ID MAVS_HUMAN Reviewed; 540 AA.
AC Q7Z434; A8K6X0; B2BD33; B2BD34; F5H6C8; M1P2Z0; Q2HWT5; Q3I0Y2; Q5T7I6;
AC Q86VY7; Q9H1H3; Q9H4Y1; Q9H8D3; Q9ULE9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Mitochondrial antiviral-signaling protein {ECO:0000305};
DE Short=MAVS {ECO:0000305};
DE AltName: Full=CARD adapter inducing interferon beta {ECO:0000303|PubMed:16177806};
DE Short=Cardif {ECO:0000303|PubMed:16177806};
DE AltName: Full=Interferon beta promoter stimulator protein 1;
DE Short=IPS-1;
DE AltName: Full=Putative NF-kappa-B-activating protein 031N;
DE AltName: Full=Virus-induced-signaling adapter;
DE Short=VISA;
GN Name=MAVS {ECO:0000303|PubMed:16125763, ECO:0000312|HGNC:HGNC:29233};
GN Synonyms=IPS1, KIAA1271, VISA;
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 1), FUNCTION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF THR-54 AND 67-GLY--VAL-69, INTERACTION WITH RIGI AND TRAF6,
RP SUBCELLULAR LOCATION, AND VARIANTS LYS-198 AND PHE-409.
RX PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
RA Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
RT "Identification and characterization of MAVS, a mitochondrial antiviral
RT signaling protein that activates NF-kappaB and IRF 3.";
RL Cell 122:669-682(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH RIGI;
RP IRF3; TRAF2 AND TRAF6, MUTAGENESIS OF GLN-145; GLU-155 AND GLU-457,
RP FUNCTION, AND VARIANT GLU-93.
RX PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
RA Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
RT "VISA is an adapter protein required for virus-triggered IFN-beta
RT Signaling.";
RL Mol. Cell 19:727-740(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RIGI; IKBKE; CHUK
RP AND IKBKB, FUNCTION, MUTAGENESIS OF CYS-508, VARIANTS LYS-198 AND PHE-409,
RP INTERACTION WITH HCV NS3/4A PROTEASE (MICROBIAL INFECTION), AND PROTEOLYTIC
RP CLEAVAGE (MICROBIAL INFECTION).
RX PubMed=16177806; DOI=10.1038/nature04193;
RA Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
RA Bartenschlager R., Tschopp J.;
RT "Cardif is an adaptor protein in the RIG-I antiviral pathway and is
RT targeted by hepatitis C virus.";
RL Nature 437:1167-1172(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH RIGI; IFIH1/MDA5; FADD AND RIPK1, FUNCTION, AND VARIANT GLU-93.
RX PubMed=16127453; DOI=10.1038/ni1243;
RA Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J.,
RA Takeuchi O., Akira S.;
RT "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon
RT induction.";
RL Nat. Immunol. 6:981-988(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RX PubMed=18207245; DOI=10.1016/j.molimm.2007.11.018;
RA Lad S.P., Yang G., Scott D.A., Chao T.H., Correia Jda S., de la Torre J.C.,
RA Li E.;
RT "Identification of MAVS splicing variants that interfere with RIGI/MAVS
RT pathway signaling.";
RL Mol. Immunol. 45:2277-2287(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=22427742; DOI=10.1371/journal.pbio.1001282;
RA Patel M.R., Loo Y.M., Horner S.M., Gale M. Jr., Malik H.S.;
RT "Convergent evolution of escape from hepaciviral antagonism in primates.";
RL PLoS Biol. 10:E1001282-E1001282(2012).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP VARIANT GLU-93.
RC TISSUE=Pericardium, Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [11]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-93; LYS-198 AND
RP PHE-409.
RC TISSUE=Brain;
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 [13]
RP INTERACTION WITH HCV NS3/4A PROTEASE (MICROBIAL INFECTION), MUTAGENESIS OF
RP CYS-435; CYS-452 AND CYS-508, AND PROTEOLYTIC CLEAVAGE (MICROBIAL
RP INFECTION).
RX PubMed=16301520; DOI=10.1073/pnas.0508531102;
RA Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.;
RT "Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral
RT signaling protein off the mitochondria to evade innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005).
RN [14]
RP INTERACTION WITH DHX58/LGP2 AND IKBKE.
RX PubMed=17020950; DOI=10.1128/jvi.01325-06;
RA Komuro A., Horvath C.M.;
RT "RNA- and virus-independent inhibition of antiviral signaling by RNA
RT helicase LGP2.";
RL J. Virol. 80:12332-12342(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP INTERACTION WITH HEPATITIS GB VIRUS B NS3/4A PROTEASE (MICROBIAL
RP INFECTION), CLEAVAGE SITE, AND MUTAGENESIS OF CYS-508.
RX PubMed=17093192; DOI=10.1128/jvi.02076-06;
RA Chen Z., Benureau Y., Rijnbrand R., Yi J., Wang T., Warter L.,
RA Lanford R.E., Weinman S.A., Lemon S.M., Martin A., Li K.;
RT "GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the
RT adaptor protein MAVS.";
RL J. Virol. 81:964-976(2007).
RN [17]
RP CLEAVAGE BY HAV PROTEIN 3CD (MICROBIAL INFECTION), CLEAVAGE SITE, AND
RP MUTAGENESIS OF GLN-427 AND GLU-463.
RX PubMed=17438296; DOI=10.1073/pnas.0611506104;
RA Yang Y., Liang Y., Qu L., Chen Z., Yi M., Li K., Lemon S.M.;
RT "Disruption of innate immunity due to mitochondrial targeting of a
RT picornaviral protease precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7253-7258(2007).
RN [18]
RP UBIQUITINATION.
RX PubMed=17460044; DOI=10.1073/pnas.0611551104;
RA Arimoto K., Takahashi H., Hishiki T., Konishi H., Fujita T., Shimotohno K.;
RT "Negative regulation of the RIG-I signaling by the ubiquitin ligase
RT RNF125.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7500-7505(2007).
RN [19]
RP INTERACTION WITH IFIH1.
RX PubMed=17600090; DOI=10.1073/pnas.0700544104;
RA Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P., Chen D.,
RA Zhai Z., Zhong B., Tien P., Shu H.B.;
RT "Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
RT signaling by the dihydroxyacetone kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
RN [20]
RP INTERACTION WITH ATG5 AND ATG12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-54.
RX PubMed=17709747; DOI=10.1073/pnas.0704014104;
RA Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q.,
RA Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
RT "The Atg5-Atg12 conjugate associates with innate antiviral immune
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
RN [21]
RP INTERACTION WITH CYLD.
RX PubMed=18636086; DOI=10.1038/embor.2008.136;
RA Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A., Cardenas W.B.,
RA Yount J.S., Moran T.M., Basler C.F., Komuro A., Horvath C.M., Xavier R.,
RA Ting A.T.;
RT "The tumour suppressor CYLD is a negative regulator of RIG-I-mediated
RT antiviral response.";
RL EMBO Rep. 9:930-936(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP INTERACTION WITH NLRX1.
RX PubMed=18200010; DOI=10.1038/nature06501;
RA Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E.,
RA Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z.,
RA Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y.;
RT "NLRX1 is a regulator of mitochondrial antiviral immunity.";
RL Nature 451:573-577(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; SER-165;
RP SER-222; SER-233; THR-234 AND SER-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [28]
RP INTERACTION WITH SRC.
RX PubMed=19419966; DOI=10.1074/jbc.m808233200;
RA Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.;
RT "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-
RT elicited antiviral signaling.";
RL J. Biol. Chem. 284:19122-19131(2009).
RN [29]
RP INTERACTION WITH PSMA7.
RX PubMed=19734229; DOI=10.4049/jimmunol.0901646;
RA Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L., Zhang Y.,
RA He X., Xu Y., Shi W., Zhong H.;
RT "Negative regulation of MAVS-mediated innate immune response by PSMA7.";
RL J. Immunol. 183:4241-4248(2009).
RN [30]
RP INTERACTION WITH PCBP2, AND UBIQUITINATION BY ITCH.
RX PubMed=19881509; DOI=10.1038/ni.1815;
RA You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
RT "PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
RT ligase AIP4.";
RL Nat. Immunol. 10:1300-1308(2009).
RN [31]
RP INTERACTION WITH C1QBP.
