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Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)

 MAVS_HUMAN              Reviewed;         540 AA.
Q7Z434; A8K6X0; B2BD33; B2BD34; F5H6C8; M1P2Z0; Q2HWT5; Q3I0Y2; Q5T7I6;
Q86VY7; Q9H1H3; Q9H4Y1; Q9H8D3; Q9ULE9;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
17-JUN-2020, entry version 175.
RecName: Full=Mitochondrial antiviral-signaling protein {ECO:0000305};
Short=MAVS {ECO:0000305};
AltName: Full=CARD adapter inducing interferon beta;
Short=Cardif;
AltName: Full=Interferon beta promoter stimulator protein 1;
Short=IPS-1;
AltName: Full=Putative NF-kappa-B-activating protein 031N;
AltName: Full=Virus-induced-signaling adapter;
Short=VISA;
Name=MAVS {ECO:0000312|HGNC:HGNC:29233}; Synonyms=IPS1, KIAA1271, VISA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
MUTAGENESIS OF THR-54 AND 67-GLY--VAL-69, INTERACTION WITH DDX58/RIG-I AND
TRAF6, SUBCELLULAR LOCATION, AND VARIANTS LYS-198 AND PHE-409.
PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
"Identification and characterization of MAVS, a mitochondrial antiviral
signaling protein that activates NF-kappaB and IRF 3.";
Cell 122:669-682(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH
DDX58/RIG-I; IRF3; TRAF2 AND TRAF6, MUTAGENESIS OF GLN-145; GLU-155 AND
GLU-457, FUNCTION, AND VARIANT GLU-93.
PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
"VISA is an adapter protein required for virus-triggered IFN-beta
Signaling.";
Mol. Cell 19:727-740(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX58/RIG-I;
IKBKE; CHUK AND IKBKB, FUNCTION, CLEAVAGE SITE, MUTAGENESIS OF CYS-508, AND
VARIANTS LYS-198 AND PHE-409.
PubMed=16177806; DOI=10.1038/nature04193;
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
Bartenschlager R., Tschopp J.;
"Cardif is an adaptor protein in the RIG-I antiviral pathway and is
targeted by hepatitis C virus.";
Nature 437:1167-1172(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
WITH DDX58/RIG-I; IFIH1/MDA5; FADD AND RIPK1, FUNCTION, AND VARIANT GLU-93.
PubMed=16127453; DOI=10.1038/ni1243;
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J.,
Takeuchi O., Akira S.;
"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon
induction.";
Nat. Immunol. 6:981-988(2005).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
PubMed=18207245; DOI=10.1016/j.molimm.2007.11.018;
Lad S.P., Yang G., Scott D.A., Chao T.H., Correia Jda S., de la Torre J.C.,
Li E.;
"Identification of MAVS splicing variants that interfere with RIGI/MAVS
pathway signaling.";
Mol. Immunol. 45:2277-2287(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=22427742; DOI=10.1371/journal.pbio.1001282;
Patel M.R., Loo Y.M., Horner S.M., Gale M. Jr., Malik H.S.;
"Convergent evolution of escape from hepaciviral antagonism in primates.";
PLoS Biol. 10:E1001282-E1001282(2012).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 6:337-345(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
VARIANT GLU-93.
TISSUE=Pericardium, Placenta, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-93; LYS-198 AND
PHE-409.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
INTERACTION WITH HCV NS3/4A PROTEASE (MICROBIAL INFECTION), CLEAVAGE SITE,
AND MUTAGENESIS OF CYS-435; CYS-452 AND CYS-508.
PubMed=16301520; DOI=10.1073/pnas.0508531102;
Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.;
"Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral
signaling protein off the mitochondria to evade innate immunity.";
Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005).
[14]
INTERACTION WITH DHX58/LGP2 AND IKBKE.
PubMed=17020950; DOI=10.1128/jvi.01325-06;
Komuro A., Horvath C.M.;
"RNA- and virus-independent inhibition of antiviral signaling by RNA
helicase LGP2.";
J. Virol. 80:12332-12342(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
INTERACTION WITH HEPATITIS GB VIRUS B NS3/4A PROTEASE (MICROBIAL
INFECTION), CLEAVAGE SITE, AND MUTAGENESIS OF CYS-508.
PubMed=17093192; DOI=10.1128/jvi.02076-06;
Chen Z., Benureau Y., Rijnbrand R., Yi J., Wang T., Warter L.,
Lanford R.E., Weinman S.A., Lemon S.M., Martin A., Li K.;
"GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the
adaptor protein MAVS.";
J. Virol. 81:964-976(2007).
[17]
CLEAVAGE BY HAV PROTEIN 3CD (MICROBIAL INFECTION), CLEAVAGE SITE, AND
MUTAGENESIS OF GLN-427 AND GLU-463.
PubMed=17438296; DOI=10.1073/pnas.0611506104;
Yang Y., Liang Y., Qu L., Chen Z., Yi M., Li K., Lemon S.M.;
"Disruption of innate immunity due to mitochondrial targeting of a
picornaviral protease precursor.";
Proc. Natl. Acad. Sci. U.S.A. 104:7253-7258(2007).
[18]
UBIQUITINATION.
PubMed=17460044; DOI=10.1073/pnas.0611551104;
Arimoto K., Takahashi H., Hishiki T., Konishi H., Fujita T., Shimotohno K.;
"Negative regulation of the RIG-I signaling by the ubiquitin ligase
RNF125.";
Proc. Natl. Acad. Sci. U.S.A. 104:7500-7505(2007).
[19]
INTERACTION WITH IFIH1.
