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 02-OCT-2024, entry version 197. 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 FUNCTION, UBIQUITINATION, PALMITOYLATION AT CYS-79, AND MUTAGENESIS OF RP CYS-79. RX PubMed=38016475; DOI=10.1016/j.molcel.2023.10.043; RA Zhang G., Jiang P., Tang W., Wang Y., Qiu F., An J., Zheng Y., Wu D., RA Zhou J., Neculai D., Shi Y., Sheng W.; RT "CPT1A induction following epigenetic perturbation promotes MAVS RT palmitoylation and activation to potentiate antitumor immunity."; RL Mol. Cell 83:4370-4385(2023). RN [71] 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 [72] 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 [73] 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 [74] 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 [75] 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 [76] 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 [77] 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 [78] {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:20127681, PubMed:20451243, PubMed:21170385, CC PubMed:23087404, 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:20127681, PubMed:20451243, CC PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, CC PubMed:27736772, PubMed:33110251). 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:24569476, PubMed:25018021, CC PubMed:27992402). 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:16127453, PubMed:16153868, PubMed:16177806). 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 PubMed:38016475). Undergoes 'Lys-48'-linked polyubiquitination CC catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated by the CC interaction with PCBP2 and leads to MAVS/IPS1 proteasomal degradation CC (PubMed:19881509). Ubiquitinated by RNF125, leading to its degradation CC by the proteasome (PubMed:17460044). Undergoes 'Lys-48'-linked CC ubiquitination catalyzed by SMURF1 (PubMed:23087404). Ubiquitinated via CC 'Lys-63'-linked ubiquitination at Lys-10, Lys-311 and Lys-461 by UBE2N CC and TRIM31, promoting MAVS polymerization and formation of three- CC stranded helical filaments on mitochondria (PubMed:27992402, CC PubMed:37582970). Undergoes 'Lys-63'-linked ubiquitination leading to CC enhanced interaction between MAVS and TRAF2 (PubMed:34880843). CC Undergoes 'Lys-27'-linked ubiquitination by TRIM21 leading to enhanced CC interaction between MAVS and TBK1 (PubMed:29743353, PubMed:36943869). CC Deubiquitinated by USP10 leading to attenuation of RIGI-mediated MAVS CC aggregation and production of type I interferon (PubMed:37582970). CC Undergoes 'Lys-48'-linked polyubiquitination catalyzed by RNF115 CC leading to its degradation (PubMed:33139700). CC {ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:19881509, CC ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:25636800, CC ECO:0000269|PubMed:27992402, ECO:0000269|PubMed:29743353, CC ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:34880843, CC ECO:0000269|PubMed:36943869, ECO:0000269|PubMed:37582970, CC ECO:0000269|PubMed:38016475}. CC -!- PTM: Palmitoylated by ZHDDC4. Palmitoylation promotes MAVS CC stabilization and activation by inhibiting 'Lys-48'- but facilitating CC 'Lys-63'-linked ubiquitination. {ECO:0000269|PubMed:38016475}. 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; 315. DR ComplexPortal; CPX-6037; MAVS-TRAF3 E3 ubiquitin ligase complex. DR DIP; DIP-35445N; -. DR IntAct; Q7Z434; 123. 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 jPOST; Q7Z434; -. DR MassIVE; 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; 713 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-9833109; Evasion by RSV of host interferon 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 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 InterPro; IPR052787; MAVS. 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 Lipoprotein; Membrane; Methylation; Mitochondrion; KW Mitochondrion outer membrane; Palmitate; Peroxisome; Phosphoprotein; KW Proteomics identification; 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 LIPID 79 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:38016475" 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 79 FT /note="C->S: Loss of palmitoylation." FT /evidence="ECO:0000269|PubMed:38016475" 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 //