RX PubMed=19164550; DOI=10.1073/pnas.0811029106;
RA Xu L., Xiao N., Liu F., Ren H., Gu J.;
RT "Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009).
RN [32]
RP INTERACTION WITH STING1.
RX PubMed=19416887; DOI=10.1073/pnas.0900818106;
RA Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y.,
RA Yang F., Shu H.B.;
RT "ISG56 is a negative-feedback regulator of virus-triggered signaling and
RT cellular antiviral response.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20451243; DOI=10.1016/j.cell.2010.04.018;
RA Dixit E., Boulant S., Zhang Y., Lee A.S., Odendall C., Shum B., Hacohen N.,
RA Chen Z.J., Whelan S.P., Fransen M., Nibert M.L., Superti-Furga G.,
RA Kagan J.C.;
RT "Peroxisomes are signaling platforms for antiviral innate immunity.";
RL Cell 141:668-681(2010).
RN [35]
RP FUNCTION, INTERACTION WITH TOMM70, AND SUBCELLULAR LOCATION.
RX PubMed=20628368; DOI=10.1038/cr.2010.103;
RA Liu X.Y., Wei B., Shi H.X., Shan Y.F., Wang C.;
RT "Tom70 mediates activation of interferon regulatory factor 3 on
RT mitochondria.";
RL Cell Res. 20:994-1011(2010).
RN [36]
RP FUNCTION, INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=20127681; DOI=10.1002/eji.200940203;
RA Oshiumi H., Sakai K., Matsumoto M., Seya T.;
RT "DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate
RT IFN-beta-inducing potential.";
RL Eur. J. Immunol. 40:940-948(2010).
RN [37]
RP FUNCTION, INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=21170385; DOI=10.1371/journal.pone.0014258;
RA Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S.,
RA Kato N., Shimotohno K., Seya T.;
RT "Hepatitis C virus core protein abrogates the DDX3 function that enhances
RT IPS-1-mediated IFN-beta induction.";
RL PLoS ONE 5:E14258-E14258(2010).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [40]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-148.
RX PubMed=21436888; DOI=10.1371/journal.ppat.1001311;
RA Mukherjee A., Morosky S.A., Delorme-Axford E., Dybdahl-Sissoko N.,
RA Oberste M.S., Wang T., Coyne C.B.;
RT "The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host
RT type I interferon and apoptotic signaling.";
RL PLoS Pathog. 7:E1001311-E1001311(2011).
RN [41]
RP INTERACTION WITH IFIT3 AND TBK1.
RX PubMed=21813773; DOI=10.4049/jimmunol.1100963;
RA Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
RT "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging
RT MAVS and TBK1.";
RL J. Immunol. 187:2559-2568(2011).
RN [42]
RP FUNCTION, INTERACTION WITH NDFIP1 AND SMURF1, AND UBIQUITINATION BY SMURF1.
RX PubMed=23087404; DOI=10.4049/jimmunol.1201445;
RA Wang Y., Tong X., Ye X.;
RT "Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing
RT E3 ligase Smurf1-mediated MAVS degradation.";
RL J. Immunol. 189:5304-5313(2012).
RN [43]
RP INTERACTION WITH HRSV NS1 (MICROBIAL INFECTION).
RX PubMed=22383950; DOI=10.1371/journal.pone.0029386;
RA Boyapalle S., Wong T., Garay J., Teng M., San Juan-Vergara H.,
RA Mohapatra S., Mohapatra S.;
RT "Respiratory syncytial virus NS1 protein colocalizes with mitochondrial
RT antiviral signaling protein MAVS following infection.";
RL PLoS ONE 7:E29386-E29386(2012).
RN [44]
RP INTERACTION WITH ANKRD17.
RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
RA Menning M., Kufer T.A.;
RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
RT Nod2-mediated inflammatory responses.";
RL FEBS Lett. 587:2137-2142(2013).
RN [45]
RP INTERACTION WITH MUL1.
RX PubMed=23399697; DOI=10.1038/icb.2013.7;
RA Jenkins K., Khoo J.J., Sadler A., Piganis R., Wang D., Borg N.A.,
RA Hjerrild K., Gould J., Thomas B.J., Nagley P., Hertzog P.J., Mansell A.;
RT "Mitochondrially localised MUL1 is a novel modulator of antiviral
RT signaling.";
RL Immunol. Cell Biol. 91:321-330(2013).
RN [46]
RP INTERACTION WITH UBXN1.
RX PubMed=23545497; DOI=10.1016/j.celrep.2013.02.027;
RA Wang P., Yang L., Cheng G., Yang G., Xu Z., You F., Sun Q., Lin R.,
RA Fikrig E., Sutton R.E.;
RT "UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune
RT response by targeting MAVS.";
RL Cell Rep. 3:1057-1070(2013).
RN [47]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [48]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NLRP3, AND MUTAGENESIS OF
RP LYS-10; LYS-311 AND LYS-461.
RX PubMed=23582325; DOI=10.1016/j.cell.2013.02.054;
RA Subramanian N., Natarajan K., Clatworthy M.R., Wang Z., Germain R.N.;
RT "The adaptor MAVS promotes NLRP3 mitochondrial localization and
RT inflammasome activation.";
RL Cell 153:348-361(2013).
RN [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-165; SER-180;
RP SER-188; THR-215 AND SER-222, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [50]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX PubMed=24390337; DOI=10.1128/jvi.02712-13;
RA Feng Q., Langereis M.A., Lork M., Nguyen M., Hato S.V., Lanke K., Emdad L.,
RA Bhoopathi P., Fisher P.B., Lloyd R.E., van Kuppeveld F.J.;
RT "Enterovirus 2Apro targets MDA5 and MAVS in infected cells.";
RL J. Virol. 88:3369-3378(2014).
RN [51]
RP INTERACTION WITH SARS-COV VIRUS PROTEIN ORF9B (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=25135833; DOI=10.4049/jimmunol.1303196;
RA Shi C.S., Qi H.Y., Boularan C., Huang N.N., Abu-Asab M., Shelhamer J.H.,
RA Kehrl J.H.;
RT "SARS-coronavirus open reading frame-9b suppresses innate immunity by
RT targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome.";
RL J. Immunol. 193:3080-3089(2014).
RN [52]
RP FUNCTION, DOMAIN, INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442,
RP UBIQUITINATION, AND MUTAGENESIS OF SER-442.
RX PubMed=25636800; DOI=10.1126/science.aaa2630;
RA Liu S., Cai X., Wu J., Cong Q., Chen X., Li T., Du F., Ren J., Wu Y.T.,
RA Grishin N.V., Chen Z.J.;
RT "Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF
RT induces IRF3 activation.";
RL Science 347:AAA2630-AAA2630(2015).
RN [53]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [54]
RP INTERACTION WITH ECSIT.
RX PubMed=25228397; DOI=10.1159/000365971;
RA Lei C.Q., Zhang Y., Li M., Jiang L.Q., Zhong B., Kim Y.H., Shu H.B.;
RT "ECSIT bridges RIG-I-like receptors to VISA in signaling events of innate
RT antiviral responses.";
RL J. Innate Immun. 7:153-164(2015).
RN [55]
RP INTERACTION WITH DDX3X AND TRAF3.
RX PubMed=27980081; DOI=10.1042/bcj20160956;
RA Gu L., Fullam A., McCormack N., Hoehn Y., Schroeder M.;
RT "DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-
RT ordinate assembly of signalling complexes downstream from MAVS.";
RL Biochem. J. 474:571-587(2017).
RN [56]
RP FUNCTION, INTERACTION WITH TAX1BP1, AND SUBCELLULAR LOCATION.
RX PubMed=27736772; DOI=10.1128/mcb.00422-16;
RA Choi Y.B., Shembade N., Parvatiyar K., Balachandran S., Harhaj E.W.;
RT "TAX1BP1 Restrains Virus-Induced Apoptosis by Facilitating Itch-Mediated
RT Degradation of the Mitochondrial Adaptor MAVS.";
RL Mol. Cell. Biol. 37:0-0(2017).
RN [57]
RP INTERACTION WITH TTLL12; TBK1 AND IKBKE.
RX PubMed=28011935; DOI=10.4049/jimmunol.1601194;
RA Ju L.G., Zhu Y., Lei P.J., Yan D., Zhu K., Wang X., Li Q.L., Li X.J.,
RA Chen J.W., Li L.Y., Wu M.;
RT "TTLL12 Inhibits the Activation of Cellular Antiviral Signaling through
RT Interaction with VISA/MAVS.";
RL J. Immunol. 198:1274-1284(2017).
