IRF7_HUMAN
ID IRF7_HUMAN Reviewed; 503 AA.
AC Q92985; B9EGL3; O00331; O00332; O00333; O75924; Q9UE79;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Interferon regulatory factor 7;
DE Short=IRF-7;
GN Name=IRF7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT GLU-179.
RC TISSUE=Spleen;
RA Grossman A., Nicholl J., Antonio L., Luethy R., Suggs S., Sutherland G.R.,
RA Mak T.W.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RX PubMed=9315633; DOI=10.1128/mcb.17.10.5748;
RA Zhang L., Pagano J.S.;
RT "IRF-7, a new interferon regulatory factor associated with Epstein-Barr
RT virus latency.";
RL Mol. Cell. Biol. 17:5748-5757(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), AND VARIANTS GLU-179 AND ARG-412.
RX PubMed=9786932; DOI=10.1074/jbc.273.44.29210;
RA Au W.-C., Moore P.A., LaFleur D.W., Tombal B., Pitha P.M.;
RT "Characterization of the interferon regulatory factor-7 and its potential
RT role in the transcription activation of interferon A genes.";
RL J. Biol. Chem. 273:29210-29217(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
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 [6]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11073981; DOI=10.1128/mcb.20.23.8803-8814.2000;
RA Marie I.J., Smith E., Prakash A., Levy D.E.;
RT "Phosphorylation-induced dimerization of interferon regulatory factor 7
RT unmasks DNA binding and a bipartite transactivation domain.";
RL Mol. Cell. Biol. 20:8803-8814(2000).
RN [7]
RP INHIBITION OF PHOSPHORYLATION BY VACCINIA VIRUS PROTEIN E3.
RX PubMed=11124948; DOI=10.1074/jbc.m008717200;
RA Smith E.J., Marie I.J., Prakash A., Garcia-Sastre A., Levy D.E.;
RT "IRF3 and IRF7 phosphorylation in virus-infected cells does not require
RT double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is
RT blocked by Vaccinia virus E3L protein.";
RL J. Biol. Chem. 276:8951-8957(2001).
RN [8]
RP INTERACTION WITH HHV-8 PROTEIN VIRF1.
RX PubMed=11314014; DOI=10.1038/sj.onc.1204163;
RA Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A.,
RA Harrington W.J. Jr., Barber G.N., Hiscott J.;
RT "HHV-8 encoded vIRF-1 represses the interferon antiviral response by
RT blocking IRF-3 recruitment of the CBP/p300 coactivators.";
RL Oncogene 20:800-811(2001).
RN [9]
RP FUNCTION, ACETYLATION AT LYS-92, MUTAGENESIS OF GLY-90; LYS-92 AND THR-93,
RP AND PHOSPHORYLATION.
RX PubMed=12374802; DOI=10.1074/jbc.m207484200;
RA Caillaud A., Prakash A., Smith E., Masumi A., Hovanessian A.G., Levy D.E.,
RA Marie I.;
RT "Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein
RT (CBP)-associated factor (PCAF) impairs its DNA binding.";
RL J. Biol. Chem. 277:49417-49421(2002).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=11846980; DOI=10.1089/107999002753452700;
RA Zhang L., Pagano J.S.;
RT "Structure and function of IRF-7.";
RL J. Interferon Cytokine Res. 22:95-101(2002).
RN [11]
RP INTERACTION WITH HHV-8 PROTEIN ORF45 (MICROBIAL INFECTION).
RX PubMed=11943871; DOI=10.1073/pnas.082420599;
RA Zhu F.X., King S.M., Smith E.J., Levy D.E., Yuan Y.;
RT "A Kaposi's sarcoma-associated herpesviral protein inhibits virus-mediated
RT induction of type I interferon by blocking IRF-7 phosphorylation and
RT nuclear accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5573-5578(2002).
RN [12]
RP INTERACTION WITH TICAM2.
RX PubMed=14517278; DOI=10.1084/jem.20031023;
RA Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A.,
RA Latz E., Monks B., Pitha P.M., Golenbock D.T.;
RT "LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters
RT TRAM and TRIF.";
RL J. Exp. Med. 198:1043-1055(2003).
RN [13]
RP ERRATUM OF PUBMED:14517278.
RA Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A.,
RA Latz E., Monks B., Pitha P.M., Golenbock D.T.;
RL J. Exp. Med. 198:1451-1451(2003).
RN [14]
RP INTERACTION WITH TICAM1.
RX PubMed=14739303; DOI=10.1074/jbc.m311629200;
RA Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
RT "Mechanisms of the TRIF-induced interferon-stimulated response element and
RT NF-kappaB activation and apoptosis pathways.";
RL J. Biol. Chem. 279:15652-15661(2004).
RN [15]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [16]
RP PHOSPHORYLATION AT SER-477 AND SER-479 BY TBK1 AND IKKE, AND MUTAGENESIS OF
RP 477-SER--SER-479.
