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Protein

Radical S-adenosyl methionine domain-containing protein 2

Gene

Rsad2

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

Functioni

Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of viruses, including west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus and vesicular stomatitis virus (VSV). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphospate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.4 Publications

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi88 – 881Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi91 – 911Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

GO - Biological processi

  • CD4-positive, alpha-beta T cell activation Source: UniProtKB
  • CD4-positive, alpha-beta T cell differentiation Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • negative regulation of protein secretion Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
  • positive regulation of toll-like receptor 7 signaling pathway Source: UniProtKB
  • positive regulation of toll-like receptor 9 signaling pathway Source: UniProtKB
  • response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Radical S-adenosyl methionine domain-containing protein 2
Alternative name(s):
Viperin
Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
Gene namesi
Name:Rsad2Imported
Synonyms:Vig1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1929628. Rsad2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: CACAO
  • endoplasmic reticulum membrane Source: UniProtKB
  • lipid particle Source: UniProtKB
  • mitochondrial inner membrane Source: MGI
  • mitochondrial outer membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Radical S-adenosyl methionine domain-containing protein 2PRO_0000309584Add
BLAST

Proteomic databases

MaxQBiQ8CBB9.
PaxDbiQ8CBB9.
PRIDEiQ8CBB9.

PTM databases

iPTMnetiQ8CBB9.
PhosphoSiteiQ8CBB9.

Expressioni

Tissue specificityi

Expressed at higher levels in atherosclerotic arteries than in normal arteries.1 Publication

Inductioni

By interferon type I, type II and LPS. Induced by infection with Vesicular stomatitis virus and pseudorabies virus in dendritic cells, presumably through type I interferon pathway.2 Publications

Gene expression databases

BgeeiQ8CBB9.
CleanExiMM_RSAD2.
ExpressionAtlasiQ8CBB9. baseline and differential.
GenevisibleiQ8CBB9. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with FPPS (By similarity). Interacts (via C-terminus) with VAPA/VAP33 (via C-terminus) and inhibits its interaction with hepatitis virus C (HCV) protein NS5A. Interacts with HADHB (By similarity). Interacts with IRAK1 and TRAF6.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208378. 5 interactions.
STRINGi10090.ENSMUSP00000020970.

Structurei

3D structure databases

ProteinModelPortaliQ8CBB9.
SMRiQ8CBB9. Positions 79-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal region (1-43) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet.

Sequence similaritiesi

Belongs to the radical SAM superfamily. RSAD2 family.Curated

Phylogenomic databases

eggNOGiENOG410IGZE. Eukaryota.
ENOG410XQM5. LUCA.
GeneTreeiENSGT00390000013670.
HOVERGENiHBG053099.
InParanoidiQ8CBB9.
KOiK15045.
OMAiINRFNVE.
OrthoDBiEOG7FFMRW.
PhylomeDBiQ8CBB9.
TreeFamiTF300085.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
IPR026372. Viperin.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04278. viperin. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CBB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMLVPTALA ARLLSLFQQQ LGSLWSGLAI LFCWLRIALG WLDPGKEQPQ
60 70 80 90 100
VRGEPEDTQE TQEDGNSTQP TTPVSVNYHF TRQCNYKCGF CFHTAKTSFV
110 120 130 140 150
LPLEEAKRGL LLLKQAGLEK INFSGGEPFL QDRGEYLGKL VRFCKEELAL
160 170 180 190 200
PSVSIVSNGS LIRERWFKDY GEYLDILAIS CDSFDEQVNA LIGRGQGKKN
210 220 230 240 250
HVENLQKLRR WCRDYKVAFK INSVINRFNV DEDMNEHIKA LSPVRWKVFQ
260 270 280 290 300
CLLIEGENSG EDALREAERF LISNEEFETF LERHKEVSCL VPESNQKMKD
310 320 330 340 350
SYLILDEYMR FLNCTGGRKD PSKSILDVGV EEAIKFSGFD EKMFLKRGGK
360
YVWSKADLKL DW
Length:362
Mass (Da):41,524
Last modified:March 1, 2003 - v1
Checksum:iF56F0BBEC9F20E50
GO

