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Transcription factor 7-like 1-A (HMG box transcription factor 3-A) (TCF-3-A) (xTcf-3)

 T7L1A_XENLA             Reviewed;         554 AA.
P70062;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Transcription factor 7-like 1-A;
AltName: Full=HMG box transcription factor 3-A;
Short=TCF-3-A;
Short=xTcf-3;
Name=tcf7l1-a; Synonyms=tcf3, tcf3a;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=8756721; DOI=10.1016/S0092-8674(00)80112-9;
Molenaar M., van de Wetering M., Peterson-Maduro J., Godsave S.,
Korinkek V., Roose J., Destree O., Clevers H.;
"XTcf-3 transcription factor mediates beta-catenin-induced axis
formation in Xenopus embryos.";
Cell 86:391-399(1996).
[2]
FUNCTION, DNA-BINDING, AND INTERACTION WITH CTNNB1-A.
PubMed=9308964; DOI=10.1101/gad.11.18.2359;
Brannon M., Gomperts M., Sumoy L., Moon R.T., Kimelman D.;
"A beta-catenin/XTcf-3 complex binds to the siamois promoter to
regulate dorsal axis specification in Xenopus.";
Genes Dev. 11:2359-2370(1997).
[3]
FUNCTION, AND INTERACTION WITH AES AND TLE4-A.
PubMed=9783587; DOI=10.1038/26989;
Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
Moerer P., van de Wetering M., Destree O., Clevers H.;
"The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
transcriptional repressors.";
Nature 395:608-612(1998).
[4]
FUNCTION, INTERACTION WITH CTBP-B, AND MUTAGENESIS OF 469-PRO-LEU-470
AND 545-PRO-LEU-546.
PubMed=10375506;
Brannon M., Brown J.D., Bates R., Kimelman D., Moon R.T.;
"XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus
development.";
Development 126:3159-3170(1999).
[5]
FUNCTION.
PubMed=10495268; DOI=10.1016/S0925-4773(99)00136-7;
McGrew L.L., Takemaru K., Bates R., Moon R.T.;
"Direct regulation of the Xenopus engrailed-2 promoter by the Wnt
signaling pathway, and a molecular screen for Wnt-responsive genes,
confirm a role for Wnt signaling during neural patterning in
Xenopus.";
Mech. Dev. 87:21-32(1999).
[6]
FUNCTION.
PubMed=10559484; DOI=10.1016/S0925-4773(99)00210-5;
Marikawa Y., Elinson R.P.;
"Relationship of vegetal cortical dorsal factors in the Xenopus egg
with the Wnt/beta-catenin signaling pathway.";
Mech. Dev. 89:93-102(1999).
[7]
FUNCTION.
PubMed=11493528;
Hamilton F.S., Wheeler G.N., Hoppler S.;
"Difference in XTcf-3 dependency accounts for change in response to
beta-catenin-mediated Wnt signalling in Xenopus blastula.";
Development 128:2063-2073(2001).
[8]
FUNCTION.
PubMed=11356018; DOI=10.1006/dbio.2001.0253;
Darken R.S., Wilson P.A.;
"Axis induction by wnt signaling: target promoter responsiveness
regulates competence.";
Dev. Biol. 234:42-54(2001).
[9]
FUNCTION, INTERACTION WITH CSNK1E; CTNNB1-A AND GSK3B, SUBCELLULAR
LOCATION, AND PHOSPHORYLATION.
PubMed=11524435; DOI=10.1083/jcb.200102074;
Lee E., Salic A., Kirschner M.W.;
"Physiological regulation of beta-catenin stability by Tcf3 and
CK1epsilon.";
J. Cell Biol. 154:983-993(2001).
[10]
FUNCTION, AND DNA-BINDING.
PubMed=11238923; DOI=10.1128/MCB.21.5.1866-1873.2001;
Snider L., Thirlwell H., Miller J.R., Moon R.T., Groudine M.,
Tapscott S.J.;
"Inhibition of Tcf3 binding by I-mfa domain proteins.";
Mol. Cell. Biol. 21:1866-1873(2001).
[11]
FUNCTION.
PubMed=12445388; DOI=10.1016/S0960-9822(02)01280-0;
Roeel G., Hamilton F.S., Gent Y., Bain A.A., Destree O., Hoppler S.;
"Lef-1 and Tcf-3 transcription factors mediate tissue-specific Wnt
signaling during Xenopus development.";
Curr. Biol. 12:1941-1945(2002).
[12]
FUNCTION.
PubMed=12163405;
Houston D.W., Kofron M., Resnik E., Langland R., Destree O., Wylie C.,
Heasman J.;
"Repression of organizer genes in dorsal and ventral Xenopus cells
mediated by maternal XTcf3.";
Development 129:4015-4025(2002).
[13]
FUNCTION.
PubMed=11934150;
Rex M., Hilton E., Old R.W.;
"Multiple interactions between maternally-activated signalling
pathways control Xenopus nodal-related genes.";
Int. J. Dev. Biol. 46:217-226(2002).
[14]
DNA-BINDING.
PubMed=12049769; DOI=10.1016/S0925-4773(02)00121-1;
Yang J., Mei W., Otto A., Xiao L., Tao Q., Geng X., Rupp R.A.W.,
Ding X.;
"Repression through a distal TCF-3 binding site restricts Xenopus myf-
5 expression in gastrula mesoderm.";
Mech. Dev. 115:79-89(2002).
[15]
FUNCTION.