PubMed=17600090; DOI=10.1073/pnas.0700544104;
Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P., Chen D.,
Zhai Z., Zhong B., Tien P., Shu H.B.;
"Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
signaling by the dihydroxyacetone kinase.";
Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
[20]
INTERACTION WITH ATG5 AND ATG12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-54.
PubMed=17709747; DOI=10.1073/pnas.0704014104;
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q.,
Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
"The Atg5-Atg12 conjugate associates with innate antiviral immune
responses.";
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
[21]
INTERACTION WITH CYLD.
PubMed=18636086; DOI=10.1038/embor.2008.136;
Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A., Cardenas W.B.,
Yount J.S., Moran T.M., Basler C.F., Komuro A., Horvath C.M., Xavier R.,
Ting A.T.;
"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated
antiviral response.";
EMBO Rep. 9:930-936(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
INTERACTION WITH NLRX1.
PubMed=18200010; DOI=10.1038/nature06501;
Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E.,
Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z.,
Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y.;
"NLRX1 is a regulator of mitochondrial antiviral immunity.";
Nature 451:573-577(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-157; SER-165;
SER-222; SER-233; THR-234 AND SER-258, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
FUNCTION.
PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
Chiu Y.-H., Macmillan J.B., Chen Z.J.;
"RNA polymerase III detects cytosolic DNA and induces type I interferons
through the RIG-I pathway.";
Cell 138:576-591(2009).
[28]
INTERACTION WITH SRC.
PubMed=19419966; DOI=10.1074/jbc.m808233200;
Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.;
"The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-
elicited antiviral signaling.";
J. Biol. Chem. 284:19122-19131(2009).
[29]
INTERACTION WITH PSMA7.
PubMed=19734229; DOI=10.4049/jimmunol.0901646;
Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L., Zhang Y.,
He X., Xu Y., Shi W., Zhong H.;
"Negative regulation of MAVS-mediated innate immune response by PSMA7.";
J. Immunol. 183:4241-4248(2009).
[30]
INTERACTION WITH PCBP2, AND UBIQUITINATION BY ITCH.
PubMed=19881509; DOI=10.1038/ni.1815;
You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
ligase AIP4.";
Nat. Immunol. 10:1300-1308(2009).
[31]
INTERACTION WITH C1QBP.
PubMed=19164550; DOI=10.1073/pnas.0811029106;
Xu L., Xiao N., Liu F., Ren H., Gu J.;
"Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009).
[32]
INTERACTION WITH STING1.
PubMed=19416887; DOI=10.1073/pnas.0900818106;
Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y.,
Yang F., Shu H.B.;
"ISG56 is a negative-feedback regulator of virus-triggered signaling and
cellular antiviral response.";
Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-165, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20451243; DOI=10.1016/j.cell.2010.04.018;
Dixit E., Boulant S., Zhang Y., Lee A.S., Odendall C., Shum B., Hacohen N.,
Chen Z.J., Whelan S.P., Fransen M., Nibert M.L., Superti-Furga G.,
Kagan J.C.;
"Peroxisomes are signaling platforms for antiviral innate immunity.";
Cell 141:668-681(2010).
[35]
FUNCTION, INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
PubMed=20127681; DOI=10.1002/eji.200940203;
Oshiumi H., Sakai K., Matsumoto M., Seya T.;
"DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate
IFN-beta-inducing potential.";
Eur. J. Immunol. 40:940-948(2010).
[36]
FUNCTION, INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
PubMed=21170385; DOI=10.1371/journal.pone.0014258;
Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S.,
Kato N., Shimotohno K., Seya T.;
"Hepatitis C virus core protein abrogates the DDX3 function that enhances
IPS-1-mediated IFN-beta induction.";
PLoS ONE 5:E14258-E14258(2010).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-148.
PubMed=21436888; DOI=10.1371/journal.ppat.1001311;
Mukherjee A., Morosky S.A., Delorme-Axford E., Dybdahl-Sissoko N.,
Oberste M.S., Wang T., Coyne C.B.;
"The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host
type I interferon and apoptotic signaling.";
PLoS Pathog. 7:E1001311-E1001311(2011).
[40]
INTERACTION WITH IFIT3 AND TBK1.
PubMed=21813773; DOI=10.4049/jimmunol.1100963;
Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
"IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging
MAVS and TBK1.";
J. Immunol. 187:2559-2568(2011).
[41]
FUNCTION, INTERACTION WITH NDFIP1 AND SMURF1, AND UBIQUITINATION BY SMURF1.
PubMed=23087404; DOI=10.4049/jimmunol.1201445;
Wang Y., Tong X., Ye X.;
"Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing
E3 ligase Smurf1-mediated MAVS degradation.";
J. Immunol. 189:5304-5313(2012).
[42]
INTERACTION WITH HRSV NS1 (MICROBIAL INFECTION).
PubMed=22383950; DOI=10.1371/journal.pone.0029386;
Boyapalle S., Wong T., Garay J., Teng M., San Juan-Vergara H.,
Mohapatra S., Mohapatra S.;
"Respiratory syncytial virus NS1 protein colocalizes with mitochondrial
antiviral signaling protein MAVS following infection.";
PLoS ONE 7:E29386-E29386(2012).
[43]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
[44]
INTERACTION WITH MUL1.
PubMed=23399697; DOI=10.1038/icb.2013.7;
Jenkins K., Khoo J.J., Sadler A., Piganis R., Wang D., Borg N.A.,
Hjerrild K., Gould J., Thomas B.J., Nagley P., Hertzog P.J., Mansell A.;
"Mitochondrially localised MUL1 is a novel modulator of antiviral
signaling.";
Immunol. Cell Biol. 91:321-330(2013).
[45]
INTERACTION WITH UBXN1.
