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Radical S-adenosyl methionine domain-containing protein 2 (Cytomegalovirus-induced gene 5 protein) (Viperin) (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible)

 RSAD2_HUMAN             Reviewed;         361 AA.
Q8WXG1; Q8WVI4;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
31-JAN-2018, entry version 117.
RecName: Full=Radical S-adenosyl methionine domain-containing protein 2;
AltName: Full=Cytomegalovirus-induced gene 5 protein;
AltName: Full=Viperin;
AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible;
Name=RSAD2 {ECO:0000312|EMBL:EAX01034.1};
Synonyms=CIG5 {ECO:0000312|EMBL:AAY14802.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
TISSUE=Foreskin fibroblast {ECO:0000269|PubMed:9391139};
PubMed=9391139; DOI=10.1073/pnas.94.25.13985;
Zhu H., Cong J.-P., Shenk T.;
"Use of differential display analysis to assess the effect of human
cytomegalovirus infection on the accumulation of cellular RNAs:
induction of interferon-responsive RNAs.";
Proc. Natl. Acad. Sci. U.S.A. 94:13985-13990(1997).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL50053.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
INDUCTION.
TISSUE=Macrophage {ECO:0000269|PubMed:11752458};
PubMed=11752458; DOI=10.1073/pnas.011593298;
Chin K.-C., Cresswell P.;
"Viperin (cig5), an IFN-inducible antiviral protein directly induced
by human cytomegalovirus.";
Proc. Natl. Acad. Sci. U.S.A. 98:15125-15130(2001).
[3] {ECO:0000312|EMBL:AAY14802.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4] {ECO:0000312|EMBL:EAX01034.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAH17969.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-42.
TISSUE=Prostate {ECO:0000312|EMBL:AAH17969.1};
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] {ECO:0000305}
UP-REGULATION IN ATHEROSCLEROSIS.
PubMed=15890971; DOI=10.1161/01.ATV.0000170130.85334.38;
Olofsson P.S., Jatta K., Waagsaeter D., Gredmark S., Hedin U.,
Paulsson-Berne G., Soederberg-Naucler C., Hansson G.K., Sirsjoe A.;
"The antiviral cytomegalovirus inducible gene 5/viperin is expressed
in atherosclerosis and regulated by proinflammatory agents.";
Arterioscler. Thromb. Vasc. Biol. 25:E113-E116(2005).
[7] {ECO:0000305}
FUNCTION, AND INDUCTION.
PubMed=16108059; DOI=10.1002/hep.20844;
Helbig K.J., Lau D.T.-Y., Semendric L., Harley H.A.J., Beard M.R.;
"Analysis of ISG expression in chronic hepatitis C identifies viperin
as a potential antiviral effector.";
Hepatology 42:702-710(2005).
[8] {ECO:0000305}
INDUCTION.
PubMed=16150475; DOI=10.1016/j.virol.2005.07.035;
Khaiboullina S.F., Rizvanov A.A., Holbrook M.R., St Jeor S.;
"Yellow fever virus strains Asibi and 17D-204 infect human umbilical
cord endothelial cells and induce novel changes in gene expression.";
Virology 342:167-176(2005).
[9] {ECO:0000305}
INDUCTION.
PubMed=16849320; DOI=10.1074/jbc.M604516200;
Severa M., Coccia E.M., Fitzgerald K.A.;
"Toll-like receptor-dependent and -independent viperin gene expression
and counter-regulation by PRDI-binding factor-1/BLIMP1.";
J. Biol. Chem. 281:26188-26195(2006).
[10] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16982913; DOI=10.4049/jimmunol.177.7.4735;
Rivieccio M.A., Suh H.-S., Zhao Y., Zhao M.-L., Chin K.-C., Lee S.C.,
Brosnan C.F.;
"TLR3 ligation activates an antiviral response in human fetal
astrocytes: a role for viperin/cig5.";
J. Immunol. 177:4735-4741(2006).
[11]
FUNCTION.