RN [58]
RP INTERACTION WITH SENECA VALLEY VIRUS PROTEASE 3C (MICROBIAL INFECTION),
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-148;
RP GLN-159; GLN-162; GLN-196 AND GLN-198.
RX PubMed=28566380; DOI=10.1128/jvi.00823-17;
RA Qian S., Fan W., Liu T., Wu M., Zhang H., Cui X., Zhou Y., Hu J., Wei S.,
RA Chen H., Li X., Qian P.;
RT "Seneca Valley virus suppresses host type I interferon production by
RT targeting adaptor proteins MAVS, TRIF, and TANK for cleavage.";
RL J. Virol. 91:0-0(2017).
RN [59]
RP FUNCTION, SUBUNIT, AND UBIQUITINATION AT LYS-10; LYS-311 AND LYS-461.
RX PubMed=27992402; DOI=10.1038/ni.3641;
RA Liu B., Zhang M., Chu H., Zhang H., Wu H., Song G., Wang P., Zhao K.,
RA Hou J., Wang X., Zhang L., Gao C.;
RT "The ubiquitin E3 ligase TRIM31 promotes aggregation and activation of the
RT signaling adaptor MAVS through Lys63-linked polyubiquitination.";
RL Nat. Immunol. 18:214-224(2017).
RN [60]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLY-209;
RP GLY-251 AND GLY-265.
RX PubMed=28253362; DOI=10.1371/journal.ppat.1006243;
RA Wang B., Xi X., Lei X., Zhang X., Cui S., Wang J., Jin Q., Zhao Z.;
RT "Correction: Enterovirus 71 Protease 2Apro Targets MAVS to Inhibit Anti-
RT Viral Type I Interferon Responses.";
RL PLoS Pathog. 13:E1006243-E1006243(2017).
RN [61]
RP INTERACTION WITH GPATCH3.
RX PubMed=28414768; DOI=10.1371/journal.ppat.1006328;
RA Nie Y., Ran Y., Zhang H.Y., Huang Z.F., Pan Z.Y., Wang S.Y., Wang Y.Y.;
RT "GPATCH3 negatively regulates RLR-mediated innate antiviral responses by
RT disrupting the assembly of VISA signalosome.";
RL PLoS Pathog. 13:E1006328-E1006328(2017).
RN [62]
RP FUNCTION, UBIQUITINATION AT LYS-325, MUTAGENESIS OF LYS-325, AND
RP INTERACTION WITH TBK1.
RX PubMed=29743353; DOI=10.1128/jvi.00321-18;
RA Xue B., Li H., Guo M., Wang J., Xu Y., Zou X., Deng R., Li G., Zhu H.;
RT "TRIM21 Promotes Innate Immune Response to RNA Viral Infection through
RT Lys27-Linked Polyubiquitination of MAVS.";
RL J. Virol. 92:0-0(2018).
RN [63]
RP INTERACTION WITH CLPB.
RX PubMed=31522117; DOI=10.1016/j.isci.2019.08.056;
RA Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O.,
RA Tamada T., Koshiba T.;
RT "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes:
RT Insight into a Role of the Coiled-Coil Region.";
RL IScience 19:1065-1078(2019).
RN [64]
RP INTERACTION WITH TRAF3IP3.
RX PubMed=31390091; DOI=10.15252/embj.2019102075;
RA Zhu W., Li J., Zhang R., Cai Y., Wang C., Qi S., Chen S., Liang X., Qi N.,
RA Hou F.;
RT "TRAF3IP3 mediates the recruitment of TRAF3 to MAVS for antiviral innate
RT immunity.";
RL EMBO J. 38:e102075-e102075(2019).
RN [65]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-429 AND ASP-490.
RX PubMed=30878284; DOI=10.1016/j.molcel.2019.02.013;
RA Ning X., Wang Y., Jing M., Sha M., Lv M., Gao P., Zhang R., Huang X.,
RA Feng J.M., Jiang Z.;
RT "Apoptotic caspases suppress type i interferon production via the cleavage
RT of cGAS, MAVS, and IRF3.";
RL Mol. Cell 74:19-31(2019).
RN [66]
RP INTERACTION WITH ANDES HANTAVIRUS NON-STRUCTURAL PROTEIN NS-S (MICROBIAL
RP INFECTION).
RX PubMed=32321811; DOI=10.1128/jvi.00454-20;
RA Vera-Otarola J., Solis L., Lowy F., Olguin V., Angulo J., Pino K.,
RA Tischler N.D., Otth C., Padula P., Lopez-Lastra M.;
RT "The Andes Orthohantavirus NSs Protein Antagonizes the Type I Interferon
RT Response by Inhibiting MAVS Signaling.";
RL J. Virol. 94:0-0(2020).
RN [67]
RP INTERACTION WITH FOOT-AND-MOUTH DISEASE VIRUS PROTEIN VP1 (MICROBIAL
RP INFECTION).
RX PubMed=33232374; DOI=10.1371/journal.ppat.1009057;
RA Ekanayaka P., Lee S.Y., Herath T.U.B., Kim J.H., Kim T.H., Lee H.,
RA Chathuranga K., Chathuranga W.A.G., Park J.H., Lee J.S.;
RT "Foot-and-mouth disease virus VP1 target the MAVS to inhibit type-I
RT interferon signaling and VP1 E83K mutation results in virus attenuation.";
RL PLoS Pathog. 16:e1009057-e1009057(2020).
RN [68]
RP FUNCTION, AND UBIQUITINATION BY RNF115.
RX PubMed=33139700; DOI=10.1038/s41467-020-19318-3;
RA Zhang Z.D., Xiong T.C., Yao S.Q., Wei M.C., Chen M., Lin D., Zhong B.;
RT "RNF115 plays dual roles in innate antiviral responses by catalyzing
RT distinct ubiquitination of MAVS and MITA.";
RL Nat. Commun. 11:5536-5536(2020).
RN [69]
RP FUNCTION, INTERACTION WITH N4BP3 AND TRAF2, AND UBIQUITINATION.
RX PubMed=34880843; DOI=10.3389/fmicb.2021.770600;
RA Wang C., Ling T., Zhong N., Xu L.G.;
RT "N4BP3 Regulates RIG-I-Like Receptor Antiviral Signaling Positively by
RT Targeting Mitochondrial Antiviral Signaling Protein.";
RL Front. Microbiol. 12:770600-770600(2021).
RN [70]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 3-93, SUBUNIT, AND
RP MUTAGENESIS OF GLU-26 AND TRP-56.
RX PubMed=24569476; DOI=10.7554/elife.01489;
RA Xu H., He X., Zheng H., Huang L.J., Hou F., Yu Z., de la Cruz M.J.,
RA Borkowski B., Zhang X., Chen Z.J., Jiang Q.X.;
RT "Structural basis for the prion-like MAVS filaments in antiviral innate
RT immunity.";
RL Elife 3:E01489-E01489(2014).
RN [71]
RP INTERACTION WITH SARS-COV-2 VIRUS PROTEIN ORF9B (MICROBIAL INFECTION), AND
RP FUNCTION.
RX PubMed=33110251; DOI=10.1038/s41423-020-00571-x;
RA Fu Y.Z., Wang S.Y., Zheng Z.Q., Yi H., Li W.W., Xu Z.S., Wang Y.Y.;
RT "SARS-CoV-2 membrane glycoprotein M antagonizes the MAVS-mediated innate
RT antiviral response.";
RL Cell. Mol. Immunol. 18:613-620(2021).
RN [72]
RP FUNCTION, INTERACTION WITH UBL7, AND UBIQUITINATION BY TRIM21.
RX PubMed=36943869; DOI=10.1016/j.celrep.2023.112272;
RA Jiang W., Li X., Xu H., Gu X., Li S., Zhu L., Lu J., Duan X., Li W.,
RA Fang M.;
RT "UBL7 enhances antiviral innate immunity by promoting Lys27-linked
RT polyubiquitination of MAVS.";
RL Cell Rep. 42:112272-112272(2023).
