TFEC_PANTR
ID TFEC_PANTR Reviewed; 347 AA.
AC A2T713;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Transcription factor EC;
DE Short=TFE-C;
GN Name=TFEC; Synonyms=TCFEC;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; DQ977352; ABM91968.1; -; Genomic_DNA.
DR RefSeq; NP_001074952.1; NM_001081483.1.
DR RefSeq; XP_016813554.1; XM_016958065.1.
DR AlphaFoldDB; A2T713; -.
DR SMR; A2T713; -.
DR STRING; 9598.ENSPTRP00000033580; -.
DR PaxDb; A2T713; -.
DR Ensembl; ENSPTRT00000107525; ENSPTRP00000088067; ENSPTRG00000047353.
DR GeneID; 463668; -.
DR KEGG; ptr:463668; -.
DR CTD; 22797; -.
DR VGNC; VGNC:4533; TFEC.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000159404; -.
DR HOGENOM; CLU_031638_0_0_1; -.
DR InParanoid; A2T713; -.
DR OMA; HQIVNQT; -.
DR OrthoDB; 1211990at2759; -.
DR TreeFam; TF317174; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000047353; Expressed in adult mammalian kidney and 15 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..347
FT /note="Transcription factor EC"
FT /id="PRO_0000313566"
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; 38921 MW; B12B5FF2B63AB884 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 YCQQLTVSQR PSPEFCDQAI AFSDPLSYFT DLSFSAALKE
EQRLDGMLLD DTISPFGTDP LLSATSPAVS KESSRRSSFS SDDGDEL