PubMed=17686841; DOI=10.1128/JVI.01282-07;
Zhang Y., Burke C.W., Ryman K.D., Klimstra W.B.;
"Identification and characterization of interferon-induced proteins
that inhibit alphavirus replication.";
J. Virol. 81:11246-11255(2007).
[12]
INTERACTION WITH FPPS.
PubMed=18005724; DOI=10.1016/j.chom.2007.06.009;
Wang X., Hinson E.R., Cresswell P.;
"The interferon-inducible protein viperin inhibits influenza virus
release by perturbing lipid rafts.";
Cell Host Microbe 2:96-105(2007).
[13]
FUNCTION.
PubMed=18005719; DOI=10.1016/j.chom.2007.07.005;
Waheed A.A., Freed E.O.;
"Influenza virus not cRAFTy enough to dodge viperin.";
Cell Host Microbe 2:71-72(2007).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=19074433; DOI=10.1074/jbc.M807261200;
Hinson E.R., Cresswell P.;
"The N-terminal amphipathic alpha-helix of viperin mediates
localization to the cytosolic face of the endoplasmic reticulum and
inhibits protein secretion.";
J. Biol. Chem. 284:4705-4712(2009).
[15]
COFACTOR.
PubMed=20176015; DOI=10.1016/j.febslet.2010.02.041;
Duschene K.S., Broderick J.B.;
"The antiviral protein viperin is a radical SAM enzyme.";
FEBS Lett. 584:1263-1267(2010).
[16]
INTERACTION WITH HHV-5 PROTEIN UL37 AND HADHB, AND SUBCELLULAR
LOCATION.
PubMed=21527675; DOI=10.1126/science.1202007;
Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.;
"Human cytomegalovirus directly induces the antiviral protein viperin
to enhance infectivity.";
Science 332:1093-1097(2011).
[17]
INTERACTION WITH VAPA.
PubMed=21957124; DOI=10.1099/vir.0.033860-0;
Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.;
"Viperin inhibits hepatitis C virus replication by interfering with
binding of NS5A to host protein hVAP-33.";
J. Gen. Virol. 93:83-92(2012).
[18]
COFACTOR, AND MUTAGENESIS OF CYS-83; CYS-87 AND CYS-90.
PubMed=22363738; DOI=10.1371/journal.pone.0031797;
Haldar S., Paul S., Joshi N., Dasgupta A., Chattopadhyay K.;
"The presence of the iron-sulfur motif is important for the
conformational stability of the antiviral protein, Viperin.";
PLoS ONE 7:E31797-E31797(2012).
[19]
REVIEW.
PubMed=22177558; DOI=10.1016/j.chom.2011.11.004;
Seo J.Y., Yaneva R., Cresswell P.;
"Viperin: a multifunctional, interferon-inducible protein that
regulates virus replication.";
Cell Host Microbe 10:534-539(2011).
[20]
REVIEW.
PubMed=21142818; DOI=10.1089/jir.2010.0127;
Fitzgerald K.A.;
"The interferon inducible gene: Viperin.";
J. Interferon Cytokine Res. 31:131-135(2011).
[21]
REVIEW.
PubMed=22182524; DOI=10.1016/j.micinf.2011.11.015;
Mattijssen S., Pruijn G.J.;
"Viperin, a key player in the antiviral response.";
Microbes Infect. 14:419-426(2012).
[22]
STRUCTURE BY NMR OF 45-361, IDENTIFICATION BY MASS SPECTROMETRY, AND
COFACTOR.
PubMed=20026307; DOI=10.1016/j.bbrc.2009.12.070;
Shaveta G., Shi J., Chow V.T., Song J.;
"Structural characterization reveals that viperin is a radical S-
adenosyl-L-methionine (SAM) enzyme.";
Biochem. Biophys. Res. Commun. 391:1390-1395(2010).
