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Protein

Transcription factor EC

Gene

Tfec

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter. Collaborates with MITF in target gene activation. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence) (By similarity). Binds to element F in an E-box sequence-specific manner (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor EC
Short name:
TFE-C
Short name:
mTFEC
Gene namesi
Name:Tfec
Synonyms:Tcfec
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1333760. Tfec.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Transcription factor ECPRO_0000313565Add
BLAST

Proteomic databases

EPDiQ9WTW4.
PaxDbiQ9WTW4.
PRIDEiQ9WTW4.

PTM databases

PhosphoSiteiQ9WTW4.

Expressioni

Tissue specificityi

Expressed in osteoclast-like cells (at protein level). Expressed in cells of the mononuclear phagocyte lineage. Expressed in macrophages and in osteoclast-like cells.1 Publication

Developmental stagei

Expressed in the early developing retinal pigmented epithelium and in the peripheral retina.1 Publication

Inductioni

Up-regulated in bone marrow-derived macrophages by Th2 cytokines, IL-4, IL-13 and LPS.1 Publication

Gene expression databases

BgeeiQ9WTW4.
CleanExiMM_TCFEC.
ExpressionAtlasiQ9WTW4. baseline and differential.
GenevisibleiQ9WTW4. MM.

Interactioni

Subunit structurei

Homodimer. Forms heterodimers with MITF. Interacts with MITF. Forms heterodimers with TFE3 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031533.

Structurei

3D structure databases

ProteinModelPortaliQ9WTW4.
SMRiQ9WTW4. Positions 111-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 16354bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9090Necessary for transcriptional transactivationBy similarityAdd
BLAST
Regioni242 – 31776Necessary for transcriptional transactivationBy similarityAdd
BLAST

Domaini

Contains an activation domain in the C-terminal region.

Sequence similaritiesi

Belongs to the MiT/TFE family.Curated
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1318. Eukaryota.
ENOG4110SME. LUCA.
GeneTreeiENSGT00390000004402.
HOGENOMiHOG000231368.
HOVERGENiHBG006768.
InParanoidiQ9WTW4.
KOiK15591.
OMAiTKQQTHL.
OrthoDBiEOG72G182.
PhylomeDBiQ9WTW4.
TreeFamiTF317174.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR021802. MiT/TFE_C.
IPR024101. TFEC.
[Graphical view]
PANTHERiPTHR12565:SF106. PTHR12565:SF106. 1 hit.
PfamiPF11851. DUF3371. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WTW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFDCRVCDQ TLKRAQPPAA SCMPLAEHEP MSPDSDAGCA GNPFTNLLAL
60 70 80 90 100
GKKDGAEKWH LSGSILDVYS DEQGISSANA GLTDAPCPSI LPMRKEIAET
110 120 130 140 150
DGRALAKERQ KKDNHNLIER RRRYNINYRI KELGTLIPKS NDPDMRWNKG
160 170 180 190 200
TILKASVDYI KWLQKEQQRA RELEHRQKKL EHANRQLRLR IQELEIQARA
210 220 230 240 250
HGLPILASLG TADVGTHITK QQTHPERNLG GCCLQLTPTQ GTSPEFYEQA
260 270 280 290 300
VAFSDPLSHF TDLSFSAALK EEQRLDGMLL SDTICPFGTD PLLSAISPAV
310
SKASSRSSLS SEDGDEL
Length:317
Mass (Da):35,144
Last modified:November 1, 1999 - v1
Checksum:i668F186489D63AA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701A → V in BAE35199 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077742 mRNA. Translation: AAD24426.1.
AK137141 mRNA. Translation: BAE23248.1.
AK156327 mRNA. Translation: BAE33676.1.
AK159579 mRNA. Translation: BAE35199.1.
BC098494 mRNA. Translation: AAH98494.1.
CCDSiCCDS19920.1.
RefSeqiNP_112475.1. NM_031198.3.
UniGeneiMm.36217.

