ID   TFEC_PONPY              Reviewed;         347 AA.
AC   A2T7L8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Transcription factor EC;
DE            Short=TFE-C;
GN   Name=TFEC; Synonyms=TCFEC;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional regulator that acts as a repressor or an
CC       activator. Acts as a transcriptional repressor on minimal promoter
CC       containing element F (that includes an E-box sequence). Binds to
CC       element F in an E-box sequence-specific manner. Acts as a
CC       transcriptional transactivator on the proximal promoter region of the
CC       tartrate-resistant acid phosphatase (TRAP) E-box containing promoter.
CC       Collaborates with MITF in target gene activation. Acts as a
CC       transcriptional repressor on minimal promoter containing mu E3 enhancer
CC       sequence. Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain
CC       gene enhancer. Binds DNA in a homo- or heterodimeric form (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Forms heterodimers with MITF and TFE3. Interacts
CC       with MITF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
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DR   EMBL; DQ977502; ABM89296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2T7L8; -.
DR   SMR; A2T7L8; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR021802; MiT/TFE_C.
DR   InterPro; IPR024101; TFEC.
DR   PANTHER; PTHR45776:SF1; PTHR45776:SF1; 1.
DR   Pfam; PF11851; DUF3371; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Nucleus; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..347
FT                   /note="Transcription factor EC"
FT                   /id="PRO_0000313567"
FT   DOMAIN          139..192
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..119
FT                   /note="Necessary for transcriptional transactivation"
FT                   /evidence="ECO:0000250"
FT   REGION          271..347
FT                   /note="Necessary for transcriptional transactivation"
FT                   /evidence="ECO:0000250"
FT   REGION          319..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  38788 MW;  A29B4C4A1C88A985 CRC64;
     MTLDHQIINP TLKWSQPAVP SGGPLVQHAH TTLDSDAGLT ENPLTKLLAI GKEDDNAQWH
     MEDVIEDIIG MESSFKEEGA DSPLLMQRTL SGSILDVYSG EQGISPINMG LTSASCPSSL
     PMKREITETD TRALAKERQK KDNHNLIERR RRYNINYRIK ELGTLIPKSN DPDMRWNKGT
     ILKASVEYIK WLQKEQQRAR ELEHRQKKLE QANRRLLLRI QELEIQARTH GLPTLASLGT
     VDLGAHVTKQ QSHPEQNSVD YCQQLTVSQG PSPELCDQAI AFSDPLSYFT DLSFSAALKE
     EQRLDGMLLD DTISPFGTDP LLSATSPAVS KESSRRSSFS SDDGDEL