MAVS_MOUSE
ID MAVS_MOUSE Reviewed; 503 AA.
AC Q8VCF0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mitochondrial antiviral-signaling protein {ECO:0000305};
DE Short=MAVS {ECO:0000305};
DE AltName: Full=CARD adapter inducing interferon beta;
DE Short=Cardif;
DE AltName: Full=Interferon beta promoter stimulator protein 1;
DE Short=IPS-1 {ECO:0000303|PubMed:24037184};
DE AltName: Full=Virus-induced-signaling adapter;
DE Short=VISA {ECO:0000303|PubMed:24037184};
GN Name=Mavs {ECO:0000312|MGI:MGI:2444773};
GN Synonyms=Ips1 {ECO:0000303|PubMed:24037184},
GN Visa {ECO:0000303|PubMed:24037184};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
RA Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
RT "Identification and characterization of MAVS, a mitochondrial antiviral
RT signaling protein that activates NF-kappaB and IRF 3.";
RL Cell 122:669-682(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
RA Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
RT "VISA is an adapter protein required for virus-triggered IFN-beta
RT Signaling.";
RL Mol. Cell 19:727-740(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16177806; DOI=10.1038/nature04193;
RA Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
RA Bartenschlager R., Tschopp J.;
RT "Cardif is an adaptor protein in the RIG-I antiviral pathway and is
RT targeted by hepatitis C virus.";
RL Nature 437:1167-1172(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, Liver, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP INTERACTION WITH TRAFD1.
RX PubMed=18849341; DOI=10.1074/jbc.m806923200;
RA Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.;
RT "FLN29 deficiency reveals its negative regulatory role in the Toll-like
RT receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase
RT signaling pathway.";
RL J. Biol. Chem. 283:33858-33864(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-172 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH SMURF1.
RX PubMed=23087404; DOI=10.4049/jimmunol.1201445;
RA Wang Y., Tong X., Ye X.;
RT "Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing
RT E3 ligase Smurf1-mediated MAVS degradation.";
RL J. Immunol. 189:5304-5313(2012).
RN [10]
RP FUNCTION, AND INTERACTION WITH DHX33.
RX PubMed=24037184; DOI=10.1038/cmi.2013.40;
RA Liu Y., Lu N., Yuan B., Weng L., Wang F., Liu Y.J., Zhang Z.;
RT "The interaction between the helicase DHX33 and IPS-1 as a novel pathway to
RT sense double-stranded RNA and RNA viruses in myeloid dendritic cells.";
RL Cell. Mol. Immunol. 11:49-57(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-234, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP INTERACTION WITH ZNFX1.
RX PubMed=31685995; DOI=10.1038/s41556-019-0416-0;
RA Wang Y., Yuan S., Jia X., Ge Y., Ling T., Nie M., Lan X., Chen S., Xu A.;
RT "Mitochondria-localised ZNFX1 functions as a dsRNA sensor to initiate
RT antiviral responses through MAVS.";
RL Nat. Cell Biol. 21:1346-1356(2019).
CC -!- FUNCTION: Required for innate immune defense against viruses
CC (PubMed:24037184). Acts downstream of DHX33, DDX58/RIG-I and
CC IFIH1/MDA5, which detect intracellular dsRNA produced during viral
CC replication, to coordinate pathways leading to the activation of NF-
CC kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral
CC cytokines such as IFN-beta and RANTES (CCL5) (PubMed:24037184).
CC Peroxisomal and mitochondrial MAVS act sequentially to create an
CC antiviral cellular state (By similarity). Upon viral infection,
CC peroxisomal MAVS induces the rapid interferon-independent expression of
CC defense factors that provide short-term protection, whereas
CC mitochondrial MAVS activates an interferon-dependent signaling pathway
CC with delayed kinetics, which amplifies and stabilizes the antiviral
CC response (By similarity). May activate the same pathways following
CC detection of extracellular dsRNA by TLR3 (By similarity). May protect
CC cells from apoptosis (By similarity). {ECO:0000250|UniProtKB:Q7Z434,
CC ECO:0000269|PubMed:24037184}.
CC -!- SUBUNIT: Self-associates and polymerizes (via CARD domains) to form 400
CC nM long three-stranded helical filaments on mitochondria, filament
CC nucleation requires interaction with DDX58/RIG-I whose CARD domains act
CC as a template for filament assembly (By similarity). Interacts with
CC DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP (By similarity). May
CC interact with FADD, RIPK1, IKBKE, CHUK and IKBKB (By similarity).