-!- FUNCTION: 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 DNA and RNA viruses, including human
cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus
(WNV), dengue virus, sindbis virus, influenza A virus, sendai
virus, vesicular stomatitis virus (VSV), and human
immunodeficiency virus (HIV-1). 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 diphosphate 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. {ECO:0000269|PubMed:11752458,
ECO:0000269|PubMed:16108059, ECO:0000269|PubMed:16982913,
ECO:0000269|PubMed:17686841, ECO:0000269|PubMed:18005719,
ECO:0000269|PubMed:19074433}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:20026307,
ECO:0000269|PubMed:20176015, ECO:0000269|PubMed:22363738};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000269|PubMed:20026307, ECO:0000269|PubMed:20176015,
ECO:0000269|PubMed:22363738};
-!- SUBUNIT: Homodimer. Interacts with IRAK1 and TRAF6 (By
similarity). Interacts with FPPS. Interacts with human
cytomegalovirus/HHV-5 protein vMIA/UL37; this interaction results
in RSAD2/viperin relocalization from the endoplasmic reticulum to
the mitochondria. Interacts with HADHB. Interacts (via C-terminus)
with VAPA/VAP33 (via C-terminus) and inhibits its interaction with
hepatitis virus C (HCV) protein NS5A. {ECO:0000250,
ECO:0000269|PubMed:18005724, ECO:0000269|PubMed:19074433,
ECO:0000269|PubMed:21527675, ECO:0000269|PubMed:21957124}.
-!- INTERACTION:
O92835:- (xeno); NbExp=4; IntAct=EBI-12736320, EBI-12736594;
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-12736320, EBI-6927873;
O76071:CIAO1; NbExp=2; IntAct=EBI-12736320, EBI-725145;
Q9P0L0:VAPA; NbExp=10; IntAct=EBI-12736320, EBI-1059156;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein; Cytoplasmic side. Golgi apparatus
{ECO:0000269|PubMed:11752458, ECO:0000269|PubMed:16982913}.
Endoplasmic reticulum {ECO:0000269|PubMed:11752458,
ECO:0000269|PubMed:16982913}. Lipid droplet {ECO:0000250}.
Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer
membrane. Note=Infection with human cytomegalovirus (HCMV) causes
relocation to the Golgi apparatus and to cytoplasmic vacuoles
which also contain HCMV proteins glycoprotein B and pp28.
Interaction with human cytomegalovirus/HHV-5 protein vMIA/UL37
results in its relocalization from the endoplasmic reticulum to
the mitochondria.
-!- INDUCTION: By interferon type I, type II and bacterial
lipopolysaccharides (LPS). Little or no induction by IFNG/IFN-
gamma is observed in monocytic cell lines. Induced by infection
with hepatitis C virus, yellow fever virus and Sendai virus,
presumably through type I interferon pathway. Induction by
infection with human cytomegalovirus (HCMV), stomatitis virus
(VSV), chikungunya virus (CHIKV), Japanese encephalitis virus
(JEV) occurs independent of the IFN pathway.
{ECO:0000269|PubMed:11752458, ECO:0000269|PubMed:16108059,
ECO:0000269|PubMed:16150475, ECO:0000269|PubMed:16849320,
ECO:0000269|PubMed:9391139}.
-!- DOMAIN: The N-terminal region (1-42) is necessary for its
localization to the endoplasmic reticulum membrane and lipid
droplet.
-!- MISCELLANEOUS: Up-regulated in atherosclerosis. Latent viruses
like HCMV may be involved in atherogenesis by initiating local
inflammation. This may induce up-regulation of antiviral gene
RSAD2, which modulates lipids synthesis, and thus could play a
role in abnormal lipid accumulation leading to atherosclerosis.
-!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
{ECO:0000305}.
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EMBL; AF026941; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF442151; AAL50053.1; -; mRNA.
