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Protein

Mitochondrial antiviral-signaling protein

Gene

Mavs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  • CARD domain binding Source: MGI
  • protein kinase binding Source: MGI
  • signal transducer activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial antiviral-signaling protein
Short name:
MAVS
Alternative name(s):
CARD adapter inducing interferon beta
Short name:
Cardif
Interferon beta promoter stimulator protein 1
Short name:
IPS-1
Virus-induced-signaling adapter
Short name:
VISA
Gene namesi
Name:Mavs
Synonyms:Ips1, Visa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2444773. Mavs.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 478478CytoplasmicBy similarityAdd
BLAST
Transmembranei479 – 49618HelicalSequence analysisAdd
BLAST
Topological domaini497 – 5037Mitochondrial intermembraneBy similarity

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial membrane Source: MGI
  • mitochondrial outer membrane Source: MGI
  • mitochondrion Source: UniProtKB
  • peroxisomal membrane Source: MGI
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Mitochondrial antiviral-signaling proteinPRO_0000144097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei251 – 2511PhosphoserineBy similarity
Modified residuei256 – 2561PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineCombined sources

Post-translational modificationi

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.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VCF0.
MaxQBiQ8VCF0.
PaxDbiQ8VCF0.
PRIDEiQ8VCF0.

PTM databases

iPTMnetiQ8VCF0.
PhosphoSiteiQ8VCF0.
SwissPalmiQ8VCF0.

Expressioni

Gene expression databases

BgeeiQ8VCF0.
CleanExiMM_D430028G21RIK.
ExpressionAtlasiQ8VCF0. baseline and differential.
GenevisibleiQ8VCF0. MM.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Traf3Q608034EBI-3862816,EBI-520135

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230748. 7 interactions.
IntActiQ8VCF0. 4 interactions.
MINTiMINT-2839937.
STRINGi10090.ENSMUSP00000038339.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GHUX-ray2.20B138-158[»]
ProteinModelPortaliQ8VCF0.
SMRiQ8VCF0. Positions 1-93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 7768CARDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 7768Required for interaction with NLRX1By similarityAdd
BLAST
Regioni143 – 1475Interaction with TRAF2By similarity
Regioni153 – 1586Interaction with TRAF6 1By similarity
Regioni431 – 4366Interaction with TRAF6 2By similarity

Domaini

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).By similarity
The transmembrane domain and residues 285-420 are essential for its interaction with DHX58/LGP2.By similarity

Sequence similaritiesi

Contains 1 CARD domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IS5U. Eukaryota.
ENOG410Y2HK. LUCA.
GeneTreeiENSGT00510000049120.
HOGENOMiHOG000231697.
HOVERGENiHBG079638.
InParanoidiQ8VCF0.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG71ZP2Z.
PhylomeDBiQ8VCF0.
TreeFamiTF333444.

Family and domain databases

InterProiIPR031964. CARD_dom.
IPR026148. Mt_antiviral_sig_pro.
[Graphical view]
PANTHERiPTHR21446. PTHR21446. 2 hits.
PfamiPF16739. CARD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VCF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFAEDKTYK YIRDNHSKFC CVDVLEILPY LSCLTASDQD RLRASYRQIG
60 70 80 90 100
NRDTLWGLFN NLQRRPGWVE VFIRALQICE LPGLADQVTR VYQSYLPPGT
110 120 130 140 150
SLRSLEPLQL PDFPAAVSGP SAFAPGHNIP DHGLRETPSC PKPVQDTQPP
160 170 180 190 200
ESPVENSEQL LQTNSGAVAR MSGGSLIPSP NQQALSPQPS REHQEQEPEL
210 220 230 240 250
GGAHAANVAS VPIATYGPVS PTVSFQPLPR TALRTNLLSG VTVSALSADT
260 270 280 290 300
SLSSSSTGSA FAKGAGDQAK AATCFSTTLT NSVTTSSVPS PRLVPVKTMS
310 320 330 340 350
SKLPLSSKST AAMTSTVLTN TAPSKLPSNS VYAGTVPSRV PASVAKAPAN
360 370 380 390 400
TIPPERNSKQ AKETPEGPAT KVTTGGNQTG PNSSIRSLHS GPEMSKPGVL
410 420 430 440 450
VSQLDEPFSA CSVDLAISPS SSLVSEPNHG PEENEYSSFR IQVDESPSAD
460 470 480 490 500
LLGSPEPLAT QQPQEEEEHC ASSMPWAKWL GATSALLAVF LAVMLYRSRR

