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Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Pancreas specific transcription factor 1c) (Transcription factor 3) (TCF-3) (Transcription regulator Pan)

 TFE2_RAT                Reviewed;         649 AA.
P21677; P21676; Q08440; Q4VY47;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
23-MAY-2018, entry version 165.
RecName: Full=Transcription factor E2-alpha;
AltName: Full=Immunoglobulin enhancer-binding factor E12/E47;
AltName: Full=Pancreas specific transcription factor 1c;
AltName: Full=Transcription factor 3;
Short=TCF-3;
AltName: Full=Transcription regulator Pan;
Name=Tcf3; Synonyms=Pan, Ptf1c, Tcfe2a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E12 AND E47), AND FUNCTION.
PubMed=2200736; DOI=10.1101/gad.4.6.1035;
Nelson C., Shen L.-P., Meister A., Fodor E., Rutter W.J.;
"Pan: a transcriptional regulator that binds chymotrypsin, insulin,
and AP-4 enhancer motifs.";
Genes Dev. 4:1035-1043(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E12).
STRAIN=Sprague-Dawley;
Wellauer P.K.;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 427-649 (ISOFORM E12).
PubMed=1766666;
Metz R., Ziff E.;
"The helix-loop-helix protein rE12 and the C/EBP-related factor rNFIL-
6 bind to neighboring sites within the c-fos serum response element.";
Oncogene 6:2165-2178(1991).
[4]
INTERACTION WITH UBE2I.
STRAIN=CD Charles River; TISSUE=Aorta;
PubMed=9013644; DOI=10.1074/jbc.272.6.3845;
Kho C.-J., Huggins G.S., Endege W.O., Hsieh C.-M., Lee M.-E.,
Haber E.;
"Degradation of E2A proteins through a ubiquitin-conjugating enzyme,
UbcE2A.";
J. Biol. Chem. 272:3845-3851(1997).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Transcriptional regulator. Involved in the initiation of
neuronal differentiation. Heterodimers between TCF3 and tissue-
specific basic helix-loop-helix (bHLH) proteins play major roles
in determining tissue-specific cell fate during embryogenesis,
like muscle or early B-cell differentiation. Dimers bind DNA on E-
box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa
immunoglobulin gene enhancer (By similarity). Binds to the
consensus sequence CAC/GCTGT/C present, in the chymotrypsin,
insulin, AP-4, and several other gene enhancer motifs
(PubMed:2200736). {ECO:0000250|UniProtKB:P15806,
ECO:0000269|PubMed:2200736}.
-!- SUBUNIT: Homodimer. Heterodimer. Forms a heterodimer with MYOG;
heterodimerization enhances MYOG DNA-binding and transcriptional
activities. Forms a heterodimer with ASH1 and TWIST2. Forms a
heterodimer with NEUROD1; the heterodimer is inhibited in presence
of ID2, but not NR0B2, to E-box element. Isoform E12 interacts
with RALGAPA1 and FIGLA. Interacts with EP300, NEUROD2, PTF1A and
TGFB1I1. Component of a nuclear TAL-1 complex composed at least of
CBFA2T3, LDB1, TAL1 and TCF3. Efficient DNA binding requires
dimerization with another bHLH protein (By similarity). Interacts
with UBE2I. Interacts with BHLHA9. Forms a heterodimer with ATOH8;
repress transcription of TCF3 and TCF3/NEUROG3 dimer-induced
transactivation of E box-dependent promoters (By similarity).
{ECO:0000250|UniProtKB:P15806, ECO:0000250|UniProtKB:P15923,
ECO:0000269|PubMed:9013644}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=E12; Synonyms=PAN-2;
IsoId=P21677-1; Sequence=Displayed;
Name=E47; Synonyms=PAN-1;
IsoId=P21677-2; Sequence=VSP_002157;
Note=Contains a phosphothreonine at position 526. {ECO:0000250};
-!- PTM: Phosphorylated following NGF stimulation.
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EMBL; X54549; CAA38421.1; -; mRNA.
EMBL; X62323; CAA44199.1; -; mRNA.
EMBL; AJ973227; CAJ00426.1; -; mRNA.
