TFEC_MOUSE
ID TFEC_MOUSE Reviewed; 317 AA.
AC Q9WTW4; Q3TWR7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription factor EC;
DE Short=TFE-C;
DE Short=mTFEC;
GN Name=Tfec; Synonyms=Tcfec;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10036191; DOI=10.1006/geno.1998.5588;
RA Rehli M., Den Elzen N., Cassady A.I., Ostrowski M.C., Hume D.A.;
RT "Cloning and characterization of the murine genes for bHLH-ZIP
RT transcription factors TFEC and TFEB reveal a common gene organization for
RT all MiT subfamily members.";
RL Genomics 56:111-120(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBUNIT.
RX PubMed=7958932; DOI=10.1101/gad.8.22.2770;
RA Hemesath T.J., Steingrimsson E., McGill G., Hansen M.J., Vaught J.,
RA Hodgkinson C.A., Arnheiter H., Copeland N.G., Jenkins N.A., Fisher D.E.;
RT "microphthalmia, a critical factor in melanocyte development, defines a
RT discrete transcription factor family.";
RL Genes Dev. 8:2770-2780(1994).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9973413;
RA Rehli M., Lichanska A., Cassady A.I., Ostrowski M.C., Hume D.A.;
RT "TFEC is a macrophage-restricted member of the microphthalmia-TFE subfamily
RT of basic helix-loop-helix leucine zipper transcription factors.";
RL J. Immunol. 162:1559-1565(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH MITF.
RX PubMed=11818452;
RA Mansky K.C., Sulzbacher S., Purdom G., Nelsen L., Hume D.A., Rehli M.,
RA Ostrowski M.C.;
RT "The microphthalmia transcription factor and the related helix-loop-helix
RT zipper factors TFE-3 and TFE-C collaborate to activate the tartrate-
RT resistant acid phosphatase promoter.";
RL J. Leukoc. Biol. 71:304-310(2002).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=15459106; DOI=10.1242/dev.01300;
RA Rowan S., Chen C.-M.A., Young T.L., Fisher D.E., Cepko C.L.;
RT "Transdifferentiation of the retina into pigmented cells in ocular
RT retardation mice defines a new function of the homeodomain gene Chx10.";
RL Development 131:5139-5152(2004).
RN [8]
RP INDUCTION.
RX PubMed=15908341; DOI=10.4049/jimmunol.174.11.7111;
RA Rehli M., Sulzbacher S., Pape S., Ravasi T., Wells C.A., Heinz S.,
RA Sollner L., El Chartouni C., Krause S.W., Steingrimsson E., Hume D.A.,
RA Andreesen R.;
RT "Transcription factor Tfec contributes to the IL-4-inducible expression of
RT a small group of genes in mouse macrophages including the granulocyte
RT colony-stimulating factor receptor.";
RL J. Immunol. 174:7111-7122(2005).
CC -!- FUNCTION: Transcriptional regulator that acts as a repressor or an
CC activator. Acts as a transcriptional transactivator on the proximal
CC promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box
CC containing promoter. Collaborates with MITF in target gene activation.
CC Acts as a transcriptional repressor on minimal promoter containing
CC element F (that includes an E-box sequence) (By similarity). Binds to
CC element F in an E-box sequence-specific manner (By similarity). Acts as
CC a transcriptional repressor on minimal promoter containing mu E3
CC enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the
CC immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in
CC a homo- or heterodimeric form. {ECO:0000250,
CC ECO:0000269|PubMed:11818452}.
CC -!- SUBUNIT: Homodimer. Forms heterodimers with MITF. Interacts with MITF.
CC Forms heterodimers with TFE3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expressed in osteoclast-like cells (at protein
CC level). Expressed in cells of the mononuclear phagocyte lineage.
CC Expressed in macrophages and in osteoclast-like cells.
CC {ECO:0000269|PubMed:9973413}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the early developing retinal
CC pigmented epithelium and in the peripheral retina.
CC {ECO:0000269|PubMed:15459106}.
CC -!- INDUCTION: Up-regulated in bone marrow-derived macrophages by Th2
CC cytokines, IL-4, IL-13 and LPS. {ECO:0000269|PubMed:15908341}.
CC -!- DOMAIN: Contains an activation domain in the C-terminal region.
CC -!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF077742; AAD24426.1; -; mRNA.
DR EMBL; AK137141; BAE23248.1; -; mRNA.
DR EMBL; AK156327; BAE33676.1; -; mRNA.
DR EMBL; AK159579; BAE35199.1; -; mRNA.
DR EMBL; BC098494; AAH98494.1; -; mRNA.
DR CCDS; CCDS19920.1; -.
DR RefSeq; NP_112475.1; NM_031198.3.
DR AlphaFoldDB; Q9WTW4; -.
DR SMR; Q9WTW4; -.
DR BioGRID; 204017; 1.
DR STRING; 10090.ENSMUSP00000031533; -.
DR PhosphoSitePlus; Q9WTW4; -.
DR MaxQB; Q9WTW4; -.
DR PaxDb; Q9WTW4; -.
DR PeptideAtlas; Q9WTW4; -.
DR PRIDE; Q9WTW4; -.
DR ProteomicsDB; 262891; -.
DR Antibodypedia; 31571; 234 antibodies from 30 providers.
DR DNASU; 21426; -.
DR Ensembl; ENSMUST00000031533; ENSMUSP00000031533; ENSMUSG00000029553.
DR GeneID; 21426; -.
DR KEGG; mmu:21426; -.
DR UCSC; uc009aze.2; mouse.
DR CTD; 22797; -.
DR MGI; MGI:1333760; Tfec.
DR VEuPathDB; HostDB:ENSMUSG00000029553; -.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000159404; -.
DR HOGENOM; CLU_031638_0_0_1; -.
DR InParanoid; Q9WTW4; -.
DR OMA; ICPFGTD; -.
DR OrthoDB; 1211990at2759; -.
DR PhylomeDB; Q9WTW4; -.
DR TreeFam; TF317174; -.
DR BioGRID-ORCS; 21426; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tfec; mouse.
DR PRO; PR:Q9WTW4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9WTW4; protein.
DR Bgee; ENSMUSG00000029553; Expressed in epithelium of small intestine and 99 other tissues.
DR ExpressionAtlas; Q9WTW4; baseline and differential.
DR Genevisible; Q9WTW4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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:MGI.
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; 2.
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 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..317
FT /note="Transcription factor EC"
FT /id="PRO_0000313565"
FT DOMAIN 110..163
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..90
FT /note="Necessary for transcriptional transactivation"
FT /evidence="ECO:0000250"
FT REGION 242..317
FT /note="Necessary for transcriptional transactivation"
FT /evidence="ECO:0000250"
FT CONFLICT 170
FT /note="A -> V (in Ref. 2; BAE35199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35144 MW; 668F186489D63AA8 CRC64;
MTFDCRVCDQ TLKRAQPPAA SCMPLAEHEP MSPDSDAGCA GNPFTNLLAL GKKDGAEKWH
LSGSILDVYS DEQGISSANA GLTDAPCPSI LPMRKEIAET DGRALAKERQ KKDNHNLIER
RRRYNINYRI KELGTLIPKS NDPDMRWNKG TILKASVDYI KWLQKEQQRA RELEHRQKKL
EHANRQLRLR IQELEIQARA HGLPILASLG TADVGTHITK QQTHPERNLG GCCLQLTPTQ
GTSPEFYEQA VAFSDPLSHF TDLSFSAALK EEQRLDGMLL SDTICPFGTD PLLSAISPAV
SKASSRSSLS SEDGDEL