Genome annotation databases

EnsembliENSMUST00000031533; ENSMUSP00000031533; ENSMUSG00000029553.
GeneIDi21426.
KEGGimmu:21426.
UCSCiuc009aze.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077742 mRNA. Translation: AAD24426.1.
AK137141 mRNA. Translation: BAE23248.1.
AK156327 mRNA. Translation: BAE33676.1.
AK159579 mRNA. Translation: BAE35199.1.
BC098494 mRNA. Translation: AAH98494.1.
CCDSiCCDS19920.1.
RefSeqiNP_112475.1. NM_031198.3.
UniGeneiMm.36217.

3D structure databases

ProteinModelPortaliQ9WTW4.
SMRiQ9WTW4. Positions 111-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031533.

PTM databases

PhosphoSiteiQ9WTW4.

Proteomic databases

EPDiQ9WTW4.
PaxDbiQ9WTW4.
PRIDEiQ9WTW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031533; ENSMUSP00000031533; ENSMUSG00000029553.
GeneIDi21426.
KEGGimmu:21426.
UCSCiuc009aze.2. mouse.

Organism-specific databases

CTDi22797.
MGIiMGI:1333760. Tfec.

Phylogenomic databases

eggNOGiKOG1318. Eukaryota.
ENOG4110SME. LUCA.
GeneTreeiENSGT00390000004402.
HOGENOMiHOG000231368.
HOVERGENiHBG006768.
InParanoidiQ9WTW4.
KOiK15591.
OMAiTKQQTHL.
OrthoDBiEOG72G182.
PhylomeDBiQ9WTW4.
TreeFamiTF317174.

Miscellaneous databases

PROiQ9WTW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTW4.
CleanExiMM_TCFEC.
ExpressionAtlasiQ9WTW4. baseline and differential.
GenevisibleiQ9WTW4. MM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR021802. MiT/TFE_C.
IPR024101. TFEC.
[Graphical view]
PANTHERiPTHR12565:SF106. PTHR12565:SF106. 1 hit.
PfamiPF11851. DUF3371. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the murine genes for bHLH-ZIP transcription factors TFEC and TFEB reveal a common gene organization for all MiT subfamily members."
    Rehli M., Den Elzen N., Cassady A.I., Ostrowski M.C., Hume D.A.
    Genomics 56:111-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen and Urinary bladder.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  4. "microphthalmia, a critical factor in melanocyte development, defines a discrete transcription factor family."
    Hemesath T.J., Steingrimsson E., McGill G., Hansen M.J., Vaught J., Hodgkinson C.A., Arnheiter H., Copeland N.G., Jenkins N.A., Fisher D.E.
    Genes Dev. 8:2770-2780(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  5. "TFEC is a macrophage-restricted member of the microphthalmia-TFE subfamily of basic helix-loop-helix leucine zipper transcription factors."
    Rehli M., Lichanska A., Cassady A.I., Ostrowski M.C., Hume D.A.
    J. Immunol. 162:1559-1565(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "The microphthalmia transcription factor and the related helix-loop-helix zipper factors TFE-3 and TFE-C collaborate to activate the tartrate-resistant acid phosphatase promoter."
    Mansky K.C., Sulzbacher S., Purdom G., Nelsen L., Hume D.A., Rehli M., Ostrowski M.C.
    J. Leukoc. Biol. 71:304-310(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MITF.
  7. "Transdifferentiation of the retina into pigmented cells in ocular retardation mice defines a new function of the homeodomain gene Chx10."
    Rowan S., Chen C.-M.A., Young T.L., Fisher D.E., Cepko C.L.
    Development 131:5139-5152(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Transcription factor Tfec contributes to the IL-4-inducible expression of a small group of genes in mouse macrophages including the granulocyte colony-stimulating factor receptor."
    Rehli M., Sulzbacher S., Pape S., Ravasi T., Wells C.A., Heinz S., Sollner L., El Chartouni C., Krause S.W., Steingrimsson E., Hume D.A., Andreesen R.
    J. Immunol. 174:7111-7122(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiTFEC_MOUSE
AccessioniPrimary (citable) accession number: Q9WTW4
Secondary accession number(s): Q3TWR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.