Sequence cautioni

The sequence BAE29281.1 differs from that shown. Reason: Erroneous termination at position 46. Translated as Lys.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151S → R in BAE31578 (PubMed:16141072).Curated
Sequence conflicti15 – 151S → R in BAE30379 (PubMed:16141072).Curated
Sequence conflicti15 – 151S → R in BAE29807 (PubMed:16141072).Curated
Sequence conflicti15 – 151S → R in BAE29764 (PubMed:16141072).Curated
Sequence conflicti26 – 261S → C in BAE30676 (PubMed:16141072).Curated
Sequence conflicti26 – 261S → G in BAE31898 (PubMed:16141072).Curated
Sequence conflicti26 – 261S → G in BAE31903 (PubMed:16141072).Curated
Sequence conflicti52 – 521R → P in BAE30920 (PubMed:16141072).Curated
Sequence conflicti55 – 551P → L in AAF60314 (PubMed:11038379).Curated
Sequence conflicti55 – 551P → L in CAJ18585 (Ref. 3) Curated
Sequence conflicti55 – 551P → L in AAH57868 (PubMed:15489334).Curated
Sequence conflicti55 – 551P → L in AAL50054 (PubMed:11752458).Curated
Sequence conflicti57 – 571D → E in AAF60314 (PubMed:11038379).Curated
Sequence conflicti57 – 571D → E in CAJ18585 (Ref. 3) Curated
Sequence conflicti57 – 571D → E in AAH57868 (PubMed:15489334).Curated
Sequence conflicti57 – 571D → E in AAL50054 (PubMed:11752458).Curated
Sequence conflicti70 – 701P → R in AAF60314 (PubMed:11038379).Curated
Sequence conflicti70 – 701P → R in CAJ18585 (Ref. 3) Curated
Sequence conflicti70 – 701P → R in AAH57868 (PubMed:15489334).Curated
Sequence conflicti70 – 701P → R in AAL50054 (PubMed:11752458).Curated
Sequence conflicti73 – 731P → T in BAE31898 (PubMed:16141072).Curated
Sequence conflicti94 – 941T → K in BAE30826 (PubMed:16141072).Curated
Sequence conflicti94 – 941T → K in BAE32092 (PubMed:16141072).Curated
Sequence conflicti125 – 1251G → E in BAE29848 (PubMed:16141072).Curated
Sequence conflicti148 – 1481L → Q in BAE31064 (PubMed:16141072).Curated
Sequence conflicti149 – 1491A → S in BAE30826 (PubMed:16141072).Curated
Sequence conflicti163 – 1631R → Q in AAF60314 (PubMed:11038379).Curated
Sequence conflicti163 – 1631R → Q in AAL50054 (PubMed:11752458).Curated
Sequence conflicti211 – 2111W → R in BAE31565 (PubMed:16141072).Curated
Sequence conflicti211 – 2111W → R in BAE31383 (PubMed:16141072).Curated
Sequence conflicti211 – 2111W → R in BAE30737 (PubMed:16141072).Curated
Sequence conflicti241 – 2411L → Q in BAE31898 (PubMed:16141072).Curated
Sequence conflicti241 – 2411L → Q in BAE31903 (PubMed:16141072).Curated
Sequence conflicti247 – 2471K → E in BAE30673 (PubMed:16141072).Curated
Sequence conflicti247 – 2471K → E in BAE30203 (PubMed:16141072).Curated
Sequence conflicti262 – 2621D → G in BAE30726 (PubMed:16141072).Curated
Sequence conflicti270 – 2701F → L in BAE31348 (PubMed:16141072).Curated
Sequence conflicti273 – 2731S → G in BAE31064 (PubMed:16141072).Curated
Sequence conflicti339 – 3391F → Y in BAE30676 (PubMed:16141072).Curated
Sequence conflicti339 – 3391F → Y in BAE30787 (PubMed:16141072).Curated
Sequence conflicti339 – 3391F → Y in BAE30790 (PubMed:16141072).Curated
Sequence conflicti339 – 3391F → Y in BAE30920 (PubMed:16141072).Curated