RN [73]
RP FUNCTION, INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BILF1 (MICROBIAL
RP INFECTION), SUBCELLULAR LOCATION, UFMYLATION AT LYS-461 (MICROBIAL
RP INFECTION), AND MUTAGENESIS OF LYS-461.
RX PubMed=37311461; DOI=10.1016/j.molcel.2023.05.018;
RA Yiu S.P.T., Zerbe C., Vanderwall D., Huttlin E.L., Weekes M.P.,
RA Gewurz B.E.;
RT "An Epstein-Barr virus protein interaction map reveals NLRP3 inflammasome
RT evasion via MAVS UFMylation.";
RL Mol. Cell 0:0-0(2023).
RN [74]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=37582970; DOI=10.1038/s41423-023-01065-2;
RA Liu F., Zhuang W., Song B., Yang Y., Liu J., Zheng Y., Liu B., Zheng J.,
RA Zhao W., Gao C.;
RT "MAVS-loaded unanchored Lys63-linked polyubiquitin chains activate the RIG-
RT I-MAVS signaling cascade.";
RL Cell. Mol. Immunol. 0:0-0(2023).
RN [75]
RP INTERACTION WITH SMIM30.
RX PubMed=37656786; DOI=10.1126/sciadv.adg7053;
RA Shi T.T., Huang Y., Li Y., Dai X.L., He Y.H., Ding J.C., Ran T., Shi Y.,
RA Yuan Q., Li W.J., Liu W.;
RT "MAVI1, an endoplasmic reticulum-localized microprotein, suppresses
RT antiviral innate immune response by targeting MAVS on mitochondrion.";
RL Sci. Adv. 9:eadg7053-eadg7053(2023).
RN [76]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-99 IN COMPLEX WITH RIGI,
RP STRUCTURE BY ELECTRON MICROSCOPY (3.64 ANGSTROMS) OF 1-97, AND SUBUNIT.
RX PubMed=25018021; DOI=10.1016/j.molcel.2014.06.010;
RA Wu B., Peisley A., Tetrault D., Li Z., Egelman E.H., Magor K.E., Walz T.,
RA Penczek P.A., Hur S.;
RT "Molecular imprinting as a signal-activation mechanism of the viral RNA
RT sensor RIG-I.";
RL Mol. Cell 55:511-523(2014).
RN [77] {ECO:0007744|PDB:5JEK}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 433-450 IN COMPLEX WITH IRF3,
RP INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442, AND MUTAGENESIS OF
RP SER-442.
RX PubMed=27302953; DOI=10.1073/pnas.1603269113;
RA Zhao B., Shu C., Gao X., Sankaran B., Du F., Shelton C.L., Herr A.B.,
RA Ji J.Y., Li P.;
RT "Structural basis for concerted recruitment and activation of IRF-3 by
RT innate immune adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3403-E3412(2016).
CC -!- FUNCTION: Adapter required for innate immune defense against viruses
CC (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806,
CC PubMed:19631370, PubMed:20451243, PubMed:23087404, PubMed:20127681,
CC PubMed:21170385, PubMed:27992402, PubMed:33139700, PubMed:37582970).
CC Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect
CC intracellular dsRNA produced during viral replication, to coordinate
CC pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to
CC the subsequent induction of antiviral cytokines such as IFNB and RANTES
CC (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868,
CC PubMed:16177806, PubMed:19631370, PubMed:20451243, PubMed:23087404,
CC PubMed:25636800, PubMed:20127681, PubMed:21170385, PubMed:20628368,
CC PubMed:33110251, PubMed:27736772). Peroxisomal and mitochondrial MAVS
CC act sequentially to create an antiviral cellular state
CC (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the
CC rapid interferon-independent expression of defense factors that provide
CC short-term protection, whereas mitochondrial MAVS activates an
CC interferon-dependent signaling pathway with delayed kinetics, which
CC amplifies and stabilizes the antiviral response (PubMed:20451243). May
CC activate the same pathways following detection of extracellular dsRNA
CC by TLR3 (PubMed:16153868). May protect cells from apoptosis
CC (PubMed:16125763). Involved in NLRP3 inflammasome activation by
CC mediating NLRP3 recruitment to mitochondria (PubMed:23582325).
CC {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
CC ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806,
CC ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20127681,
CC ECO:0000269|PubMed:20451243, ECO:0000269|PubMed:20628368,
CC ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:23087404,
CC ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:25636800,
CC ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:27992402,
CC ECO:0000269|PubMed:33110251, ECO:0000269|PubMed:33139700,
CC ECO:0000269|PubMed:37582970}.
CC -!- SUBUNIT: Self-associates and polymerizes (via CARD domains) to form 400
CC nM long three-stranded helical filaments on mitochondria, filament
CC nucleation requires interaction with RIGI whose CARD domains act as a
CC template for filament assembly (PubMed:27992402, PubMed:24569476,
CC PubMed:25018021). Interacts with RIGI, IFIH1/MDA5, TRAF2, TRAF6 and
CC C1QBP (PubMed:16125763, PubMed:16127453, PubMed:17600090,
CC PubMed:33110251). May interact with FADD, RIPK1, CHUK and IKBKB
CC (PubMed:16153868, PubMed:16177806, PubMed:16127453). Interacts (when
CC phosphorylated) with IRF3; following activation and phosphorylation on
CC the pLxIS motif by TBK1, recruits IRF3 (PubMed:25636800,
CC PubMed:27302953, PubMed:33110251). Interacts with NLRX1
CC (PubMed:18200010). Interaction with NLRX1 requires the CARD domain
CC (PubMed:18200010). Interacts with PSMA7 (PubMed:19734229). Interacts
CC with TRAFD1 (By similarity). Interacts (via C-terminus) with PCBP2 in a
CC complex containing MAVS/IPS1, PCBP2 and ITCH (PubMed:19881509).
CC Interacts with CYLD (PubMed:18636086). Interacts with SRC
CC (PubMed:19419966). Interacts with DHX58/LGP2 and IKBKE
CC (PubMed:16177806, PubMed:17020950, PubMed:28011935). Interacts with
CC STING1 (PubMed:19416887). Interacts with IFIT3 (via N-terminus)
CC (PubMed:21813773). Interacts with TBK1 only in the presence of IFIT3
CC (PubMed:21813773, PubMed:28011935, PubMed:29743353). Interacts with
CC TTLL12; the interaction prevents MAVS binding to TBK1 and IKBKE
CC (PubMed:28011935). Interacts with MUL1 (PubMed:23399697). Interacts
CC with ANKRD17 (PubMed:23711367). Interacts with NDFIP1
CC (PubMed:23087404). Interacts with SMURF1; the interaction is mediated
CC by NDFIP1 and leads to MAVS ubiquitination and degradation
CC (PubMed:23087404). Interacts with UBXN1; this interaction inhibits
CC MAVS-mediated antiviral pathway (PubMed:23545497). Interacts (via C-
CC terminus) with GPATCH3; the interaction is markedly increased upon
CC viral infection (PubMed:28414768). Directly interacts (via CARD domain)
CC with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5
CC conjugates (PubMed:17709747). Interacts with DHX33 (via the helicase C-
CC terminal domain) (By similarity). Interacts with DDX3X (via C-
CC terminus); this interaction occurs rapidly, but transiently after
CC Sendai virus infection (PubMed:20127681, PubMed:21170385,
CC PubMed:27980081). The interaction with DDX3X potentiates MAVS-mediated
CC IFNB induction (PubMed:20127681). Conversely inhibition of this
CC interaction, for instance by HCV core protein, prevents MAVS-mediated
CC IFNB induction (PubMed:21170385). Transiently interacts with TRAF3
CC early during Sendai virus infection (PubMed:27980081). Interacts with
CC CLPB; the interaction is enhanced by Sendai virus infection
CC (PubMed:31522117). Interacts with TRAF3IP3 (PubMed:31390091). Interacts
CC with TOMM70; the interaction is enhanced by Sendai virus infection
CC (PubMed:20628368). Interacts with ZNFX1 (By similarity). Interacts with
CC N4BP3; this interaction promotes the polyubiquitination of MAVS
CC (PubMed:34880843). Interacts with TAX1BP1; this interaction induces
CC MAVS polyubiquitination (PubMed:27736772). Interacts with NLRP3;
CC promoting NLRP3 recruitment to mitochondria and activation of the NLRP3
CC inflammasome (PubMed:23582325). Interacts with ECSIT; this interaction
CC bridges RIGI to the MAVS complex at the mitochondrion
CC (PubMed:25228397). Interacts with UBL7; this interaction promotes MAVS
CC 'Lys-27'-linked ubiquitination leading to type I interferon production
CC (PubMed:36943869). Interacts (via transmembrane domain) with
CC SMIM30/MAVI1 (via transmembrane domain); the interaction disrupts MAVS
CC interaction with RIGI and inhibits MAVS aggregation, resulting in the
CC repression of type I interferon signaling and innate immune responses
CC (PubMed:37656786). {ECO:0000250, ECO:0000250|UniProtKB:Q8VCF0,
CC ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
CC ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806,
CC ECO:0000269|PubMed:17020950, ECO:0000269|PubMed:17600090,
CC ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:18200010,
CC ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19164550,
CC ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:19419966,
CC ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:19881509,
CC ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20628368,
CC ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21813773,
CC ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:23399697,
CC ECO:0000269|PubMed:23545497, ECO:0000269|PubMed:23582325,
CC ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24569476,
CC ECO:0000269|PubMed:25018021, ECO:0000269|PubMed:25228397,
CC ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953,
CC ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:27980081,
CC ECO:0000269|PubMed:27992402, ECO:0000269|PubMed:28011935,
CC ECO:0000269|PubMed:28414768, ECO:0000269|PubMed:31390091,
CC ECO:0000269|PubMed:31522117, ECO:0000269|PubMed:33110251,
CC ECO:0000269|PubMed:34880843, ECO:0000269|PubMed:36943869,
CC ECO:0000269|PubMed:37656786}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus (HCV)
CC NS3/4A protease; this interaction leads to MAVS cleavage, thereby
CC preventing the establishment of an antiviral state.
