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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.
25-OCT-2017, entry version 151.
RecName: Full=Mitochondrial antiviral-signaling protein;
Short=MAVS;
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; 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, 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, 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]
INTERACTION WITH HUMAN HEPATITIS A VIRUS PROTEIN 3ABC, 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 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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
INTERACTION WITH TMEM173/MITA.
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
INTERACTION WITH HRSV NS1.
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
-!- FUNCTION: Required for innate immune defense against viruses. Acts
downstream of 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). Peroxisomal and mitochondrial
MAVS act sequentially to create an antiviral cellular state. 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. May activate the same
pathways following detection of extracellular dsRNA by TLR3. May
protect cells from apoptosis. {ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370,
ECO:0000269|PubMed:20451243, ECO:0000269|PubMed:23087404}.
-!- 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. Interacts
with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP
(PubMed:17600090). May interact with IRF3, FADD, RIPK1, CHUK and
IKBKB. Interacts with NLRX1. Interaction with NLRX1 requires the
CARD domain. Interacts with PSMA7. Interacts with TRAFD1 (By
similarity). Interacts (via C-terminus) with PCBP2 in a complex
containing MAVS/IPS1, PCBP2 and ITCH. Interacts with CYLD.
Interacts with SRC. Interacts with DHX58/LGP2 and IKBKE. Interacts
with TMEM173/MITA. Interacts with IFIT3 (via N-terminus).
Interacts with TBK1 only in the presence of IFIT3. Interacts with
MUL1. Interacts with ANKRD17. Interacts with and is cleaved by HCV
and hepatitis GB virus B NS3/4A proteases. Interacts with and is
cleaved by HHAV protein 3ABC. Interacts with human respiratory
syncytial virus (HRSV) NS1 protein; this interaction disrupts MAVS
binding to DDX58/RIG-I. 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). {ECO:0000250,
ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806,
ECO:0000269|PubMed:16301520, ECO:0000269|PubMed:17020950,
ECO:0000269|PubMed:17093192, ECO:0000269|PubMed:17438296,
ECO:0000269|PubMed:17600090, 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:21813773, ECO:0000269|PubMed:22383950,
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:28414768}.
-!- INTERACTION:
A2T3M4:- (xeno); NbExp=4; IntAct=EBI-995373, EBI-9522123;
P00519:ABL1; NbExp=6; IntAct=EBI-995373, EBI-375543;
Q9H1Y0:ATG5; NbExp=4; IntAct=EBI-15577799, EBI-1047414;
P46379:BAG6; NbExp=2; IntAct=EBI-995373, EBI-347552;
Q07021:C1QBP; NbExp=5; IntAct=EBI-995373, EBI-347528;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-995373, EBI-739580;
O00571:DDX3X; NbExp=4; IntAct=EBI-995373, EBI-353779;
O95786:DDX58; NbExp=13; IntAct=EBI-995373, EBI-995350;
O95786-1:DDX58; NbExp=8; IntAct=EBI-15577799, EBI-15577823;
Q9BYX4:IFIH1; NbExp=5; IntAct=EBI-995373, EBI-6115771;
Q14164:IKBKE; NbExp=4; IntAct=EBI-995373, EBI-307369;
Q13568:IRF5; NbExp=2; IntAct=EBI-995373, EBI-3931258;
Q9Y2W7:KCNIP3; NbExp=3; IntAct=EBI-995373, EBI-751501;
Q6WB96:M2 (xeno); NbExp=4; IntAct=EBI-995373, EBI-6863628;
Q8IWA4:MFN1; NbExp=2; IntAct=EBI-995373, EBI-1048197;
Q96P20:NLRP3; NbExp=4; IntAct=EBI-995373, EBI-6253230;
Q91WS2-1:Nlrp6 (xeno); NbExp=2; IntAct=EBI-15577799, EBI-16182226;
Q86UT6-1:NLRX1; NbExp=3; IntAct=EBI-15577799, EBI-15680006;
Q9Y6K5:OAS3; NbExp=2; IntAct=EBI-995373, EBI-6115729;
O43353:RIPK2; NbExp=3; IntAct=EBI-995373, EBI-358522;
Q96EQ8:RNF125; NbExp=2; IntAct=EBI-15577799, EBI-2339208;
P42224:STAT1; NbExp=3; IntAct=EBI-995373, EBI-1057697;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-995373, EBI-356402;
Q86WV6:TMEM173; NbExp=7; IntAct=EBI-995373, EBI-2800345;
Q12933:TRAF2; NbExp=3; IntAct=EBI-995373, EBI-355744;
Q14139:UBE4A; NbExp=2; IntAct=EBI-995373, EBI-1048119;
P61964:WDR5; NbExp=3; IntAct=EBI-15577799, EBI-540834;
Q69027:X (xeno); NbExp=2; IntAct=EBI-995373, EBI-3650820;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Mitochondrion.
