Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial antiviral-signaling protein

Gene

Mavs

Organism
Rattus norvegicus (Rat)
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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial antiviral-signaling protein
Short name:
MAVS
Alternative name(s):
Interferon beta promoter stimulator protein 1
Short name:
IPS-1
Virus-induced-signaling adapter
Short name:
VISA
Gene namesi
Name:Mavs
Synonyms:Ips1, Visa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1359371. Mavs.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 482CytoplasmicBy similarityAdd BLAST482
Transmembranei483 – 500HelicalSequence analysisAdd BLAST18
Topological domaini501 – 507Mitochondrial intermembraneBy similarity7

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440981 – 507Mitochondrial antiviral-signaling proteinAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152PhosphoserineCombined sources1
Modified residuei157PhosphoserineBy similarity1
Modified residuei172PhosphoserineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei186PhosphoserineBy similarity1
Modified residuei220PhosphoserineBy similarity1
Modified residuei234Asymmetric dimethylarginineBy similarity1
Modified residuei256PhosphoserineBy similarity1
Modified residuei387PhosphoserineBy similarity1

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

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ66HG9.
PRIDEiQ66HG9.

PTM databases

iPTMnetiQ66HG9.
PhosphoSitePlusiQ66HG9.

Expressioni

Gene expression databases

BgeeiENSRNOG00000025295.
GenevisibleiQ66HG9. RN.

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. 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 (By similarity). Interacts with ANKRD17.By similarity

Protein-protein interaction databases

IntActiQ66HG9. 1 interactor.
MINTiMINT-2841654.
STRINGi10116.ENSRNOP00000033476.

Structurei

3D structure databases

ProteinModelPortaliQ66HG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 77CARDAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 77Required for interaction with NLRX1By similarityAdd BLAST68
Regioni143 – 147Interaction with TRAF2By similarity5
Regioni153 – 158Interaction with TRAF6By similarity6
Regioni435 – 440Interaction with TRAF6By similarity6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi97 – 233Pro-richAdd BLAST137

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 288-424 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.
InParanoidiQ66HG9.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG091G040S.
PhylomeDBiQ66HG9.
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.

Q66HG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFAEEKTYK YIRYNHSKFC CVDVLEILPY LSCLTTSDQD RLRASYKQLG
60 70 80 90 100
NQGTLWELFN TLQRRPGWVE VFIRALRICE LPGLAEQVTR VYQSYLPPGA
110 120 130 140 150
SLHSLDPLQS PRIPTTVSEP SAFAAGHTIP DSGFQDKPGY PKPVQDTQPP
160 170 180 190 200
KSPVENSEEP PQANFGAIPR MSGDSLISSP NPPALSPQPS REHPEQEPEL
210 220 230 240 250
GGPSTANVDS VPIATYGPVS PTVSFQPLPR IAPRTNLSPG VTVSALSAKT
260 270 280 290 300
TLSSSSTGSA FAKGAGDQAK AATCVSTKEG VPTNSVTTSS VPSIKPVPVN
310 320 330 340 350
TMSSKLPIST KSTAATPSTV PTNIAPSKLP INSVYTGIVP SKVTASVAKA
360 370 380 390 400
SASTMPPERN NKQAKETLEA PATVVTTGSS LTRPDISSRS LHSGPELSKP
410 420 430 440 450
GVLVSQVDNE PFSACSMDLA ISPSTSLGSE PNHGPEENEY SSFRIQVDKS
460 470 480 490 500
PSVDLLGSPE PLATQQSPEE EEPCASSVSW AKWLGATSAL LAAFLAVMLY

RSRHLAQ
Length:507
Mass (Da):53,805
Last modified:October 11, 2004 - v1
Checksum:iD2924B1E34CADE47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081869 mRNA. Translation: AAH81869.1.
RefSeqiNP_001005556.1. NM_001005556.1.
XP_006235096.1. XM_006235034.3.
XP_006235097.1. XM_006235035.3.
XP_006235098.1. XM_006235036.2.
XP_008760401.1. XM_008762179.2.
UniGeneiRn.34996.

Genome annotation databases

EnsembliENSRNOT00000034146; ENSRNOP00000033476; ENSRNOG00000025295.
ENSRNOT00000090764; ENSRNOP00000073053; ENSRNOG00000025295.
GeneIDi311430.
KEGGirno:311430.
UCSCiRGD:1359371. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081869 mRNA. Translation: AAH81869.1.
RefSeqiNP_001005556.1. NM_001005556.1.
XP_006235096.1. XM_006235034.3.
XP_006235097.1. XM_006235035.3.
XP_006235098.1. XM_006235036.2.
XP_008760401.1. XM_008762179.2.
UniGeneiRn.34996.

3D structure databases

ProteinModelPortaliQ66HG9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ66HG9. 1 interactor.
MINTiMINT-2841654.
STRINGi10116.ENSRNOP00000033476.

PTM databases

iPTMnetiQ66HG9.
PhosphoSitePlusiQ66HG9.

Proteomic databases

PaxDbiQ66HG9.
PRIDEiQ66HG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000034146; ENSRNOP00000033476; ENSRNOG00000025295.
ENSRNOT00000090764; ENSRNOP00000073053; ENSRNOG00000025295.
GeneIDi311430.
KEGGirno:311430.
UCSCiRGD:1359371. rat.

Organism-specific databases

CTDi57506.
RGDi1359371. Mavs.

Phylogenomic databases

eggNOGiENOG410IS5U. Eukaryota.
ENOG410Y2HK. LUCA.
GeneTreeiENSGT00510000049120.
HOGENOMiHOG000231697.
HOVERGENiHBG079638.
InParanoidiQ66HG9.
KOiK12648.
OMAiEQDTELG.
OrthoDBiEOG091G040S.
PhylomeDBiQ66HG9.
TreeFamiTF333444.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ66HG9.

Gene expression databases

BgeeiENSRNOG00000025295.
GenevisibleiQ66HG9. RN.

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...

Entry informationi

Entry nameiMAVS_RAT
AccessioniPrimary (citable) accession number: Q66HG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. 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.