Sequence conflicti339 – 3391F → Y in BAE30927 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236064 mRNA. Translation: AAF60314.2.
AK036373 mRNA. Translation: BAC29401.1.
AK150069 mRNA. Translation: BAE29281.1. Sequence problems.
AK150406 mRNA. Translation: BAE29532.1.
AK150425 mRNA. Translation: BAE29548.1.
AK150525 mRNA. Translation: BAE29636.1.
AK150616 mRNA. Translation: BAE29706.1.
AK150684 mRNA. Translation: BAE29764.1.
AK150731 mRNA. Translation: BAE29807.1.
AK150767 mRNA. Translation: BAE29833.1.
AK150783 mRNA. Translation: BAE29848.1.
AK150788 mRNA. Translation: BAE29852.1.
AK150812 mRNA. Translation: BAE29875.1.
AK150835 mRNA. Translation: BAE29895.1.
AK151140 mRNA. Translation: BAE30147.1.
AK151185 mRNA. Translation: BAE30184.1.
AK151191 mRNA. Translation: BAE30188.1.
AK151206 mRNA. Translation: BAE30203.1.
AK151286 mRNA. Translation: BAE30271.1.
AK151308 mRNA. Translation: BAE30290.1.
AK151339 mRNA. Translation: BAE30317.1.
AK151389 mRNA. Translation: BAE30360.1.
AK151410 mRNA. Translation: BAE30375.1.
AK151412 mRNA. Translation: BAE30377.1.
AK151414 mRNA. Translation: BAE30379.1.
AK151476 mRNA. Translation: BAE30431.1.
AK151502 mRNA. Translation: BAE30453.1.
AK151538 mRNA. Translation: BAE30485.1.
AK151767 mRNA. Translation: BAE30673.1.
AK151770 mRNA. Translation: BAE30676.1.
AK151825 mRNA. Translation: BAE30722.1.
AK151833 mRNA. Translation: BAE30726.1.
AK151846 mRNA. Translation: BAE30737.1.
AK151906 mRNA. Translation: BAE30787.1.
AK151909 mRNA. Translation: BAE30790.1.
AK151940 mRNA. Translation: BAE30816.1.
AK151954 mRNA. Translation: BAE30826.1.
AK151971 mRNA. Translation: BAE30840.1.
AK152050 mRNA. Translation: BAE30906.1.
AK152065 mRNA. Translation: BAE30920.1.
AK152075 mRNA. Translation: BAE30927.1.
AK152235 mRNA. Translation: BAE31060.1.
AK152239 mRNA. Translation: BAE31062.1.
AK152241 mRNA. Translation: BAE31064.1.
AK152310 mRNA. Translation: BAE31116.1.
AK152354 mRNA. Translation: BAE31146.1.
AK152493 mRNA. Translation: BAE31264.1.
AK152600 mRNA. Translation: BAE31348.1.
AK152601 mRNA. Translation: BAE31349.1.
AK152631 mRNA. Translation: BAE31374.1.
AK152644 mRNA. Translation: BAE31383.1.
AK152664 mRNA. Translation: BAE31399.1.
AK152796 mRNA. Translation: BAE31501.1.
AK152861 mRNA. Translation: BAE31552.1.
AK152880 mRNA. Translation: BAE31565.1.
AK152895 mRNA. Translation: BAE31578.1.
AK152934 mRNA. Translation: BAE31608.1.
AK152962 mRNA. Translation: BAE31625.1.
AK153003 mRNA. Translation: BAE31643.1.
AK153024 mRNA. Translation: BAE31658.1.
AK153062 mRNA. Translation: BAE31688.1.
AK153077 mRNA. Translation: BAE31702.1.
AK153078 mRNA. Translation: BAE31703.1.
AK153232 mRNA. Translation: BAE31825.1.
AK153234 mRNA. Translation: BAE31827.1.
AK153306 mRNA. Translation: BAE31887.1.
AK153318 mRNA. Translation: BAE31898.1.
AK153324 mRNA. Translation: BAE31903.1.
AK153435 mRNA. Translation: BAE31992.1.
AK153556 mRNA. Translation: BAE32092.1.
AK159147 mRNA. Translation: BAE34854.1.
CT010378 mRNA. Translation: CAJ18585.1.
BC057868 mRNA. Translation: AAH57868.1.
AF442152 mRNA. Translation: AAL50054.1.
CCDSiCCDS25848.1.
RefSeqiNP_067359.2. NM_021384.4.
UniGeneiMm.24045.