CC {ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis GB virus B
CC NS3/4A protease; this interaction leads to MAVS cleavage.
CC {ECO:0000269|PubMed:17093192}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus/HRSV protein NS1; this interaction disrupts MAVS
CC binding to RIGI. {ECO:0000269|PubMed:22383950}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Andes virus Nnon-
CC structural protein NS-S; this interaction may reduce MAVS
CC ubiquitination and leads to inhibition of MAVS-induced type-I IFN
CC signaling pathway. {ECO:0000269|PubMed:32321811}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Seneca Valley virus
CC protease 3C; this interaction allows the cleavage of MAVS and
CC subsequent suppression of host innate immunity.
CC {ECO:0000269|PubMed:28566380}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV virus protein
CC ORF9b; this interaction mediates MAVS proteasomal degradation.
CC {ECO:0000269|PubMed:25135833}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV-2 virus protein
CC M; this interaction impairs MAVS self-association and its recruitment
CC of downstream components. {ECO:0000269|PubMed:33110251}.
CC -!- SUBUNIT: (Microbial infection) Interacts with foot-and-mouth disease
CC virus protein VP1; this interaction competes with TRAF3 interaction to
CC MAVS leading to suppression of host innate immunity.
CC {ECO:0000269|PubMed:33232374}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein BILF1; this interaction mediates MAVS routing from mitochondria
CC to lysosomes. {ECO:0000269|PubMed:37311461}.
CC -!- INTERACTION:
CC Q7Z434; P00519: ABL1; NbExp=6; IntAct=EBI-995373, EBI-375543;
CC Q7Z434; P46379: BAG6; NbExp=2; IntAct=EBI-995373, EBI-347552;
CC Q7Z434; Q07021: C1QBP; NbExp=5; IntAct=EBI-995373, EBI-347528;
CC Q7Z434; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-995373, EBI-739580;
CC Q7Z434; P27797: CALR; NbExp=3; IntAct=EBI-995373, EBI-1049597;
CC Q7Z434; P12830: CDH1; NbExp=3; IntAct=EBI-995373, EBI-727477;
CC Q7Z434; O00571: DDX3X; NbExp=4; IntAct=EBI-995373, EBI-353779;
CC Q7Z434; P36957: DLST; NbExp=3; IntAct=EBI-995373, EBI-351007;
CC Q7Z434; Q9BYX4: IFIH1; NbExp=7; IntAct=EBI-995373, EBI-6115771;
CC Q7Z434; Q14164: IKBKE; NbExp=4; IntAct=EBI-995373, EBI-307369;
CC Q7Z434; Q13568: IRF5; NbExp=2; IntAct=EBI-995373, EBI-3931258;
CC Q7Z434; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-995373, EBI-751501;
CC Q7Z434; Q8IWA4: MFN1; NbExp=2; IntAct=EBI-995373, EBI-1048197;
CC Q7Z434; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-995373, EBI-1055945;
CC Q7Z434; Q96P20: NLRP3; NbExp=4; IntAct=EBI-995373, EBI-6253230;
CC Q7Z434; Q9Y6K5: OAS3; NbExp=2; IntAct=EBI-995373, EBI-6115729;
CC Q7Z434; O95786: RIGI; NbExp=19; IntAct=EBI-995373, EBI-995350;
CC Q7Z434; O43353: RIPK2; NbExp=3; IntAct=EBI-995373, EBI-358522;
CC Q7Z434; O75746: SLC25A12; NbExp=3; IntAct=EBI-995373, EBI-1047585;
CC Q7Z434; P42224: STAT1; NbExp=3; IntAct=EBI-995373, EBI-1057697;
CC Q7Z434; Q86WV6: STING1; NbExp=9; IntAct=EBI-995373, EBI-2800345;
CC Q7Z434; Q9UHD2: TBK1; NbExp=6; IntAct=EBI-995373, EBI-356402;
CC Q7Z434; P37173: TGFBR2; NbExp=3; IntAct=EBI-995373, EBI-296151;
CC Q7Z434; Q12933: TRAF2; NbExp=5; IntAct=EBI-995373, EBI-355744;
CC Q7Z434; Q9Y4K3: TRAF6; NbExp=4; IntAct=EBI-995373, EBI-359276;
CC Q7Z434; Q14139: UBE4A; NbExp=2; IntAct=EBI-995373, EBI-1048119;
CC Q7Z434; P0DTD8: 7b; Xeno; NbExp=3; IntAct=EBI-995373, EBI-25475914;
CC Q7Z434; Q7TFA1: 7b; Xeno; NbExp=2; IntAct=EBI-995373, EBI-25492846;
CC Q7Z434; P59636: 9b; Xeno; NbExp=5; IntAct=EBI-995373, EBI-9021274;
CC Q7Z434; P0DTC5: M; Xeno; NbExp=11; IntAct=EBI-995373, EBI-25475853;
CC Q7Z434; Q6WB96: M2; Xeno; NbExp=4; IntAct=EBI-995373, EBI-6863628;
CC Q7Z434; PRO_0000449623 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-995373, EBI-25475864;
CC Q7Z434; Q69027: X; Xeno; NbExp=2; IntAct=EBI-995373, EBI-3650820;
CC Q7Z434; A2T3M4; Xeno; NbExp=4; IntAct=EBI-995373, EBI-9522123;
CC Q7Z434-1; Q9H1Y0: ATG5; NbExp=4; IntAct=EBI-15577799, EBI-1047414;
CC Q7Z434-1; Q9BYX4: IFIH1; NbExp=3; IntAct=EBI-15577799, EBI-6115771;
CC Q7Z434-1; Q86UT6-1: NLRX1; NbExp=3; IntAct=EBI-15577799, EBI-15680006;
CC Q7Z434-1; O95786-1: RIGI; NbExp=8; IntAct=EBI-15577799, EBI-15577823;
CC Q7Z434-1; Q96EQ8: RNF125; NbExp=2; IntAct=EBI-15577799, EBI-2339208;
CC Q7Z434-1; Q86WV6: STING1; NbExp=7; IntAct=EBI-15577799, EBI-2800345;
CC Q7Z434-1; P61964: WDR5; NbExp=3; IntAct=EBI-15577799, EBI-540834;
CC Q7Z434-1; Q91WS2-1: Nlrp6; Xeno; NbExp=2; IntAct=EBI-15577799, EBI-16182226;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16125763}; Single-pass membrane protein
CC {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:11780052,
CC ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:20127681,
CC ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:21170385,
CC ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:25135833,
CC ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:37311461}. Peroxisome
CC {ECO:0000269|PubMed:20451243}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q7Z434-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z434-2; Sequence=VSP_010262, VSP_010263;
CC Name=3;
CC IsoId=Q7Z434-3; Sequence=VSP_010261, VSP_010264;
CC Name=4;
CC IsoId=Q7Z434-4; Sequence=VSP_045872;
CC Name=5; Synonyms=MAVS1b, exon 3 deletion;
CC IsoId=Q7Z434-5; Sequence=VSP_047817, VSP_047818;
CC Name=6; Synonyms=MAVS1a, exon 2 deletion;
CC IsoId=Q7Z434-6; Sequence=VSP_047816, VSP_010263;
CC -!- TISSUE SPECIFICITY: Present in T-cells, monocytes, epithelial cells and
CC hepatocytes (at protein level). Ubiquitously expressed, with highest
CC levels in heart, skeletal muscle, liver, placenta and peripheral blood
CC leukocytes. {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
CC ECO:0000269|PubMed:16153868}.