PubMed=23545497; DOI=10.1016/j.celrep.2013.02.027;
Wang P., Yang L., Cheng G., Yang G., Xu Z., You F., Sun Q., Lin R.,
Fikrig E., Sutton R.E.;
"UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune
response by targeting MAVS.";
Cell Rep. 3:1057-1070(2013).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-165; SER-180;
SER-188; THR-215 AND SER-222, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[48]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
PubMed=24390337; DOI=10.1128/jvi.02712-13;
Feng Q., Langereis M.A., Lork M., Nguyen M., Hato S.V., Lanke K., Emdad L.,
Bhoopathi P., Fisher P.B., Lloyd R.E., van Kuppeveld F.J.;
"Enterovirus 2Apro targets MDA5 and MAVS in infected cells.";
J. Virol. 88:3369-3378(2014).
[49]
FUNCTION, DOMAIN, INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442,
UBIQUITINATION, AND MUTAGENESIS OF SER-442.
PubMed=25636800; DOI=10.1126/science.aaa2630;
Liu S., Cai X., Wu J., Cong Q., Chen X., Li T., Du F., Ren J., Wu Y.T.,
Grishin N.V., Chen Z.J.;
"Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF
induces IRF3 activation.";
Science 347:AAA2630-AAA2630(2015).
[50]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[51]
INTERACTION WITH DDX3X AND TRAF3.
PubMed=27980081; DOI=10.1042/bcj20160956;
Gu L., Fullam A., McCormack N., Hoehn Y., Schroeder M.;
"DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-
ordinate assembly of signalling complexes downstream from MAVS.";
Biochem. J. 474:571-587(2017).
[52]
INTERACTION WITH TTLL12; TBK1 AND IKBKE.
PubMed=28011935; DOI=10.4049/jimmunol.1601194;
Ju L.G., Zhu Y., Lei P.J., Yan D., Zhu K., Wang X., Li Q.L., Li X.J.,
Chen J.W., Li L.Y., Wu M.;
"TTLL12 Inhibits the Activation of Cellular Antiviral Signaling through
Interaction with VISA/MAVS.";
J. Immunol. 198:1274-1284(2017).
[53]
INTERACTION WITH SENECA VALLEY VIRUS PROTEASE 3C (MICROBIAL INFECTION),
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION), AND MUTAGENESIS OF GLN-148;
GLN-159; GLN-162; GLN-196 AND GLN-198.
PubMed=28566380; DOI=10.1128/jvi.00823-17;
Qian S., Fan W., Liu T., Wu M., Zhang H., Cui X., Zhou Y., Hu J., Wei S.,
Chen H., Li X., Qian P.;
"Seneca Valley virus suppresses host type I interferon production by
targeting adaptor proteins MAVS, TRIF, and TANK for cleavage.";
J. Virol. 91:0-0(2017).
[54]
PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
PubMed=28253362; DOI=10.1371/journal.ppat.1006243;
Wang B., Xi X., Lei X., Zhang X., Cui S., Wang J., Jin Q., Zhao Z.;
"Correction: Enterovirus 71 Protease 2Apro Targets MAVS to Inhibit Anti-
Viral Type I Interferon Responses.";
PLoS Pathog. 13:E1006243-E1006243(2017).
[55]
INTERACTION WITH GPATCH3.
PubMed=28414768; DOI=10.1371/journal.ppat.1006328;
Nie Y., Ran Y., Zhang H.Y., Huang Z.F., Pan Z.Y., Wang S.Y., Wang Y.Y.;
"GPATCH3 negatively regulates RLR-mediated innate antiviral responses by
disrupting the assembly of VISA signalosome.";
PLoS Pathog. 13:E1006328-E1006328(2017).
[56]
STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 3-93, SUBUNIT, AND
MUTAGENESIS OF GLU-26 AND TRP-56.
PubMed=24569476; DOI=10.7554/elife.01489;
Xu H., He X., Zheng H., Huang L.J., Hou F., Yu Z., de la Cruz M.J.,
Borkowski B., Zhang X., Chen Z.J., Jiang Q.X.;
"Structural basis for the prion-like MAVS filaments in antiviral innate
immunity.";
Elife 3:E01489-E01489(2014).
[57]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-99 IN COMPLEX WITH DDX58/RIG-I,
STRUCTURE BY ELECTRON MICROSCOPY (3.64 ANGSTROMS) OF 1-97, AND SUBUNIT.
PubMed=25018021; DOI=10.1016/j.molcel.2014.06.010;
Wu B., Peisley A., Tetrault D., Li Z., Egelman E.H., Magor K.E., Walz T.,
Penczek P.A., Hur S.;
"Molecular imprinting as a signal-activation mechanism of the viral RNA
sensor RIG-I.";
Mol. Cell 55:511-523(2014).
[58] {ECO:0000244|PDB:5JEK}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 433-450 IN COMPLEX WITH IRF3,
INTERACTION WITH IRF3, PHOSPHORYLATION AT SER-442, AND MUTAGENESIS OF
SER-442.
PubMed=27302953; DOI=10.1073/pnas.1603269113;
Zhao B., Shu C., Gao X., Sankaran B., Du F., Shelton C.L., Herr A.B.,
Ji J.Y., Li P.;
"Structural basis for concerted recruitment and activation of IRF-3 by
innate immune adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 113:E3403-E3412(2016).
-!- FUNCTION: Required for innate immune defense against viruses
(PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806,
PubMed:19631370, PubMed:20451243, PubMed:23087404, PubMed:20127681,
PubMed:21170385). Acts downstream of DHX33, DDX58/RIG-I and IFIH1/MDA5,
which detect intracellular dsRNA produced during viral replication, to
coordinate pathways leading to the activation of NF-kappa-B, IRF3 and
IRF7, and to the subsequent induction of antiviral cytokines such as
IFN-beta and RANTES (CCL5) (PubMed:16125763, PubMed:16127453,
PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20451243,
PubMed:23087404, PubMed:25636800, PubMed:20127681, PubMed:21170385).
