ID   TFE2_XENLA              Reviewed;         658 AA.
AC   Q01978; Q5D0A6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Transcription factor E2-alpha;
DE   AltName: Full=Transcription factor 3;
DE            Short=TCF-3;
DE   AltName: Full=Transcription factor XE12/XE47;
GN   Name=tcf3; Synonyms=e2a;
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], ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Neurula;
RX   PubMed=1322293; DOI=10.1002/j.1460-2075.1992.tb05368.x;
RA   Rashbass J., Taylor M.V., Gurdon J.B.;
RT   "The DNA-binding protein E12 co-operates with XMyoD in the activation of
RT   muscle-specific gene expression in Xenopus embryos.";
RL   EMBO J. 11:2981-2990(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=16291758; DOI=10.1074/jbc.m505869200;
RA   Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.;
RT   "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-
RT   driven transcription.";
RL   J. Biol. Chem. 281:1755-1764(2006).
CC   -!- FUNCTION: Transcriptional regulator involved in the initiation of
CC       neuronal differentiation and mesenchymal to epithelial transition.
CC       Heterodimers between tcf3 and tissue-specific basic helix-loop-helix
CC       (bHLH) proteins play major roles in determining tissue-specific cell
CC       fate during embryogenesis, like muscle or early B-cell differentiation.
CC       Together with tcf15, required for the mesenchymal to epithelial
CC       transition. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'.
CC       {ECO:0000250|UniProtKB:P15806}.
CC   -!- SUBUNIT: Homodimer. Heterodimer; efficient DNA binding requires
CC       dimerization with another bHLH protein (By similarity). Interacts with
CC       tgfb1i1 (PubMed:16291758). {ECO:0000250|UniProtKB:P15806,
CC       ECO:0000269|PubMed:16291758}.
CC   -!- INTERACTION:
CC       Q01978; Q61473: Sox17; Xeno; NbExp=3; IntAct=EBI-9106902, EBI-9106822;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15806}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=E12;
CC         IsoId=Q01978-1; Sequence=Displayed;
CC       Name=E47;
CC         IsoId=Q01978-2; Sequence=VSP_002158;
CC   -!- DEVELOPMENTAL STAGE: Isoform E12 and isoform E47 are present at all the
CC       stages of development and in all regions of the embryo.
CC       {ECO:0000269|PubMed:1322293}.
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DR   EMBL; X66959; CAA47381.1; -; mRNA.
DR   EMBL; BC046840; AAH46840.1; -; mRNA.
DR   PIR; S23391; S23391.
DR   RefSeq; NP_001079668.1; NM_001086199.1. [Q01978-1]
DR   RefSeq; XP_018116184.1; XM_018260695.1. [Q01978-1]
DR   AlphaFoldDB; Q01978; -.
DR   SMR; Q01978; -.
DR   BioGRID; 97598; 5.
DR   IntAct; Q01978; 1.
DR   MaxQB; Q01978; -.
DR   DNASU; 379355; -.
DR   GeneID; 379355; -.
DR   KEGG; xla:379355; -.
DR   CTD; 379355; -.
DR   Xenbase; XB-GENE-865159; tcf3.L.
DR   OMA; AHVHRPH; -.
DR   OrthoDB; 571132at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 379355; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..658
FT                   /note="Transcription factor E2-alpha"
FT                   /id="PRO_0000127470"
FT   DOMAIN          555..608
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          42..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           173..179
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        140..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         534..606
FT                   /note="DEDEDEDDDNLPPEQKAEREKERRVANNARERLRVKDINEAFKELGRMCQLH
FT                   LNSEKPQTKLLILHQAVSVIL -> SKEDCVEEKDTKDRERRMSNNARERVRVRDINEA
FT                   FKELGRMVQMHMKADKAQTKLIILQQAVAVIM (in isoform E47)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002158"
SQ   SEQUENCE   658 AA;  70091 MW;  B7D8A3A069D9E033 CRC64;
     MNQQQRMTAV GTDKELSDLL DFSMMFPLPV ANGKTRPTTL ASTQFGGGSG LEERTGSAPW
     GTEDHNGSTF DQGRGYGDGT HYGEHRELPS HEGNLSAPFL ASGLVGKNDR PPYSTFGRDS
     GMTMNQTGFL SGDLAMNSPS ALSPNAGKAG SQYYTYPNNS RRRPGDSNLD AQPKKVRKVP
     PGLPSSVYPA NSGDEYCGDR GSYASTKTPN SVYPGAFYMA DGLHSSDIWA SSGGIGQGGY
     SSVLNSSQSS VSQTTGFSSL HPHERMGFPM HSGEVNPSVT SSFSSTPAQY GVSSHTPPIS
     TGDTIIGNRG TATGSSGDAL GKALASIYSP DHSSTNFSST PSTPVGSPQG ITGSGQWPRA
     NGPGALSPSY DGTLHTLQNK MEDRLDEAIH VLRSHAVGQT GALPGGHDDI HSLLSATASV
     LGSGFPAAVL SLANRHSMLN SHTEEALPSA SNMLHSQVTV PAQPGSLPDL TRPQDSYSGL
     PGLGRAIPPG RVPDIKRESK EDEENRSVAD LSDDEKKESK PQRSRTRCSI NSQDEDEDED
     DDNLPPEQKA EREKERRVAN NARERLRVKD INEAFKELGR MCQLHLNSEK PQTKLLILHQ
     AVSVILSLEQ QVRERNLNPK AACLKRREEE KVSGVDPQMG LSGGHPGVGD SHNPVGHM