CC -!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif: following
CC phosphorylation by TBK1, the phosphorylated pLxIS motif of MAVS
CC recruits IRF3 (PubMed:25636800). IRF3 is then phosphorylated and
CC activated by TBK1 to induce type-I interferons and other cytokines
CC (PubMed:25636800). {ECO:0000269|PubMed:25636800}.
CC -!- DOMAIN: Both CARD and transmembrane domains are essential for antiviral
CC function. The CARD domain is responsible for interaction with RIGI and
CC IFIH1/MDA5. {ECO:0000269|PubMed:16125763}.
CC -!- DOMAIN: The transmembrane domain and residues 300-444 are essential for
CC its interaction with DHX58/LGP2. {ECO:0000269|PubMed:17020950}.
CC -!- PTM: Following activation, phosphorylated by TBK1 at Ser-442 in the
CC pLxIS motif (PubMed:25636800, PubMed:27302953). The phosphorylated
CC pLxIS motif constitutes an IRF3-binding motif, leading to recruitment
CC of the transcription factor IRF3 to induce type-I interferons and other
CC cytokines (PubMed:25636800). {ECO:0000269|PubMed:25636800,
CC ECO:0000269|PubMed:27302953}.
CC -!- PTM: Ubiquitinated (PubMed:19881509, PubMed:23087404, PubMed:25636800).
CC Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH; ITCH-
CC dependent polyubiquitination is mediated by the interaction with PCBP2
CC and leads to MAVS/IPS1 proteasomal degradation (PubMed:19881509).
CC Ubiquitinated by RNF125, leading to its degradation by the proteasome
CC (PubMed:17460044). Undergoes 'Lys-48'-linked ubiquitination catalyzed
CC by SMURF1 (PubMed:23087404). Ubiquitinated via 'Lys-63'-linked
CC ubiquitination at Lys-10, Lys-311 and Lys-461 by UBE2N and TRIM31,
CC promoting MAVS polymerization and formation of three-stranded helical
CC filaments on mitochondria (PubMed:27992402, PubMed:37582970). Undergoes
CC 'Lys-63'-linked ubiquitination leading to enhanced interaction between
CC MAVS and TRAF2 (PubMed:34880843). Undergoes 'Lys-27'-linked
CC ubiquitination by TRIM21 leading to enhanced interaction between MAVS
CC and TBK1 (PubMed:29743353, PubMed:36943869). Deubiquitinated by USP10
CC leading to attenuation of RIGI-mediated MAVS aggregation and production
CC of type I interferon (PubMed:37582970). Undergoes 'Lys-48'-linked
CC polyubiquitination catalyzed by RNF115 leading to its degradation
CC (PubMed:33139700). {ECO:0000269|PubMed:17460044,
CC ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:23087404,
CC ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27992402,
CC ECO:0000269|PubMed:29743353, ECO:0000269|PubMed:33139700,
CC ECO:0000269|PubMed:34880843, ECO:0000269|PubMed:36943869,
CC ECO:0000269|PubMed:37582970}.
CC -!- PTM: Proteolytically cleaved by apoptotic caspases during apoptosis,
CC leading to its inactivation (PubMed:30878284). Cleavage by CASP3 during
CC virus-induced apoptosis inactivates it, preventing cytokine
CC overproduction (PubMed:30878284). {ECO:0000269|PubMed:30878284}.
CC -!- PTM: (Microbial infection) Cleaved and degraded by hepatitis A virus
CC (HAV) protein 3ABC allowing the virus to disrupt the activation of host
CC IRF3 through the MDA5 pathway. {ECO:0000269|PubMed:17438296}.
CC -!- PTM: (Microbial infection) Cleaved by the protease 2A of coxsackievirus
CC B3, poliovirus and enterovirus 71 allowing the virus to disrupt the
CC host type I interferon production. {ECO:0000269|PubMed:24390337,
CC ECO:0000269|PubMed:28253362}.
CC -!- PTM: (Microbial infection) Cleaved by Seneca Valley virus protease 3C
CC allowing the virus to suppress interferon type-I production.
CC {ECO:0000269|PubMed:28566380}.
CC -!- PTM: (Microbial infection) Cleaved by HCV protease NS3/4A, thereby
CC preventing the establishment of an antiviral state.
CC {ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520}.
CC -!- PTM: (Microbial infection) UFMylated by ULF1 in association with
CC Epstein-Barr virus BILF1; leading to MAVS routing to the lysosome.
CC {ECO:0000269|PubMed:37311461}.
CC -!- MISCELLANEOUS: [Isoform 5]: Selectively activates an IFNbeta but not an
CC IL8 promoter. Interacts with RIP1 and FADD and exhibits anti-viral
CC activity against VSV infection. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86585.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14684.1; Type=Frameshift; Evidence={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; DQ174270; AAZ80417.1; -; mRNA.
DR EMBL; DQ167126; ABA54890.1; -; mRNA.
DR EMBL; DQ181928; ABA19229.1; -; mRNA.
DR EMBL; AB232371; BAE79738.1; -; mRNA.
DR EMBL; EF467323; ABR24161.1; -; mRNA.
DR EMBL; EF467324; ABR24162.1; -; mRNA.
DR EMBL; KC415005; AGF94754.1; -; mRNA.
DR EMBL; AB033097; BAA86585.1; ALT_INIT; mRNA.
DR EMBL; AB097003; BAC77356.1; -; mRNA.
DR EMBL; AK023799; BAB14684.1; ALT_FRAME; mRNA.
DR EMBL; AK123956; BAC85734.1; -; mRNA.
DR EMBL; AK130992; BAC85473.1; -; mRNA.
DR EMBL; AK291785; BAF84474.1; -; mRNA.
DR EMBL; AK296897; BAG59455.1; -; mRNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10481.1; -; Genomic_DNA.
DR EMBL; BC044952; AAH44952.1; -; mRNA.
DR CCDS; CCDS33437.1; -. [Q7Z434-1]
DR CCDS; CCDS56176.1; -. [Q7Z434-4]
DR RefSeq; NP_001193420.1; NM_001206491.1. [Q7Z434-4]
DR RefSeq; NP_065797.2; NM_020746.4. [Q7Z434-1]
DR PDB; 2MS7; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-100.
DR PDB; 2MS8; NMR; -; A=1-100.
DR PDB; 2VGQ; X-ray; 2.10 A; A=1-93.
DR PDB; 3J6C; EM; 9.60 A; A=3-93.
DR PDB; 3J6J; EM; 3.64 A; A/B/C/D/E/G/I/L=1-97.
DR PDB; 3RC5; X-ray; 1.60 A; B=502-508.
DR PDB; 4P4H; X-ray; 3.40 A; I/J/K/L/M/N/O/P=1-99.
DR PDB; 4Z8M; X-ray; 2.95 A; C/D=450-468.
DR PDB; 5JEK; X-ray; 2.40 A; C/D=433-448.
DR PDB; 7DNI; EM; 3.20 A; M/N/O/P=1-97.
DR PDBsum; 2MS7; -.
DR PDBsum; 2MS8; -.
DR PDBsum; 2VGQ; -.
DR PDBsum; 3J6C; -.
DR PDBsum; 3J6J; -.
DR PDBsum; 3RC5; -.
DR PDBsum; 4P4H; -.
DR PDBsum; 4Z8M; -.
DR PDBsum; 5JEK; -.
DR PDBsum; 7DNI; -.
DR AlphaFoldDB; Q7Z434; -.