Peroxisomal and mitochondrial MAVS act sequentially to create an
antiviral cellular state (PubMed:20451243). Upon viral infection,
peroxisomal MAVS induces the rapid interferon-independent expression of
defense factors that provide short-term protection, whereas
mitochondrial MAVS activates an interferon-dependent signaling pathway
with delayed kinetics, which amplifies and stabilizes the antiviral
response (PubMed:20451243). May activate the same pathways following
detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect
cells from apoptosis (PubMed:16125763). {ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370,
ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20451243,
ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:25636800}.
-!- SUBUNIT: Self-associates and polymerizes (via CARD domains) to form 400
nM long three-stranded helical filaments on mitochondria, filament
nucleation requires interaction with DDX58/RIG-I whose CARD domains act
as a template for filament assembly (PubMed:24569476, PubMed:25018021).
Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP
(PubMed:16125763, PubMed:16127453, PubMed:17600090). May interact with
FADD, RIPK1, CHUK and IKBKB (PubMed:16153868, PubMed:16177806,
PubMed:16127453). Interacts (when phosphorylated) with IRF3; following
activation and phosphorylation on the pLxIS motif by TBK1, recruits
IRF3 (PubMed:25636800, PubMed:27302953). Interacts with NLRX1
(PubMed:18200010). Interaction with NLRX1 requires the CARD domain
(PubMed:18200010). Interacts with PSMA7 (PubMed:19734229). Interacts
with TRAFD1 (By similarity). Interacts (via C-terminus) with PCBP2 in a
complex containing MAVS/IPS1, PCBP2 and ITCH (PubMed:19881509).
Interacts with CYLD (PubMed:18636086). Interacts with SRC
(PubMed:19419966). Interacts with DHX58/LGP2 and IKBKE
(PubMed:16177806, PubMed:17020950, PubMed:28011935). Interacts with
STING1 (PubMed:19416887). Interacts with IFIT3 (via N-terminus)
(PubMed:21813773). Interacts with TBK1 only in the presence of IFIT3
(PubMed:21813773, PubMed:28011935). Interacts with TTLL12; the
interaction prevents MAVS binding to TBK1 and IKBKE (PubMed:28011935).
Interacts with MUL1 (PubMed:23399697). Interacts with ANKRD17
(PubMed:23711367). Interacts with NDFIP1 (PubMed:23087404). Interacts
with SMURF1; the interaction is mediated by NDFIP1 and leads to MAVS
ubiquitination and degradation (PubMed:23087404). Interacts with UBXN1;
this interaction inhibits MAVS-mediated antiviral pathway
(PubMed:23545497). Interacts (via C-terminus) with GPATCH3; the
interaction is markedly increased upon viral infection
(PubMed:28414768). Directly interacts (via CARD domain) with ATG5 and
ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates
(PubMed:17709747). Interacts with DHX33 (via the helicase C-terminal
domain) (By similarity). Interacts with DDX3X (via C-terminus); this
interaction occurs rapidly, but transiently after Sendai virus
infection (PubMed:20127681, PubMed:21170385, PubMed:27980081). The
interaction with DDX3X potentiates MAVS-mediated IFNB induction
(PubMed:20127681). Conversely inhibition of this interaction, for
instance by HCV core protein, prevents MAVS-mediated IFNB induction
(PubMed:21170385). Transiently interacts with TRAF3 early during Sendai
virus infection (PubMed:27980081). {ECO:0000250,
ECO:0000250|UniProtKB:Q8VCF0, ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:17020950,
ECO:0000269|PubMed:17600090, ECO:0000269|PubMed:17709747,
ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18636086,
ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:19416887,
ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:19734229,
ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:20127681,
ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21813773,
ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:23399697,
ECO:0000269|PubMed:23545497, ECO:0000269|PubMed:23711367,
ECO:0000269|PubMed:24569476, ECO:0000269|PubMed:25018021,
ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953,
ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:28011935,
ECO:0000269|PubMed:28414768}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C/HCV NS3/4A
protease; this interaction leads to MAVS cleavage.
{ECO:0000269|PubMed:16301520}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis GB virus B
NS3/4A protease; this interaction leads to MAVS cleavage.
{ECO:0000269|PubMed:17093192}.
-!- SUBUNIT: (Microbial infection) Interacts with human respiratory
syncytial virus/HRSV protein NS1; this interaction disrupts MAVS
binding to DDX58/RIG-I. {ECO:0000269|PubMed:22383950}.
-!- SUBUNIT: (Microbial infection) Interacts with Seneca Valley virus
protease 3C; this interaction allows the cleavage of MAVS and
subsequent suppression of host innate immunity.
{ECO:0000269|PubMed:28566380}.
