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Toll-like receptor 3 (CD antigen CD283)

 TLR3_HUMAN              Reviewed;         904 AA.
O15455; B2RAI7; B7Z7K0; E6Y0F0; E6Y0F1; E9PGH4; Q4VAL2; Q504W0;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-MAR-2018, entry version 183.
RecName: Full=Toll-like receptor 3;
AltName: CD_antigen=CD283;
Flags: Precursor;
Name=TLR3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9435236; DOI=10.1073/pnas.95.2.588;
Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.;
"A family of human receptors structurally related to Drosophila
Toll.";
Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Neuron;
PubMed=17085778; DOI=10.1385/JMN:29:3:185;
Lafon M., Megret F., Lafage M., Prehaud C.;
"The innate immune facet of brain: human neurons express TLR-3 and
sense viral dsRNA.";
J. Mol. Neurosci. 29:185-194(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-412.
Macquin C., Bahram S.;
"TLR polymorphism.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
PHE-412.
TISSUE=Testis, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
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).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[9]
PROTEIN SEQUENCE OF 24-38.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[10]
FUNCTION, AND INTERACTION WITH TICAM1.
PubMed=12471095; DOI=10.4049/jimmunol.169.12.6668;
Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K.,
Akira S.;
"A novel Toll/IL-1 receptor domain-containing adapter that
preferentially activates the IFN-beta promoter in the Toll-like
receptor signaling.";
J. Immunol. 169:6668-6672(2002).
[11]
FUNCTION, AND INTERACTION WITH TICAM1.
TISSUE=Lung;
PubMed=12539043; DOI=10.1038/ni886;
Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T.;
"TICAM-1, an adapter molecule that participates in Toll-like receptor
3 mediated interferon-beta induction.";
Nat. Immunol. 4:161-167(2003).
[12]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-95; CYS-122; ASN-196 AND
ASN-247.
PubMed=16144834; DOI=10.1074/jbc.M507163200;
de Bouteiller O., Merck E., Hasan U.A., Hubac S., Benguigui B.,
Trinchieri G., Bates E.E., Caux C.;
"Recognition of double-stranded RNA by human toll-like receptor 3 and
downstream receptor signaling requires multimerization and an acidic
pH.";
J. Biol. Chem. 280:38133-38145(2005).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRC.
PubMed=16858407; DOI=10.1038/sj.emboj.7601222;
Johnsen I.B., Nguyen T.T., Ringdal M., Tryggestad A.M., Bakke O.,
Lien E., Espevik T., Anthonsen M.W.;
"Toll-like receptor 3 associates with c-Src tyrosine kinase on
endosomes to initiate antiviral signaling.";
EMBO J. 25:3335-3346(2006).
[14]
FUNCTION, AND MUTAGENESIS OF HIS-539 AND ASN-541.
PubMed=16720699; DOI=10.1073/pnas.0603245103;
Bell J.K., Askins J., Hall P.R., Davies D.R., Segal D.M.;
"The dsRNA binding site of human Toll-like receptor 3.";
Proc. Natl. Acad. Sci. U.S.A. 103:8792-8797(2006).
[15]
PHOSPHORYLATION AT TYR-759 AND TYR-858, FUNCTION, AND MUTAGENESIS OF
TYR-759.
PubMed=17178723; DOI=10.1074/jbc.C600226200;
Sarkar S.N., Elco C.P., Peters K.L., Chattopadhyay S., Sen G.C.;
"Two tyrosine residues of Toll-like receptor 3 trigger different steps
of NF-kappa B activation.";
J. Biol. Chem. 282:3423-3427(2007).
[16]
FUNCTION, DOUBLE-STRANDED RNA-BINDING, AND HOMODIMERIZATION.
PubMed=18172197; DOI=10.1073/pnas.0710779105;
Leonard J.N., Ghirlando R., Askins J., Bell J.K., Margulies D.H.,
Davies D.R., Segal D.M.;
"The TLR3 signaling complex forms by cooperative receptor
dimerization.";
Proc. Natl. Acad. Sci. U.S.A. 105:258-263(2008).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-57.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND
INTERACTION WITH UNC93B1.
PubMed=22611194; DOI=10.1073/pnas.1115091109;
Garcia-Cattaneo A., Gobert F.X., Muller M., Toscano F., Flores M.,
Lescure A., Del Nery E., Benaroch P.;
"Cleavage of Toll-like receptor 3 by cathepsins B and H is essential
for signaling.";
Proc. Natl. Acad. Sci. U.S.A. 109:9053-9058(2012).