EMBL; S77532; AAB21103.1; -; mRNA.
PIR; A35816; A35816.
PIR; B35816; B35816.
PIR; I78853; I78853.
RefSeq; NP_001030314.1; NM_001035237.1.
RefSeq; NP_598208.2; NM_133524.2.
UniGene; Rn.10290; -.
ProteinModelPortal; P21677; -.
SMR; P21677; -.
BioGrid; 251063; 4.
CORUM; P21677; -.
STRING; 10116.ENSRNOP00000023473; -.
iPTMnet; P21677; -.
PhosphoSitePlus; P21677; -.
PaxDb; P21677; -.
PRIDE; P21677; -.
GeneID; 171046; -.
KEGG; rno:171046; -.
UCSC; RGD:620914; rat. [P21677-1]
CTD; 6929; -.
RGD; 620914; Tcf3.
eggNOG; KOG3910; Eukaryota.
eggNOG; ENOG410XYUA; LUCA.
HOGENOM; HOG000234180; -.
HOVERGEN; HBG003854; -.
InParanoid; P21677; -.
KO; K09063; -.
PhylomeDB; P21677; -.
PRO; PR:P21677; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0002326; P:B cell lineage commitment; ISS:UniProtKB.
GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 649 Transcription factor E2-alpha.
/FTId=PRO_0000127469.
DOMAIN 544 597 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 385 420 Leucine-zipper.
MOTIF 171 177 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 351 351 Phosphothreonine.
{ECO:0000250|UniProtKB:P15806}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 367 367 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P15806}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
CROSSLNK 494 494 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P15923}.
CROSSLNK 620 620 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P15923}.
VAR_SEQ 525 596 PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFK
ELGRMCQLHLSTEKPQTKLLILHQAVAVILS -> STDEVL
SLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQLH
LKSDKAQTKLLILQQAVQVILG (in isoform E47).
{ECO:0000303|PubMed:2200736}.
/FTId=VSP_002157.
CONFLICT 167 167 L -> LA (in Ref. 1; CAA44199).
{ECO:0000305}.
CONFLICT 427 427 P -> A (in Ref. 3; AAB21103).
{ECO:0000305}.
CONFLICT 508 508 D -> DH (in Ref. 3; AAB21103).
{ECO:0000305}.
CONFLICT 576 577 ST -> NS (in Ref. 3; AAB21103).
{ECO:0000305}.
CONFLICT 637 637 P -> T (in Ref. 3; AAB21103).
{ECO:0000305}.
SEQUENCE 649 AA; 67655 MW; 882F19EDB47D14EA CRC64;
MMNQSQRMAP VGSDKELSDL LDFSMMFPLP VANGKGRPAS LAGTQFAGSG LEDRPSSESW
GNSEQNSSSF DPSRAYSEGA HFSDSHSSLP PSTFLGAGLG GKGSERNAYA TFGRDTSVGT
LSQAGFLPGE LGLSSPGPLS PSGVKSSSQY YTSFPSNPRR RAADGGLDTQ PKKVRKVPPG
LPSSVYPSSS GDNYSRDATA YPSAKTPSSA YPSPFYVADG SLHPSAELWS PPGQVGFGPM
LGDGSAPLPL APGSSSVSSG AFGGLQQQDR MGYQLHGSEV NGTLPAVSSF SAAPGTYSGT
SGHTPPVSGA DSLLGTRGTT ASSSGDALGK ALASIYSPDH SSNNFSPSPS TPVGSPQGLP
GTSQWPRAGA PSALSPNYDA GLHGLSKMED RLDEAIHVLR SHAVGTASEL HGLLPGHSTL
TTSFAGPMSL GGRHAGLVSG SHPEDGLTSG ASLLHNHASL PSQPSSLPDL SQRPPDSFSG
LGRAGVTAGA SEIKREEKED EEVTSVADAE EDKKDLKVPR TRTSPDEDED DLLPPEQKAE
REKERRVANN ARERLRVRDI NEAFKELGRM CQLHLSTEKP QTKLLILHQA VAVILSLEQQ
VRERNLNPKA ACLKRREEEK VSGVVGDPQL ALSAAHPGLG EAHNPAGHL


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