DR BMRB; Q7Z434; -.
DR EMDB; EMD-30784; -.
DR EMDB; EMD-5890; -.
DR EMDB; EMD-5891; -.
DR EMDB; EMD-5922; -.
DR EMDB; EMD-5925; -.
DR EMDB; EMD-6428; -.
DR SMR; Q7Z434; -.
DR BioGRID; 121570; 307.
DR ComplexPortal; CPX-6037; MAVS-TRAF3 E3 ubiquitin ligase complex.
DR DIP; DIP-35445N; -.
DR IntAct; Q7Z434; 102.
DR MINT; Q7Z434; -.
DR STRING; 9606.ENSP00000401980; -.
DR ChEMBL; CHEMBL4523363; -.
DR GlyCosmos; Q7Z434; 6 sites, 2 glycans.
DR GlyGen; Q7Z434; 27 sites, 2 O-linked glycans (27 sites).
DR iPTMnet; Q7Z434; -.
DR MetOSite; Q7Z434; -.
DR PhosphoSitePlus; Q7Z434; -.
DR SwissPalm; Q7Z434; -.
DR BioMuta; MAVS; -.
DR DMDM; 47115748; -.
DR CPTAC; CPTAC-977; -.
DR EPD; Q7Z434; -.
DR jPOST; Q7Z434; -.
DR MassIVE; Q7Z434; -.
DR MaxQB; Q7Z434; -.
DR PaxDb; 9606-ENSP00000401980; -.
DR PeptideAtlas; Q7Z434; -.
DR ProteomicsDB; 27148; -.
DR ProteomicsDB; 3402; -.
DR ProteomicsDB; 69137; -. [Q7Z434-1]
DR ProteomicsDB; 69138; -. [Q7Z434-2]
DR ProteomicsDB; 69139; -. [Q7Z434-3]
DR Pumba; Q7Z434; -.
DR Antibodypedia; 3363; 715 antibodies from 43 providers.
DR DNASU; 57506; -.
DR Ensembl; ENST00000416600.6; ENSP00000413749.2; ENSG00000088888.18. [Q7Z434-4]
DR Ensembl; ENST00000428216.4; ENSP00000401980.2; ENSG00000088888.18. [Q7Z434-1]
DR GeneID; 57506; -.
DR KEGG; hsa:57506; -.
DR MANE-Select; ENST00000428216.4; ENSP00000401980.2; NM_020746.5; NP_065797.2.
DR UCSC; uc002wjw.5; human. [Q7Z434-1]
DR AGR; HGNC:29233; -.
DR CTD; 57506; -.
DR DisGeNET; 57506; -.
DR GeneCards; MAVS; -.
DR HGNC; HGNC:29233; MAVS.
DR HPA; ENSG00000088888; Low tissue specificity.
DR MIM; 609676; gene.
DR neXtProt; NX_Q7Z434; -.
DR OpenTargets; ENSG00000088888; -.
DR PharmGKB; PA164722208; -.
DR VEuPathDB; HostDB:ENSG00000088888; -.
DR eggNOG; ENOG502SAUA; Eukaryota.
DR GeneTree; ENSGT00510000049120; -.
DR HOGENOM; CLU_042052_0_0_1; -.
DR InParanoid; Q7Z434; -.
DR OMA; PHIDQKF; -.
DR OrthoDB; 5358122at2759; -.
DR PhylomeDB; Q7Z434; -.
DR TreeFam; TF333444; -.
DR PathwayCommons; Q7Z434; -.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
DR Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9833482; PKR-mediated signaling.
DR SignaLink; Q7Z434; -.
DR SIGNOR; Q7Z434; -.
DR BioGRID-ORCS; 57506; 21 hits in 1167 CRISPR screens.
DR ChiTaRS; MAVS; human.
DR EvolutionaryTrace; Q7Z434; -.
DR GeneWiki; VISA_(gene); -.
DR GenomeRNAi; 57506; -.
DR Pharos; Q7Z434; Tbio.
DR PRO; PR:Q7Z434; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q7Z434; Protein.
DR Bgee; ENSG00000088888; Expressed in skeletal muscle tissue of rectus abdominis and 200 other cell types or tissues.
DR Genevisible; Q7Z434; HS.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:ComplexPortal.
DR GO; GO:0050700; F:CARD domain binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProt.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0039552; F:RIG-I binding; IDA:UniProt.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IDA:UniProt.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProt.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB.
DR GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IDA:BHF-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
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; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0071660; P:positive regulation of IP-10 production; IDA:BHF-UCL.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISS:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProt.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; IDA:UniProtKB.
DR GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; NAS:ComplexPortal.
DR CDD; cd08811; CARD_IPS1; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR031964; CARD_dom.
DR InterPro; IPR042144; CARD_IPS1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR PANTHER; PTHR21446; DUF3504 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21446:SF6; MITOCHONDRIAL ANTIVIRAL-SIGNALING PROTEIN; 1.
DR Pfam; PF16739; CARD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Host-virus interaction; Immunity; Innate immunity; Isopeptide bond;
KW Membrane; Methylation; Mitochondrion; Mitochondrion outer membrane;
KW Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..540
FT /note="Mitochondrial antiviral-signaling protein"
FT /id="PRO_0000144096"
FT TOPO_DOM 1..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..540
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 10..77
FT /note="CARD"
FT REGION 10..77
FT /note="Required for interaction with NLRX1"
FT /evidence="ECO:0000269|PubMed:18200010"
FT REGION 95..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..147
FT /note="Interaction with TRAF2"
FT /evidence="ECO:0000269|PubMed:16153868"
FT REGION 153..158
FT /note="Interaction with TRAF6"
FT REGION 314..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..460
FT /note="Interaction with TRAF6"
FT REGION 476..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 439..442
FT /note="pLxIS motif"
FT /evidence="ECO:0000269|PubMed:25636800"
FT COMPBIAS 102..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 148..149
FT /note="(Microbial infection) Cleavage; by viral Seneca
FT Valley virus protease 3C"
FT /evidence="ECO:0000269|PubMed:28566380"
FT SITE 148
FT /note="(Microbial infection) Cleavage by CV3B"
FT /evidence="ECO:0000269|PubMed:21436888"
FT SITE 208..209
FT /note="(Microbial infection) Cleavage by protease 2A of
FT enterovirus 71"
FT /evidence="ECO:0000269|PubMed:28253362"
FT SITE 250..251
FT /note="(Microbial infection) Cleavage by protease 2A of
FT enterovirus 71"
FT /evidence="ECO:0000269|PubMed:28253362"
FT SITE 264..265
FT /note="(Microbial infection) Cleavage by protease 2A of
FT enterovirus 71"
FT /evidence="ECO:0000269|PubMed:28253362"
FT SITE 427..428
FT /note="(Microbial infection) Cleavage; by HAV protein 3ABC"
FT /evidence="ECO:0000269|PubMed:17438296"
FT SITE 429..430
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000269|PubMed:30878284"
FT SITE 490..491
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000269|PubMed:30878284"
FT SITE 508..509
FT /note="(Microbial infection) Cleavage; by HCV and hepatitis
FT GB virus B NS3/4A protease complex"
FT /evidence="ECO:0000269|PubMed:16177806,
FT ECO:0000269|PubMed:16301520"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 236
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCF0"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCF0"
FT MOD_RES 442
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:25636800,
FT ECO:0000269|PubMed:27302953"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:27992402"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:27992402"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:29743353"
FT CROSSLNK 461
FT /note="(Microbial infection) Glycyl lysine isopeptide (Lys-
FT Gly) (interchain with G-Cter in UFM1)"
FT /evidence="ECO:0000269|PubMed:37311461"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:27992402"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045872"
FT VAR_SEQ 40..131
FT /note="DRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASV
FT YQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> GPRTVPQTHWSHRHF
FT LLRGQGPPHLLRPTASPTTAAERRSQVTPCLSRRPRRQSPQERIQSKPCRRSAPEPSQG
FT IQMVAPWSPPLTWQPSAL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:18207245"
FT /id="VSP_047816"
FT VAR_SEQ 64..148
FT /note="RRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAE
FT RPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQ -> LPTWAGEETPGGQSSGRGLDFS
FT SLTSGAVWLWQMSDFWSCFSTWTVSIWLILHWVLLRLNLQVFAKCLAQSKWPLLLPSLS
FT CPTW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010261"
FT VAR_SEQ 98..124
FT /note="RTSDRPPDPLEPPSLPAERPGPPTPAA -> QFRASPADAQPQSHPKESRWW
FT PPGVLL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18207245"
FT /id="VSP_047817"
FT VAR_SEQ 99..131
FT /note="TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> ERPALALLDPQPAPW
FT PPLSFSLSLYFLPFSVILFLVTVKR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010262"
FT VAR_SEQ 125..540
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18207245"
FT /id="VSP_047818"
FT VAR_SEQ 132..540
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18207245"
FT /id="VSP_010263"
FT VAR_SEQ 149..540
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010264"
FT VARIANT 79
FT /note="C -> F (in dbSNP:rs11905552)"
FT /id="VAR_048609"
FT VARIANT 79
FT /note="C -> S (in dbSNP:rs11908032)"
FT /id="VAR_059197"
FT VARIANT 93
FT /note="Q -> E (in dbSNP:rs17857295)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16127453,
FT ECO:0000269|PubMed:16153868"
FT /id="VAR_048610"
FT VARIANT 198
FT /note="Q -> K (in dbSNP:rs7262903)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16177806"
FT /id="VAR_048611"
FT VARIANT 409
FT /note="S -> F (in dbSNP:rs7269320)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16177806"
FT /id="VAR_018448"
FT MUTAGEN 10
FT /note="K->R: Abolished ubiquitination by TRIM31; when
FT associated with R-311 and R-461."