LAQ
Length:503
Mass (Da):53,399
Last modified:March 1, 2002 - v1
Checksum:iFE4CA1920772BF3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ174271 mRNA. Translation: AAZ80418.1.
DQ167127 mRNA. Translation: ABA54891.1.
AK028421 mRNA. Translation: BAC25940.1.
BC020006 mRNA. Translation: AAH20006.1.
BC025825 mRNA. Translation: AAH25825.1.
BC031352 mRNA. Translation: AAH31352.1.
BC037391 mRNA. Translation: AAH37391.1.
CCDSiCCDS16760.1.
RefSeqiNP_001193314.1. NM_001206385.1.
NP_659137.1. NM_144888.2.
UniGeneiMm.287226.

Genome annotation databases

EnsembliENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
GeneIDi228607.
KEGGimmu:228607.
UCSCiuc008mld.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ174271 mRNA. Translation: AAZ80418.1.
DQ167127 mRNA. Translation: ABA54891.1.
AK028421 mRNA. Translation: BAC25940.1.
BC020006 mRNA. Translation: AAH20006.1.
BC025825 mRNA. Translation: AAH25825.1.
BC031352 mRNA. Translation: AAH31352.1.
BC037391 mRNA. Translation: AAH37391.1.
CCDSiCCDS16760.1.
RefSeqiNP_001193314.1. NM_001206385.1.
NP_659137.1. NM_144888.2.
UniGeneiMm.287226.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GHUX-ray2.20B138-158[»]
ProteinModelPortaliQ8VCF0.
SMRiQ8VCF0. Positions 1-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230748. 7 interactions.
IntActiQ8VCF0. 4 interactions.
MINTiMINT-2839937.
STRINGi10090.ENSMUSP00000038339.

PTM databases

iPTMnetiQ8VCF0.
PhosphoSiteiQ8VCF0.
SwissPalmiQ8VCF0.

Proteomic databases

EPDiQ8VCF0.
MaxQBiQ8VCF0.
PaxDbiQ8VCF0.
PRIDEiQ8VCF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
GeneIDi228607.
KEGGimmu:228607.
UCSCiuc008mld.2. mouse.

Organism-specific databases

CTDi57506.
MGIiMGI:2444773. Mavs.

Phylogenomic databases

eggNOGiENOG410IS5U. Eukaryota.
ENOG410Y2HK. LUCA.
GeneTreeiENSGT00510000049120.
HOGENOMiHOG000231697.
HOVERGENiHBG079638.
InParanoidiQ8VCF0.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG71ZP2Z.
PhylomeDBiQ8VCF0.
TreeFamiTF333444.

Enzyme and pathway databases

ReactomeiR-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiMavs. mouse.
NextBioi379056.
PROiQ8VCF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCF0.
CleanExiMM_D430028G21RIK.
ExpressionAtlasiQ8VCF0. baseline and differential.
GenevisibleiQ8VCF0. MM.

Family and domain databases

InterProiIPR031964. CARD_dom.
IPR026148. Mt_antiviral_sig_pro.
[Graphical view]
PANTHERiPTHR21446. PTHR21446. 2 hits.
PfamiPF16739. CARD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."
    Seth R.B., Sun L., Ea C.-K., Chen Z.J.
    Cell 122:669-682(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
    Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
    Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus."
    Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J.
    Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Eye, Liver and Salivary gland.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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."
    Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.
    J. Biol. Chem. 283:33858-33864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAFD1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-172 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMAVS_MOUSE
AccessioniPrimary (citable) accession number: Q8VCF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.