-!- INTERACTION:
Q7Z434; P00519: ABL1; NbExp=6; IntAct=EBI-995373, EBI-375543;
Q7Z434; P46379: BAG6; NbExp=2; IntAct=EBI-995373, EBI-347552;
Q7Z434; Q07021: C1QBP; NbExp=5; IntAct=EBI-995373, EBI-347528;
Q7Z434; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-995373, EBI-739580;
Q7Z434; O00571: DDX3X; NbExp=4; IntAct=EBI-995373, EBI-353779;
Q7Z434; O95786: DDX58; NbExp=13; IntAct=EBI-995373, EBI-995350;
Q7Z434; Q9BYX4: IFIH1; NbExp=5; IntAct=EBI-995373, EBI-6115771;
Q7Z434; Q14164: IKBKE; NbExp=4; IntAct=EBI-995373, EBI-307369;
Q7Z434; Q13568: IRF5; NbExp=2; IntAct=EBI-995373, EBI-3931258;
Q7Z434; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-995373, EBI-751501;
Q7Z434; Q8IWA4: MFN1; NbExp=2; IntAct=EBI-995373, EBI-1048197;
Q7Z434; Q96P20: NLRP3; NbExp=4; IntAct=EBI-995373, EBI-6253230;
Q7Z434; Q9Y6K5: OAS3; NbExp=2; IntAct=EBI-995373, EBI-6115729;
Q7Z434; O43353: RIPK2; NbExp=3; IntAct=EBI-995373, EBI-358522;
Q7Z434; P42224: STAT1; NbExp=3; IntAct=EBI-995373, EBI-1057697;
Q7Z434; Q86WV6: STING1; NbExp=7; IntAct=EBI-995373, EBI-2800345;
Q7Z434; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-995373, EBI-356402;
Q7Z434; Q12933: TRAF2; NbExp=5; IntAct=EBI-995373, EBI-355744;
Q7Z434; Q9Y4K3: TRAF6; NbExp=4; IntAct=EBI-995373, EBI-359276;
Q7Z434; Q14139: UBE4A; NbExp=2; IntAct=EBI-995373, EBI-1048119;
Q7Z434; Q6WB96: M2; Xeno; NbExp=4; IntAct=EBI-995373, EBI-6863628;
Q7Z434; Q69027: X; Xeno; NbExp=2; IntAct=EBI-995373, EBI-3650820;
Q7Z434; A2T3M4; Xeno; NbExp=4; IntAct=EBI-995373, EBI-9522123;
Q7Z434-1; Q9H1Y0: ATG5; NbExp=4; IntAct=EBI-15577799, EBI-1047414;
Q7Z434-1; O95786-1: DDX58; NbExp=8; IntAct=EBI-15577799, EBI-15577823;
Q7Z434-1; Q9BYX4: IFIH1; NbExp=3; IntAct=EBI-15577799, EBI-6115771;
Q7Z434-1; Q86UT6-1: NLRX1; NbExp=3; IntAct=EBI-15577799, EBI-15680006;
Q7Z434-1; Q96EQ8: RNF125; NbExp=2; IntAct=EBI-15577799, EBI-2339208;
Q7Z434-1; Q86WV6: STING1; NbExp=7; IntAct=EBI-15577799, EBI-2800345;
Q7Z434-1; P61964: WDR5; NbExp=3; IntAct=EBI-15577799, EBI-540834;
Q7Z434-1; Q91WS2-1: Nlrp6; Xeno; NbExp=2; IntAct=EBI-15577799, EBI-16182226;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:16125763}. Mitochondrion
{ECO:0000269|PubMed:11780052, ECO:0000269|PubMed:17709747,
ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:21170385}. Peroxisome
{ECO:0000269|PubMed:20451243}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q7Z434-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z434-2; Sequence=VSP_010262, VSP_010263;
Name=3;
IsoId=Q7Z434-3; Sequence=VSP_010261, VSP_010264;
Name=4;
IsoId=Q7Z434-4; Sequence=VSP_045872;
Name=5; Synonyms=MAVS1b, exon 3 deletion;
IsoId=Q7Z434-5; Sequence=VSP_047817, VSP_047818;
Name=6; Synonyms=MAVS1a, exon 2 deletion;
IsoId=Q7Z434-6; Sequence=VSP_047816, VSP_010263;
-!- TISSUE SPECIFICITY: Present in T-cells, monocytes, epithelial cells and
hepatocytes (at protein level). Ubiquitously expressed, with highest
levels in heart, skeletal muscle, liver, placenta and peripheral blood
leukocytes. {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868}.
-!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif: following
phosphorylation by TBK1, the phosphorylated pLxIS motif of MAVS
recruits IRF3 (PubMed:25636800). IRF3 is then phosphorylated and
activated by TBK1 to induce type-I interferons and other cytokines
(PubMed:25636800). {ECO:0000269|PubMed:25636800}.
-!- DOMAIN: Both CARD and transmembrane domains are essential for antiviral
function. The CARD domain is responsible for interaction with
DDX58/RIG-I and IFIH1/MDA5. {ECO:0000269|PubMed:16125763}.
-!- DOMAIN: The transmembrane domain and residues 300-444 are essential for
its interaction with DHX58/LGP2. {ECO:0000269|PubMed:17020950}.
-!- PTM: Following activation, phosphorylated by TBK1 at Ser-442 in the
pLxIS motif (PubMed:25636800, PubMed:27302953). The phosphorylated
pLxIS motif constitutes an IRF3-binding motif, leading to recruitment
of the transcription factor IRF3 to induce type-I interferons and other
cytokines (PubMed:25636800). {ECO:0000269|PubMed:25636800,
ECO:0000269|PubMed:27302953}.
-!- PTM: (Microbial infection) Cleaved and degraded by hepatitis A virus
(HAV) protein 3ABC allowing the virus to disrupt the activation of host
IRF3 through the MDA5 pathway. {ECO:0000269|PubMed:17438296}.
-!- PTM: (Microbial infection) Cleaved by the protease 2A of coxsackievirus
B3, poliovirus and enterovirus 71 allowing the virus to disrupt the
host type I interferon production. {ECO:0000269|PubMed:24390337,
ECO:0000269|PubMed:28253362}.
-!- PTM: Ubiquitinated (PubMed:19881509, PubMed:23087404, PubMed:25636800).
Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH; ITCH-
dependent polyubiquitination is mediated by the interaction with PCBP2
and leads to MAVS/IPS1 proteasomal degradation (PubMed:19881509).