RX PubMed=15367631; DOI=10.1128/jvi.78.19.10636-10649.2004;
RA tenOever B.R., Sharma S., Zou W., Sun Q., Grandvaux N., Julkunen I.,
RA Hemmi H., Yamamoto M., Akira S., Yeh W.C., Lin R., Hiscott J.;
RT "Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus
RT infection and the role of viral ribonucleoprotein in the development of
RT interferon antiviral immunity.";
RL J. Virol. 78:10636-10649(2004).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MYD88.
RX PubMed=15492225; DOI=10.1073/pnas.0406933101;
RA Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N.,
RA Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.;
RT "Role of a transductional-transcriptional processor complex involving MyD88
RT and IRF-7 in Toll-like receptor signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYD88 AND TRAF6.
RX PubMed=15361868; DOI=10.1038/ni1118;
RA Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K.,
RA Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.;
RT "Interferon-alpha induction through Toll-like receptors involves a direct
RT interaction of IRF7 with MyD88 and TRAF6.";
RL Nat. Immunol. 5:1061-1068(2004).
RN [19]
RP PHOSPHORYLATION BY IRAK1.
RX PubMed=15767370; DOI=10.1084/jem.20042372;
RA Uematsu S., Sato S., Yamamoto M., Hirotani T., Kato H., Takeshita F.,
RA Matsuda M., Coban C., Ishii K.J., Kawai T., Takeuchi O., Akira S.;
RT "Interleukin-1 receptor-associated kinase-1 plays an essential role for
RT Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha}
RT induction.";
RL J. Exp. Med. 201:915-923(2005).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=16846591; DOI=10.1016/j.bcp.2006.06.002;
RA Solis M., Goubau D., Romieu-Mourez R., Genin P., Civas A., Hiscott J.;
RT "Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and
RT control of anti-tumor activity in primary macrophages.";
RL Biochem. Pharmacol. 72:1469-1476(2006).
RN [21]
RP REVIEW ON FUNCTION.
RX PubMed=16979567; DOI=10.1016/j.immuni.2006.08.009;
RA Honda K., Takaoka A., Taniguchi T.;
RT "Type I interferon gene induction by the interferon regulatory factor
RT family of transcription factors.";
RL Immunity 25:349-360(2006).
RN [22]
RP ERRATUM OF PUBMED:16979567.
RA Honda K., Takaoka A., Taniguchi T.;
RL Immunity 25:849-849(2006).
RN [23]
RP FUNCTION.
RX PubMed=17404045; DOI=10.1196/annals.1397.036;
RA Sgarbanti M., Marsili G., Remoli A.L., Orsatti R., Battistini A.;
RT "IRF-7: new role in the regulation of genes involved in adaptive
RT immunity.";
RL Ann. N. Y. Acad. Sci. 1095:325-333(2007).
RN [24]
RP INTERACTION WITH ROTAVIRUS A NSP1 (MICROBIAL INFECTION).
RX PubMed=17301153; DOI=10.1128/jvi.02498-06;
RA Barro M., Patton J.T.;
RT "Rotavirus NSP1 inhibits expression of type I interferon by antagonizing
RT the function of interferon regulatory factors IRF3, IRF5, and IRF7.";
RL J. Virol. 81:4473-4481(2007).
RN [25]
RP INTERACTION WITH EPSTEIN-BARR VIRUS/EBV LMP1 (MICROBIAL INFECTION).
RX PubMed=19017798; DOI=10.1073/pnas.0809933105;
RA Song Y.J., Izumi K.M., Shinners N.P., Gewurz B.E., Kieff E.;
RT "IRF7 activation by Epstein-Barr virus latent membrane protein 1 requires
RT localization at activation sites and TRAF6, but not TRAF2 or TRAF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18448-18453(2008).
RN [26]
RP INTERACTION WITH EPSTEIN-BARR VIRUS/EBV LF2 (MICROBIAL INFECTION).
RX PubMed=18987133; DOI=10.1128/jvi.00602-08;
RA Wu L., Fossum E., Joo C.H., Inn K.S., Shin Y.C., Johannsen E.,
RA Hutt-Fletcher L.M., Hass J., Jung J.U.;
RT "Epstein-Barr virus LF2: an antagonist to type I interferon.";
RL J. Virol. 83:1140-1146(2009).
RN [27]
RP INTERACTION WITH EBOLAVIRUS VP35 (MICROBIAL INFECTION).
RX PubMed=19557165; DOI=10.1371/journal.ppat.1000493;
RA Chang T.H., Kubota T., Matsuoka M., Jones S., Bradfute S.B., Bray M.,
RA Ozato K.;
RT "Ebola Zaire virus blocks type I interferon production by exploiting the
RT host SUMO modification machinery.";
RL PLoS Pathog. 5:e1000493-e1000493(2009).
RN [28]
RP REVIEW ON FUNCTION.
RX PubMed=20049431; DOI=10.1007/s00262-009-0804-6;
RA Savitsky D., Tamura T., Yanai H., Taniguchi T.;
RT "Regulation of immunity and oncogenesis by the IRF transcription factor
RT family.";
RL Cancer Immunol. Immunother. 59:489-510(2010).