PubMed=14568102; DOI=10.1016/j.mod.2003.08.004;
Hilton E., Rex M., Old R.;
"VegT activation of the early zygotic gene Xnr5 requires lifting of
Tcf-mediated repression in the Xenopus blastula.";
Mech. Dev. 120:1127-1138(2003).
[16]
FUNCTION, AND INTERACTION WITH DACT1-A.
PubMed=15329348; DOI=10.1242/dev.01369;
Hikasa H., Sokol S.Y.;
"The involvement of Frodo in TCF-dependent signaling and neural tissue
development.";
Development 131:4725-4734(2004).
[17]
FUNCTION.
PubMed=15747128; DOI=10.1007/s00427-005-0474-0;
Tsuji S., Hashimoto C.;
"Choice of either beta-catenin or Groucho/TLE as a co-factor for Xtcf-
3 determines dorsal-ventral cell fate of diencephalon during Xenopus
development.";
Dev. Genes Evol. 215:275-284(2005).
[18]
FUNCTION.
PubMed=15923623; DOI=10.1128/MCB.25.12.5061-5072.2005;
Snider L., Tapscott S.J.;
"XIC is required for Siamois activity and dorsoanterior development.";
Mol. Cell. Biol. 25:5061-5072(2005).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-61.
PubMed=11136974; DOI=10.1016/S0092-8674(00)00192-6;
Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.;
"Crystal structure of a beta-catenin/Tcf complex.";
Cell 103:885-896(2000).
-!- FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA
and acts as a repressor in the absence of ctnnb1-A and possibly
ctnnb1-B, and as an activator in the presence of these proteins.
Required early in development for the establishment of the dorsal
body axis in response to maternal Wnt signaling. Also required
during development of the CNS for the establishment of dorsal-
ventral patterning in the prospective diencephalon.
{ECO:0000269|PubMed:10375506, ECO:0000269|PubMed:10495268,
ECO:0000269|PubMed:10559484, ECO:0000269|PubMed:11238923,
ECO:0000269|PubMed:11356018, ECO:0000269|PubMed:11493528,
ECO:0000269|PubMed:11524435, ECO:0000269|PubMed:11934150,
ECO:0000269|PubMed:12163405, ECO:0000269|PubMed:12445388,
ECO:0000269|PubMed:14568102, ECO:0000269|PubMed:15329348,
ECO:0000269|PubMed:15747128, ECO:0000269|PubMed:15923623,
ECO:0000269|PubMed:8756721, ECO:0000269|PubMed:9308964,
ECO:0000269|PubMed:9783587}.
-!- SUBUNIT: Interacts with csnk1e, ctnnb1-A, ctbp-B, dact1-A and
gsk3b. May interact with ase and tle4-A.
{ECO:0000269|PubMed:10375506, ECO:0000269|PubMed:11524435,
ECO:0000269|PubMed:15329348, ECO:0000269|PubMed:9308964,
ECO:0000269|PubMed:9783587}.
-!- INTERACTION:
Q8JJ48:dact1-a; NbExp=3; IntAct=EBI-6259044, EBI-6259065;
A0SNQ7:tshz3; NbExp=2; IntAct=EBI-6259044, EBI-7373787;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- PTM: Phosphorylated. Phosphorylation by csnk1e promotes binding to
ctnnb1-A while phosphorylation by gsk3b may reverse this effect.
{ECO:0000269|PubMed:11524435}.
-!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X99308; CAA67686.1; -; mRNA.
RefSeq; NP_001081483.1; NM_001088014.1.
UniGene; Xl.1100; -.
PDB; 1G3J; X-ray; 2.10 A; B/D=1-61.
PDBsum; 1G3J; -.
ProteinModelPortal; P70062; -.
SMR; P70062; -.
ELM; P70062; -.
IntAct; P70062; 5.
MINT; MINT-4790980; -.
GeneID; 397863; -.
KEGG; xla:397863; -.
CTD; 397863; -.
Xenbase; XB-GENE-6252329; tcf7l1.
HOVERGEN; HBG000419; -.
KO; K04490; -.
EvolutionaryTrace; P70062; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IPI:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR027397; Catenin_binding_dom.
InterPro; IPR013558; CTNNB1-bd_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR024940; TCF/LEF.
InterPro; IPR028773; TCF7L.
PANTHER; PTHR10373; PTHR10373; 1.
PANTHER; PTHR10373:SF25; PTHR10373:SF25; 1.
Pfam; PF08347; CTNNB1_binding; 1.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Cytoplasm; Developmental protein;
DNA-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
Transcription regulation; Wnt signaling pathway.
CHAIN 1 554 Transcription factor 7-like 1-A.
/FTId=PRO_0000048616.
DNA_BIND 324 392 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 61 Interaction with CTNNB1-A.
REGION 109 312 Interaction with AES and TLE4-A.
{ECO:0000269|PubMed:9783587}.
REGION 408 554 Interaction with CTBP-B.
{ECO:0000269|PubMed:10375506}.
COMPBIAS 148 291 Pro-rich.
COMPBIAS 483 528 Ser-rich.
MUTAGEN 469 470 PL->AS: May abrogate binding to CTBP-B.
{ECO:0000269|PubMed:10375506}.
MUTAGEN 545 546 PL->AS: May abrogate binding to CTBP-B.
{ECO:0000269|PubMed:10375506}.
HELIX 42 49 {ECO:0000244|PDB:1G3J}.
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


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