FT /evidence="ECO:0000269|PubMed:23582325"
FT MUTAGEN 26
FT /note="E->A,R: Impairs filament formation and abolishes
FT antiviral signaling activity."
FT /evidence="ECO:0000269|PubMed:24569476"
FT MUTAGEN 54
FT /note="T->A: Impairs ability to induce IFN-beta. Loss of
FT interaction with the ATG5-ATG12 conjugate."
FT /evidence="ECO:0000269|PubMed:16125763,
FT ECO:0000269|PubMed:17709747"
FT MUTAGEN 56
FT /note="W->A,E,R: Impairs filament formation and abolishes
FT antiviral signaling activity."
FT /evidence="ECO:0000269|PubMed:24569476"
FT MUTAGEN 67..69
FT /note="GWV->AAA: Impairs ability to induce IFN-beta."
FT /evidence="ECO:0000269|PubMed:16125763"
FT MUTAGEN 145
FT /note="Q->N: No interaction with TRAF2."
FT /evidence="ECO:0000269|PubMed:16153868"
FT MUTAGEN 148
FT /note="Q->A: Complete loss of cleavage by Seneca Valley
FT virus protease 3C."
FT /evidence="ECO:0000269|PubMed:28566380"
FT MUTAGEN 155
FT /note="E->D: No interaction with TRAF6; when associated
FT with D-457."
FT /evidence="ECO:0000269|PubMed:16153868"
FT MUTAGEN 159
FT /note="Q->A: No effect on cleavage by Seneca Valley virus
FT protease 3C."
FT /evidence="ECO:0000269|PubMed:28566380"
FT MUTAGEN 162
FT /note="Q->A: No effect on cleavage by Seneca Valley virus
FT protease 3C."
FT /evidence="ECO:0000269|PubMed:28566380"
FT MUTAGEN 196
FT /note="Q->A: No effect on cleavage by Seneca Valley virus
FT protease 3C."
FT /evidence="ECO:0000269|PubMed:28566380"
FT MUTAGEN 198
FT /note="Q->A: No effect on cleavage by Seneca Valley virus
FT protease 3C."
FT /evidence="ECO:0000269|PubMed:28566380"
FT MUTAGEN 209
FT /note="G->A: Complete loss of cleavage by protease 2A of
FT enterovirus 71."
FT /evidence="ECO:0000269|PubMed:28253362"
FT MUTAGEN 251
FT /note="G->A: Complete loss of cleavage by protease 2A of
FT enterovirus 71."
FT /evidence="ECO:0000269|PubMed:28253362"
FT MUTAGEN 265
FT /note="G->A: Complete loss of cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:28253362"
FT MUTAGEN 311
FT /note="K->R: Abolished ubiquitination by TRIM31; when
FT associated with R-10 and R-461."
FT /evidence="ECO:0000269|PubMed:23582325"
FT MUTAGEN 325
FT /note="K->R: Abolished ubiquitination by TRIM21."
FT /evidence="ECO:0000269|PubMed:29743353"
FT MUTAGEN 427
FT /note="Q->A: No cleavage by HHAV 3ABC."
FT /evidence="ECO:0000269|PubMed:17438296"
FT MUTAGEN 429
FT /note="D->A: Decreased cleavage by CASP3. Abolished
FT cleavage by CASP3; when associated with A-490."
FT /evidence="ECO:0000269|PubMed:30878284"
FT MUTAGEN 435
FT /note="C->R: No effect on cleavage by NS3/4A protease
FT complex."
FT /evidence="ECO:0000269|PubMed:16301520"
FT MUTAGEN 442
FT /note="S->A: Abolished ability to bind and activate IRF3."
FT /evidence="ECO:0000269|PubMed:25636800,
FT ECO:0000269|PubMed:27302953"
FT MUTAGEN 452
FT /note="C->R: No effect on cleavage by NS3/4A protease
FT complex."
FT /evidence="ECO:0000269|PubMed:16301520"
FT MUTAGEN 457
FT /note="E->D: No interaction with TRAF6; when associated
FT with D-155."
FT /evidence="ECO:0000269|PubMed:16153868"
FT MUTAGEN 461
FT /note="K->R: Abolished ubiquitination by TRIM31; when
FT associated with R-10 and R-311."
FT /evidence="ECO:0000269|PubMed:23582325"
FT MUTAGEN 461
FT /note="K->R: Abolished UFMylation by UFM1."
FT /evidence="ECO:0000269|PubMed:37311461"
FT MUTAGEN 463
FT /note="E->A: No effect on cleavage by HHAV 3ABC."
FT /evidence="ECO:0000269|PubMed:17438296"
FT MUTAGEN 490
FT /note="D->A: Decreased cleavage by CASP3. Abolished
FT cleavage by CASP3; when associated with A-429."
FT /evidence="ECO:0000269|PubMed:30878284"
FT MUTAGEN 508
FT /note="C->A,R: No cleavage by HCV and hepatitis GB virus B
FT NS3/4A protease complex."
FT /evidence="ECO:0000269|PubMed:16177806,
FT ECO:0000269|PubMed:16301520, ECO:0000269|PubMed:17093192"
FT CONFLICT 42
FT /note="L -> P (in Ref. 8; BAC77356)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="T -> N (in Ref. 9; BAF84474)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> V (in Ref. 8; BAC77356)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="S -> P (in Ref. 8; BAC77356)"
FT /evidence="ECO:0000305"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2VGQ"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2VGQ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2MS8"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:4Z8M"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:3RC5"
SQ SEQUENCE 540 AA; 56528 MW; 0E23E3E115941EE8 CRC64;
MPFAEDKTYK YICRNFSNFC NVDVVEILPY LPCLTARDQD RLRATCTLSG NRDTLWHLFN
TLQRRPGWVE YFIAALRGCE LVDLADEVAS VYQSYQPRTS DRPPDPLEPP SLPAERPGPP
TPAAAHSIPY NSCREKEPSY PMPVQETQAP ESPGENSEQA LQTLSPRAIP RNPDGGPLES
SSDLAALSPL TSSGHQEQDT ELGSTHTAGA TSSLTPSRGP VSPSVSFQPL ARSTPRASRL
PGPTGSVVST GTSFSSSSPG LASAGAAEGK QGAESDQAEP IICSSGAEAP ANSLPSKVPT
TLMPVNTVAL KVPANPASVS TVPSKLPTSS KPPGAVPSNA LTNPAPSKLP INSTRAGMVP
SKVPTSMVLT KVSASTVPTD GSSRNEETPA APTPAGATGG SSAWLDSSSE NRGLGSELSK
PGVLASQVDS PFSGCFEDLA ISASTSLGMG PCHGPEENEY KSEGTFGIHV AENPSIQLLE
GNPGPPADPD GGPRPQADRK FQEREVPCHR PSPGALWLQV AVTGVLVVTL LVVLYRRRLH
//