RN [29]
RP UBIQUITINATION.
RX PubMed=21167755; DOI=10.1016/j.immuni.2010.11.027;
RA Yu Y., Hayward G.S.;
RT "The ubiquitin E3 ligase RAUL negatively regulates type i interferon
RT through ubiquitination of the transcription factors IRF7 and IRF3.";
RL Immunity 33:863-877(2010).
RN [30]
RP REVIEW ON FUNCTION.
RX PubMed=21490621; DOI=10.1038/gene.2011.21;
RA Ning S., Pagano J.S., Barber G.N.;
RT "IRF7: activation, regulation, modification and function.";
RL Genes Immun. 12:399-414(2011).
RN [31]
RP SUMOYLATION AT LYS-444 AND LYS-446 BY TRIM28.
RX PubMed=21940674; DOI=10.4049/jimmunol.1101704;
RA Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H.,
RA Rauscher F.J. III, Ozato K., Zhu F.;
RT "Tripartite motif-containing protein 28 is a small ubiquitin-related
RT modifier E3 ligase and negative regulator of IFN regulatory factor 7.";
RL J. Immunol. 187:4754-4763(2011).
RN [32]
RP INTERACTION WITH TRIM35, AND UBIQUITINATION.
RX PubMed=25907537; DOI=10.1016/j.febslet.2015.04.019;
RA Wang Y., Yan S., Yang B., Wang Y., Zhou H., Lian Q., Sun B.;
RT "TRIM35 negatively regulates TLR7- and TLR9-mediated type I interferon
RT production by targeting IRF7.";
RL FEBS Lett. 589:1322-1330(2015).
RN [33]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-167 AND
RP GLN-189.
RX PubMed=26608321; DOI=10.1128/jvi.02395-15;
RA Xiang Z., Liu L., Lei X., Zhou Z., He B., Wang J.;
RT "3C Protease of Enterovirus D68 Inhibits Cellular Defense Mediated by
RT Interferon Regulatory Factor 7.";
RL J. Virol. 90:1613-1621(2016).
RN [34]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ
RP (MICROBIAL INFECTION).
RX PubMed=28768861; DOI=10.1128/jvi.00853-17;
RA Narulla M.S., Alasiri A., Charmier L., Noonan S., Conroy D., Hall W.W.,
RA Sheehy N.;
RT "Positive and Negative Regulation of Type I Interferons by the Human T Cell
RT Leukemia Virus Antisense Protein HBZ.";
RL J. Virol. 91:0-0(2017).
RN [35]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-151;
RP GLN-167; GLN-185; GLN-188; GLN-189 AND GLN-215.
RX PubMed=23175366; DOI=10.1128/jvi.01855-12;
RA Lei X., Xiao X., Xue Q., Jin Q., He B., Wang J.;
RT "Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses
RT cellular responses.";
RL J. Virol. 87:1690-1698(2013).
RN [36]
RP INTERACTION WITH SENECA VALLEY VIRUS PROTEASE 3C (MICROBIAL INFECTION).
RX PubMed=29427864; DOI=10.1016/j.virol.2018.01.028;
RA Xue Q., Liu H., Zhu Z., Yang F., Ma L., Cai X., Xue Q., Zheng H.;
RT "Seneca Valley Virus 3Cpro abrogates the IRF3- and IRF7-mediated innate
RT immune response by degrading IRF3 and IRF7.";
RL Virology 518:1-7(2018).
RN [37]
RP INTERACTION WITH SFTSV VIRUS NSS (MICROBIAL INFECTION).
RX PubMed=30598516; DOI=10.4049/jimmunol.1800576;
RA Hong Y., Bai M., Qi X., Li C., Liang M., Li D., Cardona C.J., Xing Z.;
RT "Suppression of the IFN-alpha and -beta Induction through Sequestering IRF7
RT into Viral Inclusion Bodies by Nonstructural Protein NSs in Severe Fever
RT with Thrombocytopenia Syndrome Bunyavirus Infection.";
RL J. Immunol. 202:841-856(2019).
RN [38] {ECO:0007744|PDB:2O61}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 8-125 IN COMPLEX WITH IRF3 AND
RP DNA, SUBUNIT, AND FUNCTION.
RX PubMed=17574024; DOI=10.1016/j.cell.2007.05.019;
RA Panne D., Maniatis T., Harrison S.C.;
RT "An atomic model of the interferon-beta enhanceosome.";
RL Cell 129:1111-1123(2007).
RN [39]
RP INVOLVEMENT IN IMD39, VARIANT IMD39 VAL-410, AND CHARACTERIZATION OF
RP VARIANT IMD39 VAL-410.