CC Interacts (when phosphorylated) with IRF3; following activation and
CC phosphorylation on the pLxIS motif by TBK1, recruits IRF3 (By
CC similarity). Interacts with NLRX1 (By similarity). Interaction with
CC NLRX1 requires the CARD domain (By similarity). Interacts with PSMA7
CC (By similarity). Interacts with TRAFD1 (PubMed:18849341). Interacts
CC (via C-terminus) with PCBP2 in a complex containing MAVS/IPS1, PCBP2
CC and ITCH (By similarity). Interacts with CYLD (By similarity).
CC Interacts with SRC (By similarity). Interacts with DHX58/LGP2 and IKBKE
CC (By similarity). Interacts with STING1 (By similarity). Interacts with
CC IFIT3 (via N-terminus) (By similarity). Interacts with TBK1 only in the
CC presence of IFIT3 (By similarity). Interacts with TTLL12; the
CC interaction prevents MAVS binding to TBK1 and IKBKE (By similarity).
CC Interacts with MUL1 (By similarity). Interacts with ANKRD17 (By
CC similarity). Interacts with NDFIP1 (By similarity). Interacts with
CC SMURF1; the interaction is mediated by NDFIP1 and leads to MAVS
CC ubiquitination and degradation (PubMed:23087404). Interacts (via C-
CC terminus) with GPATCH3; the interaction is markedly increased upon
CC viral infection (By similarity). Directly interacts (via CARD domain)
CC with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5
CC conjugates (By similarity). Interacts with DHX33 (via the helicase C-
CC terminal domain) (PubMed:24037184). Interacts with DDX3X (via C-
CC terminus); this interaction may occur rapidly, but transiently after
CC viral infection (By similarity). The interaction with DDX3X potentiates
CC MAVS-mediated IFNB induction (By similarity). Conversely inhibition of
CC this interaction prevents MAVS-mediated IFNB induction (By similarity).
CC Transiently interacts with TRAF3 early during viral infection (By
CC similarity). Interacts with CLPB (By similarity). Interacts with
CC TRAF3IP3 (By similarity). Interacts with TOMM70; the interaction is
CC enhanced by virus infection (By similarity). Interacts with ZNFX1
CC (PubMed:31685995). Interacts with DHX15 (By similarity). Interacts with
CC N4BP3; this interaction promotes the polyubiquitination of MAVS (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z434,
CC ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:23087404,
CC ECO:0000269|PubMed:24037184, ECO:0000269|PubMed:31685995}.
CC -!- INTERACTION:
CC Q8VCF0; Q60803: Traf3; NbExp=4; IntAct=EBI-3862816, EBI-520135;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q7Z434}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q7Z434}. Peroxisome
CC {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- DOMAIN: Both CARD and transmembrane domains are essential for antiviral
CC function. The CARD domain is responsible for interaction with
CC DDX58/RIG-I and IFIH1/MDA5 (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- DOMAIN: The transmembrane domain and residues 285-420 are essential for
CC its interaction with DHX58/LGP2. {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif: following
CC phosphorylation by TBK1, the phosphorylated pLxIS motif of MAVS
CC recruits IRF3. IRF3 is then phosphorylated and activated by TBK1 to
CC induce type-I interferons and other cytokines.
CC {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- DOMAIN: Both CARD and transmembrane domains are essential for antiviral
CC function. The CARD domain is responsible for interaction with
CC DDX58/RIG-I and IFIH1/MDA5. {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- DOMAIN: The transmembrane domain and residues 300-444 are essential for
CC its interaction with DHX58/LGP2. {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- PTM: Following activation, phosphorylated by TBK1 at Ser-418 in the
CC pLxIS motif. The phosphorylated pLxIS motif constitutes an IRF3-binding
CC motif, leading to recruitment of the transcription factor IRF3 to
CC induce type-I interferons and other cytokines.
CC {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- PTM: Ubiquitinated. Undergoes 'Lys-48'-linked polyubiquitination
CC catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated by the
CC interaction with PCBP2 and leads to MAVS/IPS1 proteasomal degradation.
CC Ubiquitinated by RNF125, leading to its degradation by the proteasome.
CC Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1. Undergoes
CC 'Lys-63'-linked ubiquitination leading to enhanced interaction between
CC MAVS and TRAF2. {ECO:0000250|UniProtKB:Q7Z434}.