[19]
INTERACTION WITH WDFY1 AND TICAM1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF TYR-759 AND TYR-858.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-703, FUNCTION, DISULFIDE
BONDS, SUBUNIT, GLYCOSYLATION AT ASN-52; ASN-70; ASN-196; ASN-252;
ASN-265; ASN-275; ASN-291; ASN-398; ASN-413; ASN-507 AND ASN-636, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16043704; DOI=10.1073/pnas.0505077102;
Bell J.K., Botos I., Hall P.R., Askins J., Shiloach J., Segal D.M.,
Davies D.R.;
"The molecular structure of the Toll-like receptor 3 ligand-binding
domain.";
Proc. Natl. Acad. Sci. U.S.A. 102:10976-10980(2005).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-700, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-124; ASN-252; ASN-275; ASN-291; ASN-398; ASN-413
AND ASN-507.
PubMed=15961631; DOI=10.1126/science.1115253;
Choe J., Kelker M.S., Wilson I.A.;
"Crystal structure of human toll-like receptor 3 (TLR3) ectodomain.";
Science 309:581-585(2005).
[22]
X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 22-702 IN COMPLEX WITH
ANTIBODY, DISULFIDE BONDS, SUBUNIT, DS-RNA BINDING REGIONS, AND
GLYCOSYLATION AT ASN-52; ASN-70; ASN-124; ASN-247; ASN-252; ASN-265;
ASN-275; ASN-291; ASN-398; ASN-413 AND ASN-507.
PubMed=22579623; DOI=10.1016/j.jmb.2012.05.006;
Luo J., Obmolova G., Malia T.J., Wu S.J., Duffy K.E., Marion J.D.,
Bell J.K., Ge P., Zhou Z.H., Teplyakov A., Zhao Y., Lamb R.J.,
Jordan J.L., San Mateo L.R., Sweet R.W., Gilliland G.L.;
"Lateral clustering of TLR3:dsRNA signaling units revealed by
TLR3ecd:3Fabs quaternary structure.";
J. Mol. Biol. 421:112-124(2012).
[23]
VARIANT HSE2 SER-554.
PubMed=17872438; DOI=10.1126/science.1139522;
Zhang S.-Y., Jouanguy E., Ugolini S., Smahi A., Elain G., Romero P.,
Segal D., Sancho-Shimizu V., Lorenzo L., Puel A., Picard C.,
Chapgier A., Plancoulaine S., Titeux M., Cognet C., von Bernuth H.,
Ku C.-L., Casrouge A., Zhang X.-X., Barreiro L., Leonard J.,
Hamilton C., Lebon P., Heron B., Vallee L., Quintana-Murci L.,
Hovnanian A., Rozenberg F., Vivier E., Geissmann F., Tardieu M.,
Abel L., Casanova J.-L.;
"TLR3 deficiency in patients with herpes simplex encephalitis.";
Science 317:1522-1527(2007).
[24]
VARIANT PHE-412.
PubMed=18753640; DOI=10.1056/NEJMoa0802437;
Yang Z., Stratton C., Francis P.J., Kleinman M.E., Tan P.L., Gibbs D.,
Tong Z., Chen H., Constantine R., Yang X., Chen Y., Zeng J., Davey L.,
Ma X., Hau V.S., Wang C., Harmon J., Buehler J., Pearson E., Patel S.,
Kaminoh Y., Watkins S., Luo L., Zabriskie N.A., Bernstein P.S.,
Cho W., Schwager A., Hinton D.R., Klein M.L., Hamon S.C., Simmons E.,
Yu B., Campochiaro B., Sunness J.S., Campochiaro P., Jorde L.,
Parmigiani G., Zack D.J., Katsanis N., Ambati J., Zhang K.;
"Toll-like receptor 3 and geographic atrophy in age-related macular
degeneration.";
N. Engl. J. Med. 359:1456-1463(2008).
[25]
ERRATUM.
Yang Z., Stratton C., Francis P.J., Kleinman M.E., Tan P.L., Gibbs D.,
Tong Z., Chen H., Constantine R., Yang X., Chen Y., Zeng J., Davey L.,
Ma X., Hau V.S., Wang C., Harmon J., Buehler J., Pearson E., Patel S.,
Kaminoh Y., Watkins S., Luo L., Zabriskie N.A., Bernstein P.S.,
Cho W., Schwager A., Hinton D.R., Klein M.L., Hamon S.C., Simmons E.,
Yu B., Campochiaro B., Sunness J.S., Campochiaro P., Jorde L.,
Parmigiani G., Zack D.J., Katsanis N., Ambati J., Zhang K.;
N. Engl. J. Med. 359:1859-1859(2008).
[26]
VARIANT PHE-412.