RX PubMed=25814066; DOI=10.1126/science.aaa1578;
RA Ciancanelli M.J., Huang S.X., Luthra P., Garner H., Itan Y., Volpi S.,
RA Lafaille F.G., Trouillet C., Schmolke M., Albrecht R.A., Israelsson E.,
RA Lim H.K., Casadio M., Hermesh T., Lorenzo L., Leung L.W., Pedergnana V.,
RA Boisson B., Okada S., Picard C., Ringuier B., Troussier F., Chaussabel D.,
RA Abel L., Pellier I., Notarangelo L.D., Garcia-Sastre A., Basler C.F.,
RA Geissmann F., Zhang S.Y., Snoeck H.W., Casanova J.L.;
RT "Infectious disease. Life-threatening influenza and impaired interferon
RT amplification in human IRF7 deficiency.";
RL Science 348:448-453(2015).
RN [40]
RP VARIANTS HIS-37; SER-95; ASN-117; ARG-133; 185-GLN--ALA-503 DEL; LEU-214;
RP ALA-254; GLN-369; VAL-371; VAL-410; THR-419 AND 421-GLN--ALA-503 DEL,
RP CHARACTERIZATION OF VARIANTS HIS-37; SER-95; ASN-117; ARG-133;
RP 185-GLN--ALA-503 DEL; LEU-214; ALA-254; GLN-369; VAL-371; VAL-410; THR-419
RP AND 421-GLN--ALA-503 DEL, AND FUNCTION.
RX PubMed=32972995; DOI=10.1126/science.abd4570;
RG COVID-STORM Clinicians;
RG COVID Clinicians;
RG Imagine COVID Group;
RG French COVID Cohort Study Group;
RG CoV-Contact Cohort;
RG Amsterdam UMC Covid-19 Biobank;
RG COVID Human Genetic Effort;
RG NIAID-USUHS/TAGC COVID Immunity Group;
RA Zhang Q., Bastard P., Liu Z., Le Pen J., Moncada-Velez M., Chen J.,
RA Ogishi M., Sabli I.K.D., Hodeib S., Korol C., Rosain J., Bilguvar K.,
RA Ye J., Bolze A., Bigio B., Yang R., Arias A.A., Zhou Q., Zhang Y.,
RA Onodi F., Korniotis S., Karpf L., Philippot Q., Chbihi M., Bonnet-Madin L.,
RA Dorgham K., Smith N., Schneider W.M., Razooky B.S., Hoffmann H.H.,
RA Michailidis E., Moens L., Han J.E., Lorenzo L., Bizien L., Meade P.,
RA Neehus A.L., Ugurbil A.C., Corneau A., Kerner G., Zhang P., Rapaport F.,
RA Seeleuthner Y., Manry J., Masson C., Schmitt Y., Schlueter A., Le Voyer T.,
RA Khan T., Li J., Fellay J., Roussel L., Shahrooei M., Alosaimi M.F.,
RA Mansouri D., Al-Saud H., Al-Mulla F., Almourfi F., Al-Muhsen S.Z.,
RA Alsohime F., Al Turki S., Hasanato R., van de Beek D., Biondi A.,
RA Bettini L.R., D'Angio' M., Bonfanti P., Imberti L., Sottini A., Paghera S.,
RA Quiros-Roldan E., Rossi C., Oler A.J., Tompkins M.F., Alba C.,
RA Vandernoot I., Goffard J.C., Smits G., Migeotte I., Haerynck F.,
RA Soler-Palacin P., Martin-Nalda A., Colobran R., Morange P.E., Keles S.,
RA Coelkesen F., Ozcelik T., Yasar K.K., Senoglu S., Karabela S.N.,
RA Rodriguez-Gallego C., Novelli G., Hraiech S., Tandjaoui-Lambiotte Y.,
RA Duval X., Laouenan C., Snow A.L., Dalgard C.L., Milner J.D., Vinh D.C.,
RA Mogensen T.H., Marr N., Spaan A.N., Boisson B., Boisson-Dupuis S.,
RA Bustamante J., Puel A., Ciancanelli M.J., Meyts I., Maniatis T.,
RA Soumelis V., Amara A., Nussenzweig M., Garcia-Sastre A., Krammer F.,
RA Pujol A., Duffy D., Lifton R.P., Zhang S.Y., Gorochov G., Beziat V.,
RA Jouanguy E., Sancho-Shimizu V., Rice C.M., Abel L., Notarangelo L.D.,
RA Cobat A., Su H.C., Casanova J.L.;
RT "Inborn errors of type I IFN immunity in patients with life-threatening
RT COVID-19.";
RL Science 370:0-0(2020).
CC -!- FUNCTION: Key transcriptional regulator of type I interferon (IFN)-
CC dependent immune responses and plays a critical role in the innate
CC immune response against DNA and RNA viruses. Regulates the
CC transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-
CC stimulated genes (ISG) by binding to an interferon-stimulated response
CC element (ISRE) in their promoters (PubMed:17574024, PubMed:32972995).
