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Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA)

 MAVS_MOUSE              Reviewed;         503 AA.
Q8VCF0;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
12-SEP-2018, entry version 144.
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 {ECO:0000303|PubMed:24037184};
AltName: Full=Virus-induced-signaling adapter;
Short=VISA {ECO:0000303|PubMed:24037184};
Name=Mavs {ECO:0000312|MGI:MGI:2444773};
Synonyms=Ips1 {ECO:0000303|PubMed:24037184},
Visa {ECO:0000303|PubMed:24037184};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Eye, Liver, and Salivary gland;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
INTERACTION WITH TRAFD1.
PubMed=18849341; DOI=10.1074/jbc.M806923200;
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
Yoshimura A.;
"FLN29 deficiency reveals its negative regulatory role in the Toll-
like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
helicase signaling pathway.";
J. Biol. Chem. 283:33858-33864(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-172 AND
SER-384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH 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).
[10]
FUNCTION, AND INTERACTION WITH DHX33.
PubMed=24037184; DOI=10.1038/cmi.2013.40;
Liu Y., Lu N., Yuan B., Weng L., Wang F., Liu Y.J., Zhang Z.;
"The interaction between the helicase DHX33 and IPS-1 as a novel
pathway to sense double-stranded RNA and RNA viruses in myeloid
dendritic cells.";
Cell. Mol. Immunol. 11:49-57(2014).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-234, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Required for innate immune defense against viruses. 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). 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 (By similarity).
{ECO:0000250|UniProtKB:Q7Z434, ECO:0000269|PubMed:24037184}.
-!- 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 (By
similarity). Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6
and C1QBP. May interact with IRF3, FADD, RIPK1, IKBKE, CHUK and
IKBKB. Interacts with NLRX1. Interaction with NLRX1 requires the
CARD domain. Interacts with PSMA7. Interacts with TRAFD1.
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 NDFIP1 (By similarity).
Interacts with SMURF1; the interaction is mediated by NDFIP1 and
leads to MAVS ubiquitination and degradation (PubMed:23087404).
Interacts (via C-terminus) with GPATCH3; the interaction is
markedly increased upon viral infection (By similarity). Directly
interacts (via CARD domain) with ATG5 and ATG12, either as ATG5
and ATG12 monomers or as ATG12-ATG5 conjugates (By similarity).
Interacts with DHX33 (via the helicase C-terminal domain)
(PubMed:24037184). {ECO:0000250|UniProtKB:Q7Z434,
ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:24037184}.
-!- INTERACTION:
Q60803:Traf3; NbExp=4; IntAct=EBI-3862816, EBI-520135;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q7Z434}. Mitochondrion
{ECO:0000250|UniProtKB:Q7Z434}. Peroxisome
{ECO:0000250|UniProtKB:Q7Z434}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q7Z434}.
-!- DOMAIN: The transmembrane domain and residues 285-420 are
essential for its interaction with DHX58/LGP2.
{ECO:0000250|UniProtKB:Q7Z434}.
-!- PTM: Ubiquitinated. 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. Ubiquitinated by RNF125, leading to its degradation
by the proteasome. Undergoes 'Lys-48'-linked ubiquitination
catalyzed by SMURF1. {ECO:0000250|UniProtKB:Q7Z434}.
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EMBL; DQ174271; AAZ80418.1; -; mRNA.
EMBL; DQ167127; ABA54891.1; -; mRNA.
EMBL; AK028421; BAC25940.1; -; mRNA.
EMBL; BC020006; AAH20006.1; -; mRNA.
EMBL; BC025825; AAH25825.1; -; mRNA.
EMBL; BC031352; AAH31352.1; -; mRNA.
EMBL; BC037391; AAH37391.1; -; mRNA.
CCDS; CCDS16760.1; -.
RefSeq; NP_001193314.1; NM_001206385.1.
RefSeq; NP_659137.1; NM_144888.2.
UniGene; Mm.287226; -.
PDB; 4GHU; X-ray; 2.20 A; B=138-158.
PDBsum; 4GHU; -.
ProteinModelPortal; Q8VCF0; -.
SMR; Q8VCF0; -.