PubMed=22174453; DOI=10.4049/jimmunol.1102179;
Sironi M., Biasin M., Cagliani R., Forni D., De Luca M., Saulle I.,
Lo Caputo S., Mazzotta F., Macias J., Pineda J.A., Caruz A.,
Clerici M.;
"A common polymorphism in TLR3 confers natural resistance to HIV-1
infection.";
J. Immunol. 188:818-823(2012).
-!- FUNCTION: Key component of innate and adaptive immunity. TLRs
(Toll-like receptors) control host immune response against
pathogens through recognition of molecular patterns specific to
microorganisms. TLR3 is a nucleotide-sensing TLR which is
activated by double-stranded RNA, a sign of viral infection. Acts
via the adapter TRIF/TICAM1, leading to NF-kappa-B activation,
IRF3 nuclear translocation, cytokine secretion and the
inflammatory response. {ECO:0000269|PubMed:12471095,
ECO:0000269|PubMed:12539043, ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:16144834, ECO:0000269|PubMed:16720699,
ECO:0000269|PubMed:16858407, ECO:0000269|PubMed:17178723,
ECO:0000269|PubMed:18172197, ECO:0000269|PubMed:22611194}.
-!- SUBUNIT: Monomer and homodimer; dimerization is triggered by
ligand-binding, the signaling unit is composed of one ds-RNA of
around 40 bp and two TLR3 molecules, and lateral clustering of
signaling units along the length of the ds-RNA ligand is required
for TLR3 signal transduction. Interacts (via transmembrane domain)
with UNC93B1; the interaction is required for transport from the
ER to the endosomes. Interacts with SRC; upon binding of double-
stranded RNA. Interacts with TICAM1 (via the TIR domain) in
response to poly(I:C) and this interaction is enhanced in the
presence of WDFY1 (PubMed:25736436). The tyrosine-phosphorylated
form (via TIR domain) interacts with WDFY1 (via WD repeat 2) in
response to poly(I:C) (PubMed:25736436).
{ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:12539043,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:16144834,
ECO:0000269|PubMed:16858407, ECO:0000269|PubMed:22579623,
ECO:0000269|PubMed:22611194, ECO:0000269|PubMed:25736436}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-6116630, EBI-6116630;
P27986:PIK3R1; NbExp=2; IntAct=EBI-6116630, EBI-79464;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein. Endosome membrane. Early endosome
{ECO:0000269|PubMed:25736436}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15455-1; Sequence=Displayed;
Name=2;
IsoId=O15455-2; Sequence=VSP_054188;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high level in placenta and
pancreas. Also detected in CD11c+ immature dendritic cells. Only
expressed in dendritic cells and not in other leukocytes,
including monocyte precursors. TLR3 is the TLR that is expressed
most strongly in the brain, especially in astrocytes, glia, and
neurons. {ECO:0000269|PubMed:17085778}.
-!- DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to
18.
-!- PTM: Heavily N-glycosylated, except on that part of the surface of
the ectodomain that is involved in ligand binding.
{ECO:0000269|PubMed:15961631, ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22579623}.
-!- PTM: TLR3 signaling requires a proteolytic cleavage mediated by
cathepsins CTSB and CTSH, the cleavage occurs between amino acids
252 and 346. The cleaved form of TLR3 is the predominant form
found in endosomes. {ECO:0000269|PubMed:22611194}.
-!- POLYMORPHISM: The Phe-412 allele (dbSNP:rs3775291) occurs with a
frequency of 30% in populations with European and Asian ancestry,
and confers some natural resistance to HIV-1 infection.
-!- DISEASE: Herpes simplex encephalitis 2 (HSE2) [MIM:613002]: A rare
complication of human herpesvirus 1 (HHV-1) infection, occurring
in only a small minority of HHV-1 infected individuals. HSE is
characterized by hemorrhagic necrosis of parts of the temporal and
frontal lobes. Onset is over several days and involves fever,
headache, seizures, stupor, and often coma, frequently with a
fatal outcome. {ECO:0000269|PubMed:17872438}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry. TLR3 mutations predispose otherwise
healthy individuals to isolated herpes simplex encephalitis
through a mechanism that involves impaired IFNs production and
reduced immune defense against viral infection in the central
nervous system.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=TLR3base; Note=TLR3 mutation db;
URL="http://structure.bmc.lu.se/idbase/TLR3base/";
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EMBL; U88879; AAC34134.1; -; mRNA.
EMBL; DQ445682; ABE01399.1; -; mRNA.
EMBL; AB445631; BAG55028.1; -; mRNA.
EMBL; DQ360814; ABC86908.1; -; Genomic_DNA.
EMBL; DQ360815; ABC86909.1; -; Genomic_DNA.
EMBL; DQ360816; ABC86910.1; -; Genomic_DNA.
EMBL; AK302143; BAH13636.1; -; mRNA.
EMBL; AK314208; BAG36884.1; -; mRNA.