CC Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha
CC (IFNA) genes and mediate their induction via both the virus-activated,
CC MyD88-independent pathway and the TLR-activated, MyD88-dependent
CC pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in
CC response to lipopolysaccharide (LPS) or viral infection in a type I
CC IFN-dependent manner (By similarity). Required during both the early
CC and late phases of the IFN gene induction but is more critical for the
CC late than for the early phase. Exists in an inactive form in the
CC cytoplasm of uninfected cells and following viral infection, double-
CC stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes
CC phosphorylated by IKBKE and TBK1 kinases. This induces a conformational
CC change, leading to its dimerization and nuclear localization where
CC along with other coactivators it can activate transcription of the type
CC I IFN and ISG genes. Can also play a role in regulating adaptive immune
CC responses by inducing PSMB9/LMP2 expression, either directly or through
CC induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen
CC 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can
CC activate distinct gene expression programs in macrophages and regulate
CC the anti-tumor properties of primary macrophages (By similarity)
CC (PubMed:11073981, PubMed:12374802, PubMed:15361868, PubMed:17404045).
CC {ECO:0000250|UniProtKB:P70434, ECO:0000269|PubMed:11073981,
CC ECO:0000269|PubMed:12374802, ECO:0000269|PubMed:15361868,
CC ECO:0000269|PubMed:17404045, ECO:0000269|PubMed:17574024,
CC ECO:0000269|PubMed:32972995}.
CC -!- ACTIVITY REGULATION: In the absence of viral infection, maintained as a
CC monomer in an autoinhibited state and phosphorylation disrupts this
CC autoinhibition leading to the liberation of the DNA-binding and
CC dimerization activities and its nuclear localization where it can
CC activate type I IFN and ISG genes.
CC -!- SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Heterodimer with
CC IRF3 (PubMed:17574024). Interacts with TICAM1 and TICAM2. Interacts
CC with MYD88 and TRAF6. Interacts with TRIM35 (PubMed:25907537,
CC PubMed:11073981, PubMed:11314014, PubMed:14517278, PubMed:14739303,
CC PubMed:15361868, PubMed:15492225). Interacts with NMI; the interaction
CC is direct and leads to the inhibition of IRF7-mediated type I IFN
CC production (By similarity). {ECO:0000250|UniProtKB:P70434,
CC ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:11314014,
CC ECO:0000269|PubMed:14517278, ECO:0000269|PubMed:14739303,
CC ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15492225,
CC ECO:0000269|PubMed:17574024, ECO:0000269|PubMed:25907537}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus LF2
CC and LMP1. {ECO:0000269|PubMed:18987133, ECO:0000269|PubMed:19017798}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A NSP1; this
CC interaction leads to the proteasome-dependent degradation of IRF7.
CC {ECO:0000269|PubMed:17301153}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 8/HHV-
CC 8 proteins ORF45 and vIRF-1. {ECO:0000269|PubMed:11943871}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
CC virus 1/HTLV-1 protein HBZ. {ECO:0000269|PubMed:28768861}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Seneca Valley virus
CC protease 3C; this interaction is involved in the suppression of IRF7
CC expression and phosphorylation by the virus.
CC {ECO:0000269|PubMed:29427864}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus VP35; this
CC interaction mediates the sumoylation of IRF7 and contributes to the
CC viral inhibition of IFN-type I production.
CC {ECO:0000269|PubMed:19557165}.
CC -!- SUBUNIT: (Microbial infection) Interacts with severe fever with
CC thrombocytopenia syndrome virus (SFTSV) NSs; this interaction
CC sequesters IRF7 in NSs-induced cytoplasmic inclusion bodies.
CC {ECO:0000269|PubMed:30598516}.
CC -!- INTERACTION:
CC Q92985; O00170: AIP; NbExp=2; IntAct=EBI-968267, EBI-704197;
CC Q92985; P10398: ARAF; NbExp=2; IntAct=EBI-968267, EBI-365961;
CC Q92985; Q96A33: CCDC47; NbExp=2; IntAct=EBI-968267, EBI-720151;
CC Q92985; O15111: CHUK; NbExp=4; IntAct=EBI-968267, EBI-81249;
CC Q92985; P51617: IRAK1; NbExp=2; IntAct=EBI-968267, EBI-358664;
CC Q92985; O94822: LTN1; NbExp=2; IntAct=EBI-968267, EBI-1044684;
CC Q92985; Q9ULE6: PALD1; NbExp=2; IntAct=EBI-968267, EBI-3957166;
CC Q92985; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-968267, EBI-356402;
CC Q92985; Q86UE8: TLK2; NbExp=2; IntAct=EBI-968267, EBI-1047967;
CC Q92985; Q9BVS5: TRMT61B; NbExp=3; IntAct=EBI-968267, EBI-3197877;
CC Q92985; P29128: BICP0; Xeno; NbExp=5; IntAct=EBI-968267, EBI-11292028;
CC Q92985; F5HDE4: ORF45; Xeno; NbExp=3; IntAct=EBI-968267, EBI-8843990;
CC Q92985; Q77M19: P; Xeno; NbExp=3; IntAct=EBI-968267, EBI-6149376;
CC Q92985-1; P03230: LMP1; Xeno; NbExp=5; IntAct=EBI-8850881, EBI-6973030;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The phosphorylated and
CC active form accumulates selectively in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q92985-1; Sequence=Displayed;
CC Name=B; Synonyms=Beta;
CC IsoId=Q92985-2; Sequence=VSP_002760;
CC Name=C; Synonyms=Gamma;
CC IsoId=Q92985-3; Sequence=VSP_002758, VSP_002759;
CC Name=D; Synonyms=H;
CC IsoId=Q92985-4; Sequence=VSP_002757;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in spleen, thymus and
CC peripheral blood leukocytes.