EMBL; AC017076; AAY14802.1; -; Genomic_DNA.
EMBL; CH471053; EAX01034.1; -; Genomic_DNA.
EMBL; BC017969; AAH17969.1; -; mRNA.
CCDS; CCDS1656.1; -.
RefSeq; NP_542388.2; NM_080657.4.
RefSeq; XP_011508716.1; XM_011510414.2.
UniGene; Hs.17518; -.
ProteinModelPortal; Q8WXG1; -.
SMR; Q8WXG1; -.
BioGrid; 124843; 3.
IntAct; Q8WXG1; 6.
STRING; 9606.ENSP00000371471; -.
iPTMnet; Q8WXG1; -.
PhosphoSitePlus; Q8WXG1; -.
BioMuta; RSAD2; -.
DMDM; 74724033; -.
PaxDb; Q8WXG1; -.
PeptideAtlas; Q8WXG1; -.
PRIDE; Q8WXG1; -.
DNASU; 91543; -.
Ensembl; ENST00000382040; ENSP00000371471; ENSG00000134321.
GeneID; 91543; -.
KEGG; hsa:91543; -.
UCSC; uc002qyp.2; human.
CTD; 91543; -.
DisGeNET; 91543; -.
EuPathDB; HostDB:ENSG00000134321.11; -.
GeneCards; RSAD2; -.
HGNC; HGNC:30908; RSAD2.
HPA; HPA041160; -.
HPA; HPA049409; -.
MIM; 607810; gene.
neXtProt; NX_Q8WXG1; -.
OpenTargets; ENSG00000134321; -.
PharmGKB; PA134937442; -.
eggNOG; ENOG410IGZE; Eukaryota.
eggNOG; ENOG410XQM5; LUCA.
GeneTree; ENSGT00390000013670; -.
HOGENOM; HOG000194793; -.
HOVERGEN; HBG053099; -.
InParanoid; Q8WXG1; -.
KO; K15045; -.
OMA; INRFNVE; -.
OrthoDB; EOG091G0GXY; -.
PhylomeDB; Q8WXG1; -.
TreeFam; TF300085; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; RSAD2; human.
GenomeRNAi; 91543; -.
PRO; PR:Q8WXG1; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000134321; -.
CleanEx; HS_RSAD2; -.
ExpressionAtlas; Q8WXG1; baseline and differential.
Genevisible; Q8WXG1; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS:UniProtKB.
GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0050709; P:negative regulation of protein secretion; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:UniProtKB.
GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; ISS:UniProtKB.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR007197; rSAM.
InterPro; IPR034395; SPASM/twitch_domain-containing.
InterPro; IPR026372; Viperin.
Pfam; PF04055; Radical_SAM; 1.
SFLD; SFLDF00318; Viperin; 1.
SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00729; Elp3; 1.
TIGRFAMs; TIGR04278; viperin; 1.
1: Evidence at protein level;
4Fe-4S; Antiviral defense; Atherosclerosis; Complete proteome;
Endoplasmic reticulum; Golgi apparatus; Host-virus interaction;
Immunity; Innate immunity; Iron; Iron-sulfur; Lipid droplet; Membrane;
Metal-binding; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Polymorphism; Reference proteome;
S-adenosyl-L-methionine.
CHAIN 1 361 Radical S-adenosyl methionine domain-
containing protein 2.
/FTId=PRO_0000309583.
METAL 83 83 Iron-sulfur (4Fe-4S-S-AdoMet).
METAL 87 87 Iron-sulfur (4Fe-4S-S-AdoMet).
METAL 90 90 Iron-sulfur (4Fe-4S-S-AdoMet).
VARIANT 42 42 L -> R (in dbSNP:rs17851586).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_036980.
VARIANT 52 52 V -> I (in dbSNP:rs2305257).
/FTId=VAR_053974.
MUTAGEN 83 83 C->A: Loss of ability to assemble an Fe-S
cluster and significant decrease in
protein stability.