Ubiquitinated by RNF125, leading to its degradation by the proteasome
(PubMed:17460044). Undergoes 'Lys-48'-linked ubiquitination catalyzed
by SMURF1 (PubMed:23087404). {ECO:0000269|PubMed:17460044,
ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:25636800}.
-!- PTM: (Microbial infection) Cleaved by Seneca Valley virus protease 3C
allowing the virus to suppress interferon type-I production.
{ECO:0000269|PubMed:28566380}.
-!- MISCELLANEOUS: Cleavage by HCV protease complex leads to inactivation.
-!- MISCELLANEOUS: [Isoform 5]: Selectively activates an IFNbeta but not an
IL8 promoter. Interacts with RIP1 and FADD and exhibits anti-viral
activity against VSV infection. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA86585.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=BAB14684.1; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; DQ174270; AAZ80417.1; -; mRNA.
EMBL; DQ167126; ABA54890.1; -; mRNA.
EMBL; DQ181928; ABA19229.1; -; mRNA.
EMBL; AB232371; BAE79738.1; -; mRNA.
EMBL; EF467323; ABR24161.1; -; mRNA.
EMBL; EF467324; ABR24162.1; -; mRNA.
EMBL; KC415005; AGF94754.1; -; mRNA.
EMBL; AB033097; BAA86585.1; ALT_INIT; mRNA.
EMBL; AB097003; BAC77356.1; -; mRNA.
EMBL; AK023799; BAB14684.1; ALT_FRAME; mRNA.
EMBL; AK123956; BAC85734.1; -; mRNA.
EMBL; AK130992; BAC85473.1; -; mRNA.
EMBL; AK291785; BAF84474.1; -; mRNA.
EMBL; AK296897; BAG59455.1; -; mRNA.
EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10481.1; -; Genomic_DNA.
EMBL; BC044952; AAH44952.1; -; mRNA.
CCDS; CCDS33437.1; -. [Q7Z434-1]
CCDS; CCDS56176.1; -. [Q7Z434-4]
RefSeq; NP_001193420.1; NM_001206491.1. [Q7Z434-4]
RefSeq; NP_065797.2; NM_020746.4. [Q7Z434-1]
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.
PDB; 2MS8; NMR; -; A=1-100.
PDB; 2VGQ; X-ray; 2.10 A; A=1-93.
PDB; 3J6C; EM; 9.60 A; A=3-93.
PDB; 3J6J; EM; 3.64 A; A/B/C/D/E/G/I/L=1-97.
PDB; 3RC5; X-ray; 1.60 A; B=502-508.
PDB; 4P4H; X-ray; 3.40 A; I/J/K/L/M/N/O/P=1-99.
PDB; 4Z8M; X-ray; 2.95 A; C/D=450-468.
PDB; 5JEK; X-ray; 2.40 A; C/D=433-448.
PDBsum; 2MS7; -.
PDBsum; 2MS8; -.
PDBsum; 2VGQ; -.
PDBsum; 3J6C; -.
PDBsum; 3J6J; -.
PDBsum; 3RC5; -.
PDBsum; 4P4H; -.
PDBsum; 4Z8M; -.
PDBsum; 5JEK; -.
SMR; Q7Z434; -.
BioGRID; 121570; 139.
DIP; DIP-35445N; -.
IntAct; Q7Z434; 76.
MINT; Q7Z434; -.
STRING; 9606.ENSP00000401980; -.
iPTMnet; Q7Z434; -.
MetOSite; Q7Z434; -.
PhosphoSitePlus; Q7Z434; -.
SwissPalm; Q7Z434; -.
BioMuta; MAVS; -.
DMDM; 47115748; -.
CPTAC; CPTAC-977; -.
EPD; Q7Z434; -.
jPOST; Q7Z434; -.
MassIVE; Q7Z434; -.
MaxQB; Q7Z434; -.
PaxDb; Q7Z434; -.
PeptideAtlas; Q7Z434; -.
PRIDE; Q7Z434; -.
ProteomicsDB; 27148; -.
ProteomicsDB; 3402; -.
ProteomicsDB; 69137; -. [Q7Z434-1]
ProteomicsDB; 69138; -. [Q7Z434-2]
ProteomicsDB; 69139; -. [Q7Z434-3]
Antibodypedia; 3363; 634 antibodies.
DNASU; 57506; -.
Ensembl; ENST00000416600; ENSP00000413749; ENSG00000088888. [Q7Z434-4]
Ensembl; ENST00000428216; ENSP00000401980; ENSG00000088888. [Q7Z434-1]
GeneID; 57506; -.
KEGG; hsa:57506; -.
UCSC; uc002wjw.5; human. [Q7Z434-1]
CTD; 57506; -.
DisGeNET; 57506; -.
EuPathDB; HostDB:ENSG00000088888.17; -.
GeneCards; MAVS; -.
HGNC; HGNC:29233; MAVS.
HPA; ENSG00000088888; Low tissue specificity.
MIM; 609676; gene.
neXtProt; NX_Q7Z434; -.
OpenTargets; ENSG00000088888; -.
PharmGKB; PA164722208; -.
eggNOG; ENOG410IS5U; Eukaryota.
eggNOG; ENOG410Y2HK; LUCA.
GeneTree; ENSGT00510000049120; -.
HOGENOM; CLU_042052_0_0_1; -.
InParanoid; Q7Z434; -.
KO; K12648; -.
OMA; HNGYREE; -.
OrthoDB; 887440at2759; -.
PhylomeDB; Q7Z434; -.
TreeFam; TF333444; -.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
SignaLink; Q7Z434; -.
SIGNOR; Q7Z434; -.
BioGRID-ORCS; 57506; 3 hits in 787 CRISPR screens.
ChiTaRS; MAVS; human.
EvolutionaryTrace; Q7Z434; -.