CC -!- INDUCTION: By type I interferon (IFN) and viruses.
CC -!- PTM: Acetylation inhibits its DNA-binding ability and activity.
CC {ECO:0000269|PubMed:12374802}.
CC -!- PTM: In response to a viral infection, phosphorylated on Ser-477 and
CC Ser-479 by TBK1 and IKBKE1. Phosphorylation, and subsequent activation
CC is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated
CC signaling pathway, phosphorylated by IRAK1.
CC {ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802,
CC ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15767370}.
CC -!- PTM: TRAF6-mediated ubiquitination is required for IRF7 activation (By
CC similarity). TRIM35 mediates IRF7 'Lys-48'-linked polyubiquitination
CC and subsequent proteasomal degradation (PubMed:25907537). Ubiquitinated
CC by UBE3C, leading to its degradation (PubMed:21167755).
CC {ECO:0000250|UniProtKB:P70434, ECO:0000269|PubMed:21167755,
CC ECO:0000269|PubMed:25907537}.
CC -!- PTM: Sumoylated by TRIM28, which inhibits its transactivation activity.
CC {ECO:0000269|PubMed:21940674}.
CC -!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C
CC of enterovirus 71 allowing the virus to disrupt the host type I
CC interferon production. {ECO:0000269|PubMed:23175366}.
CC -!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C
CC of human enterovirus 68D (EV68) allowing the virus to disrupt the host
CC type I interferon production. {ECO:0000269|PubMed:26608321}.
CC -!- PTM: 'Lys-48'-linked polyubiquitination and subsequent proteasomal
CC degradation is NMI-dependent in response to Sendai virus infection.
CC {ECO:0000250|UniProtKB:P70434}.
CC -!- DISEASE: Immunodeficiency 39 (IMD39) [MIM:616345]: A primary
CC immunodeficiency causing severe, life-threatening acute respiratory
CC distress upon infection with H1N1 influenza A.
CC {ECO:0000269|PubMed:25814066}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform C]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; U73036; AAB17190.1; -; mRNA.
DR EMBL; U53830; AAB80686.1; -; mRNA.
DR EMBL; U53831; AAB80688.1; -; mRNA.
DR EMBL; U53832; AAB80690.1; -; mRNA.
DR EMBL; U53832; AAB80691.1; -; mRNA.
DR EMBL; AF076494; AAC70999.1; -; mRNA.
DR EMBL; CH471158; EAX02360.1; -; Genomic_DNA.
DR EMBL; BC136555; AAI36556.1; -; mRNA.
DR CCDS; CCDS7703.1; -. [Q92985-1]
DR CCDS; CCDS7704.1; -. [Q92985-2]
DR CCDS; CCDS7705.1; -. [Q92985-4]
DR RefSeq; NP_001563.2; NM_001572.3. [Q92985-1]
DR RefSeq; NP_004020.1; NM_004029.2. [Q92985-2]
DR RefSeq; NP_004022.2; NM_004031.2. [Q92985-4]
DR RefSeq; XP_005252963.1; XM_005252906.3.
DR RefSeq; XP_016873163.1; XM_017017674.1.
DR PDB; 2O61; X-ray; 2.80 A; A=8-125.
DR PDBsum; 2O61; -.
DR AlphaFoldDB; Q92985; -.
DR SMR; Q92985; -.
DR BioGRID; 109873; 80.
DR DIP; DIP-34895N; -.
DR IntAct; Q92985; 58.
DR MINT; Q92985; -.
DR STRING; 9606.ENSP00000380697; -.
DR iPTMnet; Q92985; -.
DR PhosphoSitePlus; Q92985; -.
DR BioMuta; IRF7; -.
DR DMDM; 116242593; -.
DR EPD; Q92985; -.
DR MassIVE; Q92985; -.
DR MaxQB; Q92985; -.
DR PaxDb; Q92985; -.
DR PeptideAtlas; Q92985; -.
DR PRIDE; Q92985; -.
DR ProteomicsDB; 75643; -. [Q92985-1]
DR ProteomicsDB; 75644; -. [Q92985-2]
DR ProteomicsDB; 75645; -. [Q92985-3]
DR ProteomicsDB; 75646; -. [Q92985-4]
DR Antibodypedia; 4325; 617 antibodies from 41 providers.
DR DNASU; 3665; -.