{ECO:0000269|PubMed:22363738}.
MUTAGEN 87 87 C->A: Loss of ability to assemble an Fe-S
cluster and significant decrease in
protein stability.
{ECO:0000269|PubMed:22363738}.
MUTAGEN 90 90 C->A: Loss of ability to assemble an Fe-S
cluster and significant decrease in
protein stability.
{ECO:0000269|PubMed:22363738}.
CONFLICT 13 13 L -> F (in Ref. 1; AF026941).
{ECO:0000305}.
CONFLICT 216 217 VA -> IP (in Ref. 1; AF026941).
{ECO:0000305}.
SEQUENCE 361 AA; 42170 MW; ED014743CE1568DF CRC64;
MWVLTPAAFA GKLLSVFRQP LSSLWRSLVP LFCWLRATFW LLATKRRKQQ LVLRGPDETK
EEEEDPPLPT TPTSVNYHFT RQCNYKCGFC FHTAKTSFVL PLEEAKRGLL LLKEAGMEKI
NFSGGEPFLQ DRGEYLGKLV RFCKVELRLP SVSIVSNGSL IRERWFQNYG EYLDILAISC
DSFDEEVNVL IGRGQGKKNH VENLQKLRRW CRDYRVAFKI NSVINRFNVE EDMTEQIKAL
NPVRWKVFQC LLIEGENCGE DALREAERFV IGDEEFERFL ERHKEVSCLV PESNQKMKDS
YLILDEYMRF LNCRKGRKDP SKSILDVGVE EAIKFSGFDE KMFLKRGGKY IWSKADLKLD
W


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18-003-44299 Radical S-adenosyl methionine domain-containing protein 2 - Viperin Polyclonal 0.1 mg Protein A
RSAD2_RAT ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 2; organism: Rat; gene name: Rsad2 96T
RSAD2_MOUSE ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 2; organism: Mouse; gene name: Rsad2 96T
RSAD2_HUMAN ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 2; organism: Human; gene name: RSAD2 96T
RSAD1_HUMAN ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; organism: Human; gene name: RSAD1 96T
RSAD1_MOUSE ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; organism: Mouse; gene name: Rsad1 96T
EH2283 Radical S-adenosyl methionine domain-containing protein 2 Elisa Kit 96T
G6176 Radical S-adenosyl methionine domain-containing protein 2 (RSAD2), Rat, ELISA Kit 96T
CSB-EL020536RA Rat Radical S-adenosyl methionine domain-containing protein 2(RSAD2) ELISA kit 96T
G6175 Radical S-adenosyl methionine domain-containing protein 2 (RSAD2), Pig, ELISA Kit 96T
EIAAB44701 Homo sapiens,Human,Radical S-adenosyl methionine and flavodoxin domain-containing protein 2,RSAFD2,tRNA wybutosine-synthesizing protein 1 homolog B,TYW1B
G6173 Radical S-adenosyl methionine domain-containing protein 2 (RSAD2), Human, ELISA Kit 96T
CSB-EL020536BO Bovine Radical S-adenosyl methionine domain-containing protein 2(RSAD2) ELISA kit 96T
E1724p Bovine ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 1, mitochondrial 96T
CSB-EL020536HU Human Radical S-adenosyl methionine domain-containing protein 2(RSAD2) ELISA kit 96T
CSB-EL020536MO Mouse Radical S-adenosyl methionine domain-containing protein 2(RSAD2) ELISA kit 96T
G6172 Radical S-adenosyl methionine domain-containing protein 2 (RSAD2), Bovine, ELISA Kit 96T
E0845b Human ELISA Kit FOR Radical S-adenosyl methionine domain-containing protein 1, mitochondrial 96T
CSB-EL020536RA Rat Radical S-adenosyl methionine domain-containing protein 2(RSAD2) ELISA kit SpeciesRat 96T


 

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