CC -!- PTM: Proteolytically cleaved by apoptotic caspases during apoptosis,
CC leading to its inactivation. Cleavage by CASP3 during virus-induced
CC apoptosis inactivates it, preventing cytokine overproduction.
CC {ECO:0000250|UniProtKB:Q7Z434}.
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DR EMBL; DQ174271; AAZ80418.1; -; mRNA.
DR EMBL; DQ167127; ABA54891.1; -; mRNA.
DR EMBL; AK028421; BAC25940.1; -; mRNA.
DR EMBL; BC020006; AAH20006.1; -; mRNA.
DR EMBL; BC025825; AAH25825.1; -; mRNA.
DR EMBL; BC031352; AAH31352.1; -; mRNA.
DR EMBL; BC037391; AAH37391.1; -; mRNA.
DR CCDS; CCDS16760.1; -.
DR RefSeq; NP_001193314.1; NM_001206385.1.
DR RefSeq; NP_659137.1; NM_144888.2.
DR PDB; 4GHU; X-ray; 2.20 A; B=138-158.
DR PDBsum; 4GHU; -.
DR AlphaFoldDB; Q8VCF0; -.
DR SMR; Q8VCF0; -.
DR BioGRID; 230748; 30.
DR DIP; DIP-43890N; -.
DR IntAct; Q8VCF0; 5.
DR MINT; Q8VCF0; -.
DR STRING; 10090.ENSMUSP00000105828; -.
DR iPTMnet; Q8VCF0; -.
DR PhosphoSitePlus; Q8VCF0; -.
DR SwissPalm; Q8VCF0; -.
DR EPD; Q8VCF0; -.
DR jPOST; Q8VCF0; -.
DR MaxQB; Q8VCF0; -.
DR PaxDb; Q8VCF0; -.
DR PeptideAtlas; Q8VCF0; -.
DR PRIDE; Q8VCF0; -.
DR ProteomicsDB; 292272; -.
DR Antibodypedia; 3363; 678 antibodies from 43 providers.
DR DNASU; 228607; -.
DR Ensembl; ENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
DR Ensembl; ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
DR GeneID; 228607; -.
DR KEGG; mmu:228607; -.
DR UCSC; uc008mld.2; mouse.
DR CTD; 57506; -.
DR MGI; MGI:2444773; Mavs.
DR VEuPathDB; HostDB:ENSMUSG00000037523; -.
DR eggNOG; ENOG502SAUA; Eukaryota.
DR GeneTree; ENSGT00510000049120; -.
DR HOGENOM; CLU_042052_0_0_1; -.
DR InParanoid; Q8VCF0; -.
DR OMA; CVYQSYQ; -.
DR OrthoDB; 887440at2759; -.
DR PhylomeDB; Q8VCF0; -.
DR TreeFam; TF333444; -.
DR Reactome; R-MMU-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
DR BioGRID-ORCS; 228607; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Mavs; mouse.
DR PRO; PR:Q8VCF0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VCF0; protein.
DR Bgee; ENSMUSG00000037523; Expressed in epithelium of small intestine and 235 other tissues.
DR ExpressionAtlas; Q8VCF0; baseline and differential.
DR Genevisible; Q8VCF0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IMP:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; ISO:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0071660; P:positive regulation of IP-10 production; ISO:MGI.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IMP:MGI.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR CDD; cd08811; CARD_IPS1; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR031964; CARD_dom.
DR InterPro; IPR042144; CARD_IPS1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR026148; Mt_antiviral_sig_pro_met.
DR PANTHER; PTHR21446:SF6; PTHR21446:SF6; 1.
DR Pfam; PF16739; CARD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Immunity; Innate immunity; Membrane;
KW Methylation; Mitochondrion; Mitochondrion outer membrane; Peroxisome;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..503
FT /note="Mitochondrial antiviral-signaling protein"
FT /id="PRO_0000144097"
FT TOPO_DOM 1..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 479..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..503
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 10..77
FT /note="CARD"
FT REGION 10..77
FT /note="Required for interaction with NLRX1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT REGION 119..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..147
FT /note="Interaction with TRAF2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT REGION 153..158
FT /note="Interaction with TRAF6 1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT REGION 337..503
FT /note="Interaction with DHX33"
FT /evidence="ECO:0000269|PubMed:24037184"
FT REGION 346..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..436
FT /note="Interaction with TRAF6 2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 415..418
FT /note="pLxIS motif"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT COMPBIAS 149..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 405..406
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 234
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z434"
SQ 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