BioGrid; 230748; 9.
DIP; DIP-43890N; -.
IntAct; Q8VCF0; 6.
MINT; Q8VCF0; -.
STRING; 10090.ENSMUSP00000038339; -.
iPTMnet; Q8VCF0; -.
PhosphoSitePlus; Q8VCF0; -.
SwissPalm; Q8VCF0; -.
EPD; Q8VCF0; -.
MaxQB; Q8VCF0; -.
PaxDb; Q8VCF0; -.
PeptideAtlas; Q8VCF0; -.
PRIDE; Q8VCF0; -.
Ensembl; ENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
Ensembl; ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
GeneID; 228607; -.
KEGG; mmu:228607; -.
UCSC; uc008mld.2; mouse.
CTD; 57506; -.
MGI; MGI:2444773; Mavs.
eggNOG; ENOG410IS5U; Eukaryota.
eggNOG; ENOG410Y2HK; LUCA.
GeneTree; ENSGT00510000049120; -.
HOGENOM; HOG000231697; -.
HOVERGEN; HBG079638; -.
InParanoid; Q8VCF0; -.
KO; K12648; -.
OMA; EQDTELG; -.
OrthoDB; EOG091G040S; -.
PhylomeDB; Q8VCF0; -.
TreeFam; TF333444; -.
Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
ChiTaRS; Mavs; mouse.
PRO; PR:Q8VCF0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000037523; Expressed in 261 organ(s), highest expression level in brown adipose tissue.
CleanEx; MM_D430028G21RIK; -.
ExpressionAtlas; Q8VCF0; baseline and differential.
Genevisible; Q8VCF0; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0035591; F:signaling adaptor activity; IMP:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; ISO:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0071660; P:positive regulation of IP-10 production; ISO:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:MGI.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0039529; P:RIG-I signaling pathway; IGI:MGI.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
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; Antiviral defense; Complete proteome; Immunity;
Innate immunity; Membrane; Methylation; Mitochondrion;
Mitochondrion outer membrane; Peroxisome; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 503 Mitochondrial antiviral-signaling
protein.
/FTId=PRO_0000144097.
TOPO_DOM 1 478 Cytoplasmic. {ECO:0000305}.
TRANSMEM 479 496 Helical. {ECO:0000255}.
TOPO_DOM 497 503 Mitochondrial intermembrane.
{ECO:0000305}.
DOMAIN 10 77 CARD.
REGION 10 77 Required for interaction with NLRX1.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 143 147 Interaction with TRAF2.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 153 158 Interaction with TRAF6 1.
{ECO:0000250|UniProtKB:Q7Z434}.
REGION 337 503 Interaction with DHX33.
{ECO:0000269|PubMed:24037184}.
REGION 431 436 Interaction with TRAF6 2.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 234 234 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z434}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
SEQUENCE 503 AA; 53399 MW; FE4CA1920772BF3E CRC64;
MTFAEDKTYK YIRDNHSKFC CVDVLEILPY LSCLTASDQD RLRASYRQIG NRDTLWGLFN
NLQRRPGWVE VFIRALQICE LPGLADQVTR VYQSYLPPGT SLRSLEPLQL PDFPAAVSGP
SAFAPGHNIP DHGLRETPSC PKPVQDTQPP ESPVENSEQL LQTNSGAVAR MSGGSLIPSP
NQQALSPQPS REHQEQEPEL GGAHAANVAS VPIATYGPVS PTVSFQPLPR TALRTNLLSG
VTVSALSADT SLSSSSTGSA FAKGAGDQAK AATCFSTTLT NSVTTSSVPS PRLVPVKTMS
SKLPLSSKST AAMTSTVLTN TAPSKLPSNS VYAGTVPSRV PASVAKAPAN TIPPERNSKQ
AKETPEGPAT KVTTGGNQTG PNSSIRSLHS GPEMSKPGVL VSQLDEPFSA CSVDLAISPS
SSLVSEPNHG PEENEYSSFR IQVDESPSAD LLGSPEPLAT QQPQEEEEHC ASSMPWAKWL
GATSALLAVF LAVMLYRSRR LAQ


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