GeneWiki; VISA_(gene); -.
GenomeRNAi; 57506; -.
Pharos; Q7Z434; Tbio.
PRO; PR:Q7Z434; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; Q7Z434; protein.
Bgee; ENSG00000088888; Expressed in caecum and 228 other tissues.
Genevisible; Q7Z434; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0035591; F:signaling adaptor activity; IMP:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IMP:BHF-UCL.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IDA:BHF-UCL.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0071660; P:positive regulation of IP-10 production; IDA:BHF-UCL.
GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd08811; CARD_IPS1; 1.
InterPro; IPR031964; CARD_dom.
InterPro; IPR042144; CARD_IPS1.
InterPro; IPR026148; Mt_antiviral_sig_pro_met.
PANTHER; PTHR21446:SF6; PTHR21446:SF6; 1.
Pfam; PF16739; CARD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Host-virus interaction; Immunity; Innate immunity; Membrane; Methylation;
Mitochondrion; Mitochondrion outer membrane; Peroxisome; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1..540
/note="Mitochondrial antiviral-signaling protein"
/id="PRO_0000144096"
TOPO_DOM 1..513
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 514..534
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 535..540
/note="Mitochondrial intermembrane"
/evidence="ECO:0000305"
DOMAIN 10..77
/note="CARD"
REGION 10..77
/note="Required for interaction with NLRX1"
/evidence="ECO:0000269|PubMed:18200010"
REGION 143..147
/note="Interaction with TRAF2"
/evidence="ECO:0000269|PubMed:16153868"
REGION 153..158
/note="Interaction with TRAF6"
REGION 455..460
/note="Interaction with TRAF6"
MOTIF 439..442
/note="pLxIS motif"
/evidence="ECO:0000269|PubMed:25636800"
COMPBIAS 103..153
/note="Pro-rich"
SITE 148..149
/note="(Microbial infection) Cleavage; by viral Seneca
Valley virus protease 3C"
/evidence="ECO:0000269|PubMed:28566380"
SITE 148
/note="(Microbial infection) Cleavage by CV3B"
/evidence="ECO:0000269|PubMed:21436888"
SITE 208..209
/note="(Microbial infection) Cleavage by protease 2A of
enterovirus 71"
/evidence="ECO:0000269|PubMed:28253362"
SITE 250..251
/note="(Microbial infection) Cleavage by protease 2A of
enterovirus 71"
/evidence="ECO:0000269|PubMed:28253362"
SITE 264..265
/note="(Microbial infection) Cleavage by protease 2A of
enterovirus 71"
/evidence="ECO:0000269|PubMed:28253362"
SITE 427..428
/note="Cleavage; by HAV protein 3ABC"
/evidence="ECO:0000269|PubMed:17438296"
SITE 508..509
/note="Cleavage; by HCV and hepatitis GB virus B NS3/4A
protease complex"
MOD_RES 152
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:24275569"
MOD_RES 157
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 165
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:24275569"
MOD_RES 180
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 188
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 215
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 222
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 233
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 234
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 236
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q8VCF0"
MOD_RES 253
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 258
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231"
MOD_RES 408
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q8VCF0"
MOD_RES 442
/note="Phosphoserine; by TBK1"
/evidence="ECO:0000269|PubMed:25636800,
ECO:0000269|PubMed:27302953"
VAR_SEQ 1..141
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045872"
VAR_SEQ 40..131
/note="DRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASV
YQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> GPRTVPQTHWSHRHF
LLRGQGPPHLLRPTASPTTAAERRSQVTPCLSRRPRRQSPQERIQSKPCRRSAPEPSQG
IQMVAPWSPPLTWQPSAL (in isoform 6)"
/evidence="ECO:0000303|PubMed:18207245"
/id="VSP_047816"
VAR_SEQ 64..148
/note="RRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAE
RPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQ -> LPTWAGEETPGGQSSGRGLDFS
SLTSGAVWLWQMSDFWSCFSTWTVSIWLILHWVLLRLNLQVFAKCLAQSKWPLLLPSLS
CPTW (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_010261"
VAR_SEQ 98..124
/note="RTSDRPPDPLEPPSLPAERPGPPTPAA -> QFRASPADAQPQSHPKESRWW
PPGVLL (in isoform 5)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245"
/id="VSP_047817"
VAR_SEQ 99..131
/note="TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> ERPALALLDPQPAPW
PPLSFSLSLYFLPFSVILFLVTVKR (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_010262"
VAR_SEQ 125..540
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245"
/id="VSP_047818"
VAR_SEQ 132..540
/note="Missing (in isoform 2 and isoform 6)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245"
/id="VSP_010263"
VAR_SEQ 149..540
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_010264"
VARIANT 79
/note="C -> F (in dbSNP:rs11905552)"
/id="VAR_048609"
VARIANT 79
/note="C -> S (in dbSNP:rs11908032)"
/id="VAR_059197"
VARIANT 93
/note="Q -> E (in dbSNP:rs17857295)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868"
/id="VAR_048610"
VARIANT 198
/note="Q -> K (in dbSNP:rs7262903)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16177806"
/id="VAR_048611"
VARIANT 409
/note="S -> F (in dbSNP:rs7269320)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16177806"
/id="VAR_018448"
MUTAGEN 26
/note="E->A,R: Impairs filament formation and abolishes
antiviral signaling activity."
/evidence="ECO:0000269|PubMed:24569476"
MUTAGEN 54
/note="T->A: Impairs ability to induce IFN-beta. Loss of
interaction with the ATG5-ATG12 conjugate."
/evidence="ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:17709747"
MUTAGEN 56
/note="W->A,E,R: Impairs filament formation and abolishes
antiviral signaling activity."