Genome annotation databases

EnsembliENSMUST00000020970; ENSMUSP00000020970; ENSMUSG00000020641.
GeneIDi58185.
KEGGimmu:58185.
UCSCiuc007nfh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236064 mRNA. Translation: AAF60314.2.
AK036373 mRNA. Translation: BAC29401.1.
AK150069 mRNA. Translation: BAE29281.1. Sequence problems.
AK150406 mRNA. Translation: BAE29532.1.
AK150425 mRNA. Translation: BAE29548.1.
AK150525 mRNA. Translation: BAE29636.1.
AK150616 mRNA. Translation: BAE29706.1.
AK150684 mRNA. Translation: BAE29764.1.
AK150731 mRNA. Translation: BAE29807.1.
AK150767 mRNA. Translation: BAE29833.1.
AK150783 mRNA. Translation: BAE29848.1.
AK150788 mRNA. Translation: BAE29852.1.
AK150812 mRNA. Translation: BAE29875.1.
AK150835 mRNA. Translation: BAE29895.1.
AK151140 mRNA. Translation: BAE30147.1.
AK151185 mRNA. Translation: BAE30184.1.
AK151191 mRNA. Translation: BAE30188.1.
AK151206 mRNA. Translation: BAE30203.1.
AK151286 mRNA. Translation: BAE30271.1.
AK151308 mRNA. Translation: BAE30290.1.
AK151339 mRNA. Translation: BAE30317.1.
AK151389 mRNA. Translation: BAE30360.1.
AK151410 mRNA. Translation: BAE30375.1.
AK151412 mRNA. Translation: BAE30377.1.
AK151414 mRNA. Translation: BAE30379.1.
AK151476 mRNA. Translation: BAE30431.1.
AK151502 mRNA. Translation: BAE30453.1.
AK151538 mRNA. Translation: BAE30485.1.
AK151767 mRNA. Translation: BAE30673.1.
AK151770 mRNA. Translation: BAE30676.1.
AK151825 mRNA. Translation: BAE30722.1.
AK151833 mRNA. Translation: BAE30726.1.
AK151846 mRNA. Translation: BAE30737.1.
AK151906 mRNA. Translation: BAE30787.1.
AK151909 mRNA. Translation: BAE30790.1.
AK151940 mRNA. Translation: BAE30816.1.
AK151954 mRNA. Translation: BAE30826.1.
AK151971 mRNA. Translation: BAE30840.1.
AK152050 mRNA. Translation: BAE30906.1.
AK152065 mRNA. Translation: BAE30920.1.
AK152075 mRNA. Translation: BAE30927.1.
AK152235 mRNA. Translation: BAE31060.1.
AK152239 mRNA. Translation: BAE31062.1.
AK152241 mRNA. Translation: BAE31064.1.
AK152310 mRNA. Translation: BAE31116.1.
AK152354 mRNA. Translation: BAE31146.1.
AK152493 mRNA. Translation: BAE31264.1.
AK152600 mRNA. Translation: BAE31348.1.
AK152601 mRNA. Translation: BAE31349.1.
AK152631 mRNA. Translation: BAE31374.1.
AK152644 mRNA. Translation: BAE31383.1.
AK152664 mRNA. Translation: BAE31399.1.
AK152796 mRNA. Translation: BAE31501.1.
AK152861 mRNA. Translation: BAE31552.1.
AK152880 mRNA. Translation: BAE31565.1.
AK152895 mRNA. Translation: BAE31578.1.
AK152934 mRNA. Translation: BAE31608.1.
AK152962 mRNA. Translation: BAE31625.1.
AK153003 mRNA. Translation: BAE31643.1.
AK153024 mRNA. Translation: BAE31658.1.
AK153062 mRNA. Translation: BAE31688.1.
AK153077 mRNA. Translation: BAE31702.1.
AK153078 mRNA. Translation: BAE31703.1.
AK153232 mRNA. Translation: BAE31825.1.
AK153234 mRNA. Translation: BAE31827.1.
AK153306 mRNA. Translation: BAE31887.1.
AK153318 mRNA. Translation: BAE31898.1.
AK153324 mRNA. Translation: BAE31903.1.
AK153435 mRNA. Translation: BAE31992.1.
AK153556 mRNA. Translation: BAE32092.1.
AK159147 mRNA. Translation: BAE34854.1.
CT010378 mRNA. Translation: CAJ18585.1.
BC057868 mRNA. Translation: AAH57868.1.
AF442152 mRNA. Translation: AAL50054.1.
CCDSiCCDS25848.1.
RefSeqiNP_067359.2. NM_021384.4.
UniGeneiMm.24045.

3D structure databases

ProteinModelPortaliQ8CBB9.
SMRiQ8CBB9. Positions 79-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208378. 5 interactions.
STRINGi10090.ENSMUSP00000020970.