Peroxisome.
-!- 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;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z434-3; Sequence=VSP_010261, VSP_010264;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q7Z434-4; Sequence=VSP_045872;
Note=No experimental confirmation available.;
Name=5; Synonyms=MAVS1b, exon 3 deletion;
IsoId=Q7Z434-5; Sequence=VSP_047817, VSP_047818;
Note=Selectively activates an IFNbeta but not an IL8 promoter.
Interacts with RIP1 and FADD and exhibits anti-viral activity
against VSV infection.;
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: Both CARD and transmembrane domains are essential for
antiviral function. The CARD domain is responsible for interaction
with DDX58/RIG-I and IFIH1/MDA5.
-!- DOMAIN: The transmembrane domain and residues 300-444 are
essential for its interaction with DHX58/LGP2.
-!- PTM: Ubiquitinated (PubMed:19881509, PubMed:23087404). 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}.
-!- MISCELLANEOUS: Cleavage by HCV protease complex leads to
inactivation.
-!- SEQUENCE CAUTION:
Sequence=BAA86585.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB14684.1; Type=Frameshift; Positions=333; 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; AL353194; CAI11041.1; -; Genomic_DNA.
EMBL; AL109804; CAI11041.1; JOINED; Genomic_DNA.
EMBL; AL109804; CAI18851.1; -; Genomic_DNA.
EMBL; AL353194; CAI18851.1; JOINED; 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]
UniGene; Hs.570362; -.
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; -.
ProteinModelPortal; Q7Z434; -.
SMR; Q7Z434; -.
BioGrid; 121570; 95.
DIP; DIP-35445N; -.
IntAct; Q7Z434; 51.
MINT; MINT-3034048; -.
STRING; 9606.ENSP00000401980; -.
iPTMnet; Q7Z434; -.
PhosphoSitePlus; Q7Z434; -.
SwissPalm; Q7Z434; -.
BioMuta; MAVS; -.
DMDM; 47115748; -.
EPD; Q7Z434; -.
MaxQB; Q7Z434; -.
PaxDb; Q7Z434; -.
PeptideAtlas; Q7Z434; -.
PRIDE; Q7Z434; -.
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; CAB009187; -.
HPA; HPA049850; -.
HPA; HPA053524; -.
MIM; 609676; gene.
neXtProt; NX_Q7Z434; -.
OpenTargets; ENSG00000088888; -.
PharmGKB; PA164722208; -.
eggNOG; ENOG410IS5U; Eukaryota.
eggNOG; ENOG410Y2HK; LUCA.
GeneTree; ENSGT00510000049120; -.
HOGENOM; HOG000056441; -.
HOVERGEN; HBG079638; -.
InParanoid; Q7Z434; -.
KO; K12648; -.
OMA; EQDTELG; -.
OrthoDB; EOG091G040S; -.
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; -.
ChiTaRS; MAVS; human.
EvolutionaryTrace; Q7Z434; -.
GeneWiki; VISA_(gene); -.
GenomeRNAi; 57506; -.
PMAP-CutDB; Q7Z434; -.
PRO; PR:Q7Z434; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088888; -.
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:0004871; F:signal transducer 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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP: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:0033160; P:positive regulation of protein import into nucleus, translocation; 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:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR031964; CARD_dom.
InterPro; IPR026148; Mt_antiviral_sig_pro.
PANTHER; PTHR21446; PTHR21446; 1.
Pfam; PF16739; CARD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; 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 Mitochondrial antiviral-signaling
protein.
/FTId=PRO_0000144096.
TOPO_DOM 1 513 Cytoplasmic. {ECO:0000305}.
TRANSMEM 514 534 Helical. {ECO:0000255}.
TOPO_DOM 535 540 Mitochondrial intermembrane.
{ECO:0000305}.
DOMAIN 10 77 CARD.
REGION 10 77 Required for interaction with NLRX1.
{ECO:0000269|PubMed:18200010}.
REGION 143 147 Interaction with TRAF2.
{ECO:0000269|PubMed:16153868}.
REGION 153 158 Interaction with TRAF6.
REGION 455 460 Interaction with TRAF6.
COMPBIAS 103 153 Pro-rich.
SITE 427 428 Cleavage; by HHAV protein 3ABC.
SITE 508 509 Cleavage; by HCV and hepatitis GB virus B
NS3/4A protease complex.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 234 234 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 236 236 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VCF0}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCF0}.
VAR_SEQ 1 141 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045872.