/evidence="ECO:0000269|PubMed:24569476"
MUTAGEN 67..69
/note="GWV->AAA: Impairs ability to induce IFN-beta."
/evidence="ECO:0000269|PubMed:16125763"
MUTAGEN 145
/note="Q->N: No interaction with TRAF2."
/evidence="ECO:0000269|PubMed:16153868"
MUTAGEN 148
/note="Q->A: Complete loss of cleavage by Seneca Valley
virus protease 3C."
/evidence="ECO:0000269|PubMed:28566380"
MUTAGEN 155
/note="E->D: No interaction with TRAF6; when associated
with D-457."
/evidence="ECO:0000269|PubMed:16153868"
MUTAGEN 159
/note="Q->A: No effect on cleavage by Seneca Valley virus
protease 3C."
/evidence="ECO:0000269|PubMed:28566380"
MUTAGEN 162
/note="Q->A: No effect on cleavage by Seneca Valley virus
protease 3C."
/evidence="ECO:0000269|PubMed:28566380"
MUTAGEN 196
/note="Q->A: No effect on cleavage by Seneca Valley virus
protease 3C."
/evidence="ECO:0000269|PubMed:28566380"
MUTAGEN 198
/note="Q->A: No effect on cleavage by Seneca Valley virus
protease 3C."
/evidence="ECO:0000269|PubMed:28566380"
MUTAGEN 209
/note="G->A: Complete loss of cleavage by protease 2A of
enterovirus 71."
/evidence="ECO:0000269|PubMed:28253362"
MUTAGEN 251
/note="G->A: Complete loss of cleavage by protease 2A of
enterovirus 71."
/evidence="ECO:0000269|PubMed:28253362"
MUTAGEN 265
/note="G->A: Complete loss of cleavage by enterovirus 71."
/evidence="ECO:0000269|PubMed:28253362"
MUTAGEN 427
/note="Q->A: No cleavage by HHAV 3ABC."
/evidence="ECO:0000269|PubMed:17438296"
MUTAGEN 435
/note="C->R: No effect on cleavage by NS3/4A protease
complex."
/evidence="ECO:0000269|PubMed:16301520"
MUTAGEN 442
/note="S->A: Abolished ability to bind and activate IRF3."
/evidence="ECO:0000269|PubMed:25636800,
ECO:0000269|PubMed:27302953"
MUTAGEN 452
/note="C->R: No effect on cleavage by NS3/4A protease
complex."
/evidence="ECO:0000269|PubMed:16301520"
MUTAGEN 457
/note="E->D: No interaction with TRAF6; when associated
with D-155."
/evidence="ECO:0000269|PubMed:16153868"
MUTAGEN 463
/note="E->A: No effect on cleavage by HHAV 3ABC."
/evidence="ECO:0000269|PubMed:17438296"
MUTAGEN 508
/note="C->A,R: No cleavage by HCV and hepatitis GB virus B
NS3/4A protease complex."
/evidence="ECO:0000269|PubMed:16177806,
ECO:0000269|PubMed:16301520, ECO:0000269|PubMed:17093192"
CONFLICT 42
/note="L -> P (in Ref. 8; BAC77356)"
/evidence="ECO:0000305"
CONFLICT 191
/note="T -> N (in Ref. 9; BAF84474)"
/evidence="ECO:0000305"
CONFLICT 356
/note="A -> V (in Ref. 8; BAC77356)"
/evidence="ECO:0000305"
CONFLICT 373
/note="S -> P (in Ref. 8; BAC77356)"
/evidence="ECO:0000305"
HELIX 3..14
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 16..19
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 24..27
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 28..30
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 36..49
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 51..62
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 68..78
/evidence="ECO:0000244|PDB:2VGQ"
HELIX 82..92
/evidence="ECO:0000244|PDB:2VGQ"
STRAND 95..97
/evidence="ECO:0000244|PDB:2MS8"
STRAND 456..459
/evidence="ECO:0000244|PDB:4Z8M"
STRAND 504..507
/evidence="ECO:0000244|PDB:3RC5"
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


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WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP35: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP1224: EBV LMP1 signaling
WP2032: TSH signaling pathway
WP1165: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP931: G Protein Signaling Pathways
WP262: EBV LMP1 signaling
WP1571: EBV LMP1 signaling
WP211: BMP signaling pathway
WP2292: Chemokine signaling pathway
WP73: G Protein Signaling Pathways
WP900: Type II interferon signaling (IFNG)
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[MAVS IPS1 KIAA1271 VISA] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)
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[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[Ticam1 Trif] TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)
[IKBKB IKKB] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[DDX58] Antiviral innate immune response receptor RIG-I (DEAD box protein 58) (Probable ATP-dependent RNA helicase DDX58) (EC 3.6.4.13) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[STING1 ERIS MITA TMEM173] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[IKBKE IKKE IKKI KIAA0151] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[CHUK IKKA TCF16] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16)
[Sting1 Eris Mita Mpys Tmem173] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[TICAM2 TIRAP3 TIRP TRAM] TIR domain-containing adapter molecule 2 (TICAM-2) (Putative NF-kappa-B-activating protein 502) (TRIF-related adapter molecule) (Toll-like receptor adaptor protein 3) (Toll/interleukin-1 receptor domain-containing protein) (MyD88-4)
[BCL10 CIPER CLAP] B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[AZI2 NAP1 TBKBP2] 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1) (TILP)
[Azi2 Az2 Nap1 Tbkp2] 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1)
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[Chuk Ikka] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[PYCARD ASC CARD5 TMS1] Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Ikbke Ikke Ikki] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[Sting1 Tmem173] Stimulator of interferon genes protein (rSTING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (poSTING) (Transmembrane protein 173)

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