PTM databases

iPTMnetiQ8CBB9.
PhosphoSiteiQ8CBB9.

Proteomic databases

MaxQBiQ8CBB9.
PaxDbiQ8CBB9.
PRIDEiQ8CBB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020970; ENSMUSP00000020970; ENSMUSG00000020641.
GeneIDi58185.
KEGGimmu:58185.
UCSCiuc007nfh.2. mouse.

Organism-specific databases

CTDi91543.
MGIiMGI:1929628. Rsad2.

Phylogenomic databases

eggNOGiENOG410IGZE. Eukaryota.
ENOG410XQM5. LUCA.
GeneTreeiENSGT00390000013670.
HOVERGENiHBG053099.
InParanoidiQ8CBB9.
KOiK15045.
OMAiINRFNVE.
OrthoDBiEOG7FFMRW.
PhylomeDBiQ8CBB9.
TreeFamiTF300085.

Miscellaneous databases

PROiQ8CBB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CBB9.
CleanExiMM_RSAD2.
ExpressionAtlasiQ8CBB9. baseline and differential.
GenevisibleiQ8CBB9. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
IPR026372. Viperin.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04278. viperin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Vesicular stomatitis virus and pseudorabies virus induce a vig1/cig5 homologue in mouse dendritic cells via different pathways."
    Boudinot P., Riffault S., Salhi S., Carrat C., Sedlik C., Mahmoudi N., Charley B., Benmansour A.
    J. Gen. Virol. 81:2675-2682(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: C57BL/6J1 Publication.
    Tissue: Lymph node1 Publication.
  2. "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/6JImported.
    Tissue: BoneImported and Bone marrowImported.
  3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: NMRIImported.
    Tissue: Mammary tumorImported.
  5. "Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus."
    Chin K.-C., Cresswell P.
    Proc. Natl. Acad. Sci. U.S.A. 98:15125-15130(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-362.
  6. "The antiviral cytomegalovirus inducible gene 5/viperin is expressed in atherosclerosis and regulated by proinflammatory agents."
    Olofsson P.S., Jatta K., Waagsaeter D., Gredmark S., Hedin U., Paulsson-Berne G., Soederberg-Naucler C., Hansson G.K., Sirsjoe A.
    Arterioscler. Thromb. Vasc. Biol. 25:E113-E116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Toll-like receptor-dependent and -independent viperin gene expression and counter-regulation by PRDI-binding factor-1/BLIMP1."
    Severa M., Coccia E.M., Fitzgerald K.A.
    J. Biol. Chem. 281:26188-26195(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Identification and characterization of interferon-induced proteins that inhibit alphavirus replication."
    Zhang Y., Burke C.W., Ryman K.D., Klimstra W.B.
    J. Virol. 81:11246-11255(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Viperin is required for optimal Th2 responses and T-cell receptor-mediated activation of NF-kappaB and AP-1."
    Qiu L.Q., Cresswell P., Chin K.C.
    Blood 113:3520-3529(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The antiviral protein, viperin, localizes to lipid droplets via its N-terminal amphipathic alpha-helix."
    Hinson E.R., Cresswell P.
    Proc. Natl. Acad. Sci. U.S.A. 106:20452-20457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  12. "Viperin: a multifunctional, interferon-inducible protein that regulates virus replication."
    Seo J.Y., Yaneva R., Cresswell P.
    Cell Host Microbe 10:534-539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. "Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells."
    Saitoh T., Satoh T., Yamamoto N., Uematsu S., Takeuchi O., Kawai T., Akira S.
    Immunity 34:352-363(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IRAK1 AND TRAF6.
  14. "The interferon-inducible gene viperin restricts West Nile virus pathogenesis."
    Szretter K.J., Brien J.D., Thackray L.B., Virgin H.W., Cresswell P., Diamond M.S.
    J. Virol. 85:11557-11566(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRSAD2_MOUSE
AccessioniPrimary (citable) accession number: Q8CBB9
Secondary accession number(s): Q3U5I6
, Q3U5T4, Q3U622, Q3U627, Q3U7I6, Q3U7M1, Q3U8F4, Q3U8U7, Q3U941, Q3U977, Q3U9E1, Q3U9J0, Q3U9J3, Q3UBW6, Q3UC07, Q3UDI0, Q6PEU4, Q8VHM2, Q9JHD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 110 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.