ITF2_RAT
ID ITF2_RAT Reviewed; 589 AA.
AC Q62655; Q99N33;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Transcription factor 4;
DE Short=TCF-4;
DE AltName: Full=Immunoglobulin transcription factor 2;
DE Short=ITF-2;
DE Short=RITF-2;
DE AltName: Full=R8f DNA-binding protein;
DE AltName: Full=SL3-3 enhancer factor 2;
DE Short=SEF-2;
GN Name=Tcf4; Synonyms=Itf2, Sef2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Forebrain;
RA Diaz M.I., Lopez J., Padilla S., Madrazo J.A., Capo D., Cabrero N.,
RA Felix C., Ossorio J., Olmeda Y., Lugo D.I.;
RT "Identification and analysis of a novel helix-loop-helix transcription
RT factor-encoding gene from Rat forebrain.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-589 (ISOFORMS 1 AND 2).
RC STRAIN=New England Deaconess Hospital; TISSUE=Adrenal medulla;
RX PubMed=7913462; DOI=10.1016/s0021-9258(17)32330-x;
RA Yoon S.O., Chikaraishi D.M.;
RT "Isolation of two E-box binding factors that interact with the rat tyrosine
RT hydroxylase enhancer.";
RL J. Biol. Chem. 269:18453-18462(1994).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription factor that binds to the immunoglobulin
CC enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal
CC differentiation. Activates transcription by binding to the E box (5'-
CC CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2
CC initiator element (SSTR2-INR) to activate transcription (By
CC similarity). Interacts with the CCAAT displacement protein (CDP2) to
CC bind the tyrosine hydroxylase enhancer. {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms homo- or heterooligomers with myogenin. Interacts with
CC HIVEP2. Interacts with NEUROD2 (By similarity). Interacts with AGBL1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62655-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62655-2; Sequence=VSP_002116;
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DR EMBL; AF149284; AAK26670.1; -; mRNA.
DR EMBL; U09228; AAA21122.1; -; mRNA.
DR PIR; A53689; A53689.
DR RefSeq; NP_445821.1; NM_053369.1. [Q62655-2]
DR AlphaFoldDB; Q62655; -.
DR CORUM; Q62655; -.
DR STRING; 10116.ENSRNOP00000020431; -.
DR iPTMnet; Q62655; -.
DR PhosphoSitePlus; Q62655; -.
DR jPOST; Q62655; -.
DR PaxDb; Q62655; -.
DR GeneID; 84382; -.
DR KEGG; rno:84382; -.
DR CTD; 6925; -.
DR RGD; 69271; Tcf4.
DR eggNOG; KOG3910; Eukaryota.
DR InParanoid; Q62655; -.
DR OrthoDB; 571132at2759; -.
DR PhylomeDB; Q62655; -.
DR Reactome; R-RNO-525793; Myogenesis.
DR PRO; PR:Q62655; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISO:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0042118; P:endothelial cell activation; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0065004; P:protein-DNA complex assembly; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; ISO:RGD.
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 Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..589
FT /note="Transcription factor 4"
FT /id="PRO_0000127258"
FT DOMAIN 486..539
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..157
FT /note="Leucine-zipper"
FT REGION 138..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..403
FT /note="Class A specific domain"
FT REGION 384..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15884"
FT VAR_SEQ 464..467
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7913462, ECO:0000303|Ref.1"
FT /id="VSP_002116"
FT CONFLICT 582
FT /note="T -> A (in Ref. 2; AAA21122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 63053 MW; D2A271D197D1058C CRC64;
MTSRDLGSHD NLSPPFANSR IQSKTERGSY SSYGRENVQG CHQSLLGGDM DMGNPGTLSP
TKPGSQYYPY SSNNARRRPL HSSTMEVQTK KVRKVPPGLP SSVYAPSAST ADYNRDSPGY
SSSKPAASTF SSSFFMQDGH HSSDPWSSSS GMNQPGYGGM LGNSHIPQSS SYCSLHPHER
LSYPSHSSAD INSSLPPMST FHRSGTNHYS TSSCTPPANG TDSIMANRGT GAAGSSQTGD
ALGKALASIY SPDHTNNSFS SNPSTPVGSP PSLSAGTAVW SRNGGQASSS PNYEGPLHSL
QSRIEDRLER LDDAIHVLRN HAVGPSTAVP GGHGDMHGII GPSHNGAMGS LGSGYGTGLL
SANRHSLMVG AHREDGVALR GSHSLLPNQV PVPQLPVQSA TSPDLNPPQD PYRGMPPGLQ
GQSVSSGSSE IKSDDEGDEN LQDTKSSEDK KLDDDKKDIK SITRSRSSNN DDEDLTPEQK
AEREKERRMA NNARERLRVR DINEAFKELG RMVQLHLKSD KPQTKLLILH QAVAVILSLE
QQVRERNLNP KAACLKRREE EKVSSEPPPL SLAGPHPGMG DTANHMGQM
