InterPro : IPR001346

Name  Interferon regulatory factor DNA-binding domain Short Name  Interferon_reg_fact_DNA-bd_dom
Type  Domain Description  Viral infections induce the expression of type I interferons (IFN-alpha andIFN-beta) genes. The induction is due to the transcriptional activation of theIFN genes. Interferon regulatory factor I (IRF-1) is one of the transcriptionfactors responsible for that activation. IRF-1 binds to an upstream regulatorycis element, known as the interferon consensus sequence (ICS), which is foundin the promoters of type I IFN and IFN-inducible MHC class I genes. Interferonregulatory factor 2 (IRF-2) is a protein that also interacts with the ICS, butthat does not function as an activator; rather, it suppresses the function ofIRF-1 under certain circumstances [].These proteins share a highly conserved N-terminal domain of about 100 aminoacid residues which is involved in DNA-binding and which contain fiveconserved tryptophans. This domain is known as a 'tryptophan pentad repeat' ora 'tryptophan cluster' and is also present in:Interferon consensus sequence binding protein (ICSBP) [], a transcriptionfactor expressed predominantly in lymphoid tissues and induced by IFN-gammathat also binds to the ICS.Transcriptional regulator ISGF3 gamma subunit []. ISGF3 is responsible forthe initial stimulation of interferon-alpha-responsive genes. It recognisesand binds to the interferon-stimulated response element (ISRE) within theregulatory sequences of target genes.Interferon regulatory factor 3 (IRF-3).Interferon regulatory factor 4 (IRF-4) which binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter.Interferon regulatory factor 5 (IRF-5).Interferon regulatory factor 6 (IRF-6).Interferon regulatory factor 7 (IRF-7).Gamma Herpesviruses vIRF-1, -2 and -3, proteins with homology to thecellular transcription factors of the IRF family []. Neither vIRF-1 norvIRF-2 bind to DNA with the same specificity as cellular IRFs, indicatingthat if vIRFs are DNA-binding proteins, their binding has a patterndistinct from that of the cellular IRFs. Whether vIRF-3 can bind DNA withthe same specificity as cellular IRFs is not known.The IRF tryptophan pentad repeat DNA-binding domain has an alpha/betaarchitecture comprising a cluster of three alpha-helices (alpha1-alpha3)flanked on one side by a mixed four-stranded beta-sheet (beta1-beta4). It forms a helix-turn-helix motif that binds to ISRE consensussequences found in target promoters. Three of the tryptophan residues contactDNA by recognising a GAAA sequence [].This entry represents the IRF tryptophan pentad repeat DNA-bindingdomain.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR019817 Interferon regulatory factor, conserved site Interferon_reg_fac_CS Conserved_site

1 Found In

Id Name Short Name Type
IPR017431 Interferon regulatory factor-1/2 Interferon_reg_fac-1/2 Family

1 Parent Features

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain

5 Publications

First Author Title Year Journal Volume Pages
Taniguchi T Regulation of interferon-beta gene: structure and function of cis-elements and trans-acting factors. 1989 J Interferon Res 9 633-40
Veals SA Subunit of an alpha-interferon-responsive transcription factor is related to interferon regulatory factor and Myb families of DNA-binding proteins. 1992 Mol Cell Biol 12 3315-24
Escalante CR Structure of IRF-1 with bound DNA reveals determinants of interferon regulation. 1998 Nature 391 103-6
Driggers PH An interferon gamma-regulated protein that binds the interferon-inducible enhancer element of major histocompatibility complex class I genes. 1990 Proc Natl Acad Sci U S A 87 3743-7
Lubyova B Characterization of a novel human herpesvirus 8-encoded protein, vIRF-3, that shows homology to viral and cellular interferon regulatory factors. 2000 J Virol 74 8194-201



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)