DR Ensembl; ENST00000330243.9; ENSP00000329411.5; ENSG00000185507.21. [Q92985-4]
DR Ensembl; ENST00000348655.11; ENSP00000331803.9; ENSG00000185507.21. [Q92985-2]
DR Ensembl; ENST00000397566.5; ENSP00000380697.1; ENSG00000185507.21. [Q92985-4]
DR Ensembl; ENST00000469048.6; ENSP00000434607.1; ENSG00000185507.21. [Q92985-3]
DR Ensembl; ENST00000525445.6; ENSP00000434009.2; ENSG00000185507.21. [Q92985-1]
DR Ensembl; ENST00000533182.5; ENSP00000433903.1; ENSG00000185507.21. [Q92985-3]
DR Ensembl; ENST00000612534.4; ENSP00000479615.1; ENSG00000276561.4. [Q92985-4]
DR Ensembl; ENST00000621391.4; ENSP00000480358.1; ENSG00000276561.4. [Q92985-1]
DR Ensembl; ENST00000632827.1; ENSP00000488039.1; ENSG00000276561.4. [Q92985-4]
DR Ensembl; ENST00000633274.1; ENSP00000488591.1; ENSG00000276561.4. [Q92985-3]
DR Ensembl; ENST00000633943.1; ENSP00000488666.1; ENSG00000276561.4. [Q92985-2]
DR Ensembl; ENST00000634105.1; ENSP00000488581.1; ENSG00000276561.4. [Q92985-3]
DR GeneID; 3665; -.
DR KEGG; hsa:3665; -.
DR MANE-Select; ENST00000525445.6; ENSP00000434009.2; NM_001572.5; NP_001563.2.
DR UCSC; uc001lqg.3; human. [Q92985-1]
DR CTD; 3665; -.
DR DisGeNET; 3665; -.
DR GeneCards; IRF7; -.
DR HGNC; HGNC:6122; IRF7.
DR HPA; ENSG00000185507; Tissue enhanced (liver, lymphoid tissue).
DR MalaCards; IRF7; -.
DR MIM; 605047; gene.
DR MIM; 616345; phenotype.
DR neXtProt; NX_Q92985; -.
DR OpenTargets; ENSG00000185507; -.
DR Orphanet; 574918; Predisposition to severe viral infection due to IRF7 deficiency.
DR PharmGKB; PA29921; -.
DR VEuPathDB; HostDB:ENSG00000185507; -.
DR eggNOG; ENOG502R2I9; Eukaryota.
DR GeneTree; ENSGT00940000160931; -.
DR HOGENOM; CLU_031544_2_0_1; -.
DR InParanoid; Q92985; -.
DR OMA; QCNALEP; -.
DR OrthoDB; 648909at2759; -.
DR PhylomeDB; Q92985; -.
DR TreeFam; TF328512; -.
DR PathwayCommons; Q92985; -.
DR Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR SignaLink; Q92985; -.
DR SIGNOR; Q92985; -.
DR BioGRID-ORCS; 3665; 14 hits in 1104 CRISPR screens.
DR ChiTaRS; IRF7; human.
DR GeneWiki; IRF7; -.
DR GenomeRNAi; 3665; -.
DR Pharos; Q92985; Tbio.
DR PRO; PR:Q92985; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92985; protein.
DR Bgee; ENSG00000185507; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; Q92985; baseline and differential.
DR Genevisible; Q92985; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0019043; P:establishment of viral latency; TAS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0039530; P:MDA-5 signaling pathway; TAS:UniProtKB.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002819; P:regulation of adaptive immune response; IDA:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; TAS:UniProtKB.
DR GO; GO:0045655; P:regulation of monocyte differentiation; TAS:UniProtKB.
DR GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0034127; P:regulation of MyD88-independent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032479; P:regulation of type I interferon production; TAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:UniProtKB.