VAR_SEQ 40 131 DRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCE
LVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPT
PAAAHSIPYN -> GPRTVPQTHWSHRHFLLRGQGPPHLLR
PTASPTTAAERRSQVTPCLSRRPRRQSPQERIQSKPCRRSA
PEPSQGIQMVAPWSPPLTWQPSAL (in isoform 6).
{ECO:0000303|PubMed:18207245}.
/FTId=VSP_047816.
VAR_SEQ 64 148 RRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPP
DPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQ
ETQ -> LPTWAGEETPGGQSSGRGLDFSSLTSGAVWLWQM
SDFWSCFSTWTVSIWLILHWVLLRLNLQVFAKCLAQSKWPL
LLPSLSCPTW (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010261.
VAR_SEQ 98 124 RTSDRPPDPLEPPSLPAERPGPPTPAA -> QFRASPADAQ
PQSHPKESRWWPPGVLL (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_047817.
VAR_SEQ 99 131 TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN -> ERPA
LALLDPQPAPWPPLSFSLSLYFLPFSVILFLVTVKR (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010262.
VAR_SEQ 125 540 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_047818.
VAR_SEQ 132 540 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18207245}.
/FTId=VSP_010263.
VAR_SEQ 149 540 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010264.
VARIANT 79 79 C -> F (in dbSNP:rs11905552).
/FTId=VAR_048609.
VARIANT 79 79 C -> S (in dbSNP:rs11908032).
/FTId=VAR_059197.
VARIANT 93 93 Q -> E (in dbSNP:rs17857295).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16153868}.
/FTId=VAR_048610.
VARIANT 198 198 Q -> K (in dbSNP:rs7262903).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16177806}.
/FTId=VAR_048611.
VARIANT 409 409 S -> F (in dbSNP:rs7269320).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16125763,
ECO:0000269|PubMed:16177806}.
/FTId=VAR_018448.
MUTAGEN 26 26 E->A,R: Impairs filament formation and
abolishes antiviral signaling activity.
{ECO:0000269|PubMed:24569476}.
MUTAGEN 54 54 T->A: Impairs ability to induce IFN-beta.
{ECO:0000269|PubMed:16125763}.
MUTAGEN 56 56 W->A,E,R: Impairs filament formation and
abolishes antiviral signaling activity.
{ECO:0000269|PubMed:24569476}.
MUTAGEN 67 69 GWV->AAA: Impairs ability to induce IFN-
beta. {ECO:0000269|PubMed:16125763}.
MUTAGEN 145 145 Q->N: No interaction with TRAF2.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 155 155 E->D: No interaction with TRAF6; when
associated with D-457.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 427 427 Q->A: No cleavage by HHAV 3ABC.
{ECO:0000269|PubMed:17438296}.
MUTAGEN 435 435 C->R: No effect on cleavage by NS3/4A
protease complex.
{ECO:0000269|PubMed:16301520}.
MUTAGEN 452 452 C->R: No effect on cleavage by NS3/4A
protease complex.
{ECO:0000269|PubMed:16301520}.
MUTAGEN 457 457 E->D: No interaction with TRAF6; when
associated with D-155.
{ECO:0000269|PubMed:16153868}.
MUTAGEN 463 463 E->A: No effect on cleavage by HHAV 3ABC.
{ECO:0000269|PubMed:17438296}.
MUTAGEN 508 508 C->A,R: No cleavage by HCV and hepatitis
GB virus B NS3/4A protease complex.
{ECO:0000269|PubMed:16177806,
ECO:0000269|PubMed:16301520,
ECO:0000269|PubMed:17093192}.
CONFLICT 42 42 L -> P (in Ref. 8; BAC77356).
{ECO:0000305}.
CONFLICT 191 191 T -> N (in Ref. 9; BAF84474).
{ECO:0000305}.
CONFLICT 356 356 A -> V (in Ref. 8; BAC77356).
{ECO:0000305}.
CONFLICT 373 373 S -> P (in Ref. 8; BAC77356).
{ECO:0000305}.
HELIX 3 14 {ECO:0000244|PDB:2VGQ}.
HELIX 16 19 {ECO:0000244|PDB:2VGQ}.
HELIX 24 27 {ECO:0000244|PDB:2VGQ}.
HELIX 28 30 {ECO:0000244|PDB:2VGQ}.
HELIX 36 49 {ECO:0000244|PDB:2VGQ}.
HELIX 51 62 {ECO:0000244|PDB:2VGQ}.
HELIX 68 78 {ECO:0000244|PDB:2VGQ}.
HELIX 82 92 {ECO:0000244|PDB:2VGQ}.
STRAND 95 97 {ECO:0000244|PDB:2MS8}.
STRAND 456 459 {ECO:0000244|PDB:4Z8M}.
STRAND 504 507 {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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