACTION WITH DACT1-A.
RX PubMed=15329348; DOI=10.1242/dev.01369;
RA Hikasa H., Sokol S.Y.;
RT "The involvement of Frodo in TCF-dependent signaling and neural tissue
RT development.";
RL Development 131:4725-4734(2004).
RN [17]
RP FUNCTION.
RX PubMed=15747128; DOI=10.1007/s00427-005-0474-0;
RA Tsuji S., Hashimoto C.;
RT "Choice of either beta-catenin or Groucho/TLE as a co-factor for Xtcf-3
RT determines dorsal-ventral cell fate of diencephalon during Xenopus
RT development.";
RL Dev. Genes Evol. 215:275-284(2005).
RN [18]
RP FUNCTION.
RX PubMed=15923623; DOI=10.1128/mcb.25.12.5061-5072.2005;
RA Snider L., Tapscott S.J.;
RT "XIC is required for Siamois activity and dorsoanterior development.";
RL Mol. Cell. Biol. 25:5061-5072(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-61.
RX PubMed=11136974; DOI=10.1016/s0092-8674(00)00192-6;
RA Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/Tcf complex.";
RL Cell 103:885-896(2000).
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. Also required during development of
CC the CNS for the establishment of dorsal-ventral patterning in the
CC prospective diencephalon. {ECO:0000269|PubMed:10375506,
CC ECO:0000269|PubMed:10495268, ECO:0000269|PubMed:10559484,
CC ECO:0000269|PubMed:11238923, ECO:0000269|PubMed:11356018,
CC ECO:0000269|PubMed:11493528, ECO:0000269|PubMed:11524435,
CC ECO:0000269|PubMed:11934150, ECO:0000269|PubMed:12163405,
CC ECO:0000269|PubMed:12445388, ECO:0000269|PubMed:14568102,
CC ECO:0000269|PubMed:15329348, ECO:0000269|PubMed:15747128,
CC ECO:0000269|PubMed:15923623, ECO:0000269|PubMed:8756721,
CC ECO:0000269|PubMed:9308964, ECO:0000269|PubMed:9783587}.
CC -!- SUBUNIT: Interacts with csnk1e, ctnnb1-A, ctbp-B, dact1-A and gsk3b.
CC May interact with ase and tle4-A. {ECO:0000269|PubMed:10375506,
CC ECO:0000269|PubMed:11524435, ECO:0000269|PubMed:15329348,
CC ECO:0000269|PubMed:9308964, ECO:0000269|PubMed:9783587}.
CC -!- INTERACTION:
CC P70062; Q8JJ48: dact1-a; NbExp=3; IntAct=EBI-6259044, EBI-6259065;
CC P70062; A0SNQ7: tshz3.L; NbExp=2; IntAct=EBI-6259044, EBI-7373787;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: Phosphorylated. Phosphorylation by csnk1e promotes binding to
CC ctnnb1-A while phosphorylation by gsk3b may reverse this effect.
CC {ECO:0000269|PubMed:11524435}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR EMBL; X99308; CAA67686.1; -; mRNA.
DR RefSeq; NP_001081483.1; NM_001088014.1.
DR PDB; 1G3J; X-ray; 2.10 A; B/D=1-61.
DR PDBsum; 1G3J; -.
DR AlphaFoldDB; P70062; -.
DR SMR; P70062; -.
DR ELM; P70062; -.
DR IntAct; P70062; 5.
DR MINT; P70062; -.
DR GeneID; 397863; -.
DR KEGG; xla:397863; -.
DR CTD; 397863; -.
DR Xenbase; XB-GENE-6252329; tcf7l1.L.
DR OMA; HPLSWLV; -.
DR OrthoDB; 807716at2759; -.
DR EvolutionaryTrace; P70062; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397863; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 4.10.900.10; -; 1.
DR IDEAL; IID50010; -.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Developmental protein; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..554
FT /note="Transcription factor 7-like 1-A"
FT /id="PRO_0000048616"
FT DNA_BIND 324..392
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..61
FT /note="Interaction with CTNNB1-A"
FT REGION 109..312
FT /note="Interaction with AES and TLE4-A"
FT /evidence="ECO:0000269|PubMed:9783587"
FT REGION 183..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..554
FT /note="Interaction with CTBP-B"
FT /evidence="ECO:0000269|PubMed:10375506"
FT COMPBIAS 15..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
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..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 469..470
FT /note="PL->AS: May abrogate binding to CTBP-B."
FT /evidence="ECO:0000269|PubMed:10375506"
FT MUTAGEN 545..546
FT /note="PL->AS: May abrogate binding to CTBP-B."
FT /evidence="ECO:0000269|PubMed:10375506"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1G3J"
SQ SEQUENCE 554 AA; 60300 MW; 90B24D134AE4EBDD CRC64;
MPQLNSGGGD ELGANDELIR FKDEGEQEEK SPGEGSAEGD LADVKSSLVN ESENHSSDSD
SEVERRPPPR EAFEKHRDYL TEALRRQQDA AFFKGPPYAG YPFLMIPDLG GHYLPNGALS
PSARTYLQMK WPLLDSPSTA GLKDARSPSP AHLSNKVPVV QHPHHMHPLT PLITYSNEHF
SPGTPPGHLS PEIDPKTGIP RPPHPSELSP YYPLSPGAVG QIPHPLGWLV PPQGQPMYSI
PPGGFRHPYP ALAMNASMSS LVSSRFSPHM VPPPHHSLHT SGIPHPAIVS PIVKQEPSSG
NISPNLHTKS NMIVKKEEEK KPHIKKPLNA FMLYMKEMRA KVVAECTLKE SAAINQILGR
RWHSLSREEQ AKYYELARKE RQLHSQLYPS WSARDNYGKR KKRKREKQSP EMETHTKTKK
MCVQHLPADK SCDSPASSHG SMLDSPATPS AALASPAAPA ATHSEQAQPL SLTTKPEARA
QLSLSHSAAF LASKSPSSSS FSGHLSSPVG SPLLSRPIPL TSSILSPSGV FPSALQALPL
LQAQPLSLVT KSSD