DR GO; GO:0060337; P:type I interferon signaling pathway; IEA:Ensembl.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR IDEAL; IID00491; -.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR019471; Interferon_reg_factor-3.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SMART; SM01243; IRF-3; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Antiviral defense; Cytoplasm; Disease variant; DNA-binding;
KW Host-virus interaction; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..503
FT /note="Interferon regulatory factor 7"
FT /id="PRO_0000154562"
FT DNA_BIND 11..126
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 69..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..456
FT /note="Necessary for the interaction with NMI"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT SITE 167..168
FT /note="(Microbial infection) Cleavage; by viral EV68
FT protease 3C"
FT /evidence="ECO:0000269|PubMed:26608321"
FT SITE 189..190
FT /note="(Microbial infection) Cleavage; by viral EV 71
FT protease 3C and EV68 protease 3C"
FT /evidence="ECO:0000269|PubMed:23175366,
FT ECO:0000269|PubMed:26608321"
FT MOD_RES 92
FT /note="N6-acetyllysine; by KAT2A and KAT2B"
FT /evidence="ECO:0000269|PubMed:12374802"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT MOD_RES 477
FT /note="Phosphoserine; by TBK1 and IKKE"
FT /evidence="ECO:0000269|PubMed:15367631"
FT MOD_RES 479
FT /note="Phosphoserine; by TBK1 and IKKE"
FT /evidence="ECO:0000269|PubMed:15367631"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70434"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 1..6
FT /note="MALAPE -> MPVPERPAAGPDSPRPGTR (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9786932"
FT /id="VSP_002757"
FT VAR_SEQ 152..164
FT /note="GGPPGPFLAHTHA -> AQGSLLGSCTGGQ (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9315633"
FT /id="VSP_002758"
FT VAR_SEQ 165..503
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9315633"
FT /id="VSP_002759"
FT VAR_SEQ 228..256
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9315633"
FT /id="VSP_002760"
FT VARIANT 37
FT /note="R -> H (no effect on IFNB induction upon Sendai
FT virus infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084074"
FT VARIANT 95
FT /note="F -> S (abolished IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084075"
FT VARIANT 117
FT /note="D -> N (abolished IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084076"
FT VARIANT 133
FT /note="G -> R (no effect on IFNB induction upon Sendai
FT virus infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084077"
FT VARIANT 179
FT /note="K -> E (in dbSNP:rs1061502)"
FT /evidence="ECO:0000269|PubMed:9786932, ECO:0000269|Ref.1"
FT /id="VAR_027957"
FT VARIANT 185..503
FT /note="Missing (abolishes IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084078"
FT VARIANT 204
FT /note="D -> N (in dbSNP:rs41313489)"
FT /id="VAR_061273"
FT VARIANT 214
FT /note="G -> L (requires 2 nucleotide substitutions; no
FT effect on IFNB induction upon Sendai virus infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084079"
FT VARIANT 254
FT /note="T -> A (no effect IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084080"
FT VARIANT 369
FT /note="R -> Q (no effect on IFNB induction upon Sendai
FT virus infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084081"
FT VARIANT 371
FT /note="M -> V (decreased IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084082"
FT VARIANT 410
FT /note="F -> V (in IMD39; loss of function mutation; shows
FT abnormal localization to the cytoplasm rather than the
FT nucleus; abolished IFNB induction upon Sendai virus
FT infection; dbSNP:rs786205223)"
FT /evidence="ECO:0000269|PubMed:25814066,
FT ECO:0000269|PubMed:32972995"
FT /id="VAR_073779"
FT VARIANT 412
FT /note="Q -> R (in dbSNP:rs1131665)"
FT /evidence="ECO:0000269|PubMed:9786932"
FT /id="VAR_034017"
FT VARIANT 419
FT /note="A -> T (no effect on IFNB induction upon Sendai
FT virus infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084083"
FT VARIANT 421..503
FT /note="Missing (abolished IFNB induction upon Sendai virus
FT infection)"
FT /evidence="ECO:0000269|PubMed:32972995"
FT /id="VAR_084084"
FT MUTAGEN 90
FT /note="G->T: Loss of acetylation, increased DNA-binding and
FT activity; when associated with R-93."
FT /evidence="ECO:0000269|PubMed:12374802"
FT MUTAGEN 92
FT /note="K->R: Loss of acetylation, DNA-binding and
FT activity."
FT /evidence="ECO:0000269|PubMed:12374802"
FT MUTAGEN 93
FT /note="T->R: Loss of acetylation, increased DNA-binding and
FT activity; when associated with T-90."
FT /evidence="ECO:0000269|PubMed:12374802"
FT MUTAGEN 151
FT /note="Q->A: No effect on cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 167
FT /note="Q->A: Complete loss of inactivation of IFN-I
FT production; when associated with R-189."
FT /evidence="ECO:0000269|PubMed:26608321"
FT MUTAGEN 167
FT /note="Q->A: No effect on cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 185
FT /note="Q->A: No effect on cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 188
FT /note="Q->A: No effect on cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 189
FT /note="Q->A: Complete loss of cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 189
FT /note="Q->R: Complete loss of inactivation of IFN-I
FT production; when associated with A-167."
FT /evidence="ECO:0000269|PubMed:26608321"
FT MUTAGEN 215
FT /note="Q->A: No effect on cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:23175366"
FT MUTAGEN 477..479
FT /note="SLS->ALA: Complete loss of TBK1 and IKKE
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:15367631"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2O61"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2O61"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:2O61"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2O61"
SQ SEQUENCE 503 AA; 54278 MW; 9863C147514652DE CRC64;
MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK DLSEADARIF
KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR STRRFVMLRD NSGDPADPHK
VYALSRELCW REGPGTDQTE AEAPAAVPPP QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG
DLLLQAVQQS CLADHLLTAS WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV
ETTPSPGPQP AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV
LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL RHVAPGLHLE
LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC DTPIFDFRVF FQELVEFRAR
QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL VKLEPWLCRV HLEGTQREGV SSLDSSSLSL
CLSSANSLYD DIECFLMELE QPA