EMBL; AC104070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04628.1; -; Genomic_DNA.
EMBL; BC094737; AAH94737.1; -; mRNA.
EMBL; BC096333; AAH96333.1; -; mRNA.
EMBL; BC096334; AAH96334.1; -; mRNA.
EMBL; BC096335; AAH96335.1; -; mRNA.
CCDS; CCDS3846.1; -. [O15455-1]
RefSeq; NP_003256.1; NM_003265.2. [O15455-1]
RefSeq; XP_016864066.1; XM_017008577.1. [O15455-2]
UniGene; Hs.657724; -.
PDB; 1ZIW; X-ray; 2.10 A; A=27-700.
PDB; 2A0Z; X-ray; 2.40 A; A=22-703.
PDB; 2MK9; NMR; -; A/B=698-730.
PDB; 2MKA; NMR; -; A/B/C=698-730.
PDB; 3ULU; X-ray; 3.52 A; A=22-702.
PDB; 3ULV; X-ray; 3.52 A; A=22-702.
PDB; 5GS0; X-ray; 3.27 A; A/B=27-697.
PDBsum; 1ZIW; -.
PDBsum; 2A0Z; -.
PDBsum; 2MK9; -.
PDBsum; 2MKA; -.
PDBsum; 3ULU; -.
PDBsum; 3ULV; -.
PDBsum; 5GS0; -.
ProteinModelPortal; O15455; -.
SMR; O15455; -.
BioGrid; 112953; 32.
DIP; DIP-29660N; -.
IntAct; O15455; 8.
MINT; O15455; -.
STRING; 9606.ENSP00000296795; -.
ChEMBL; CHEMBL1075113; -.
iPTMnet; O15455; -.
PhosphoSitePlus; O15455; -.
BioMuta; TLR3; -.
MaxQB; O15455; -.
PaxDb; O15455; -.
PeptideAtlas; O15455; -.
PRIDE; O15455; -.
Ensembl; ENST00000296795; ENSP00000296795; ENSG00000164342. [O15455-1]
Ensembl; ENST00000504367; ENSP00000423684; ENSG00000164342. [O15455-2]
GeneID; 7098; -.
KEGG; hsa:7098; -.
UCSC; uc003iyq.4; human. [O15455-1]
CTD; 7098; -.
DisGeNET; 7098; -.
EuPathDB; HostDB:ENSG00000164342.12; -.
GeneCards; TLR3; -.
HGNC; HGNC:11849; TLR3.
HPA; CAB025658; -.
MalaCards; TLR3; -.
MIM; 603029; gene.
MIM; 613002; phenotype.
neXtProt; NX_O15455; -.
OpenTargets; ENSG00000164342; -.
Orphanet; 1930; Herpetic encephalitis.
PharmGKB; PA36551; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000251618; -.
HOVERGEN; HBG023181; -.
InParanoid; O15455; -.
KO; K05401; -.
OMA; HLLKDPL; -.
OrthoDB; EOG091G02Q2; -.
PhylomeDB; O15455; -.
TreeFam; TF325595; -.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-168164; Toll Like Receptor 3 (TLR3) Cascade.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-5602410; TLR3 deficiency - HSE.
Reactome; R-HSA-5602415; UNC93B1 deficiency - HSE.
Reactome; R-HSA-5602566; TICAM1 deficiency - HSE.
Reactome; R-HSA-5602571; TRAF3 deficiency - HSE.
Reactome; R-HSA-9013957; TLR3-mediated TICAM1-dependent programmed cell death.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SignaLink; O15455; -.
SIGNOR; O15455; -.
EvolutionaryTrace; O15455; -.
GeneWiki; TLR_3; -.
GenomeRNAi; 7098; -.
PRO; PR:O15455; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164342; -.
CleanEx; HS_TLR3; -.
ExpressionAtlas; O15455; baseline and differential.
Genevisible; O15455; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; TAS:BHF-UCL.
GO; GO:0009597; P:detection of virus; NAS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0006972; P:hyperosmotic response; NAS:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0007252; P:I-kappaB phosphorylation; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070266; P:necroptotic process; TAS:Reactome.
GO; GO:0097527; P:necroptotic signaling pathway; IDA:UniProtKB.
GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; NAS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; IDA:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IDA:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IDA:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0034346; P:positive regulation of type III interferon production; IEA:Ensembl.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027173; TLR3.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44599; PTHR44599; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 6.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 16.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 19.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
RNA-binding; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000269|PubMed:15340161}.
CHAIN 24 904 Toll-like receptor 3.
/FTId=PRO_0000034715.
TOPO_DOM 24 704 Lumenal. {ECO:0000255}.
TRANSMEM 705 725 Helical. {ECO:0000255}.
TOPO_DOM 726 904 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 51 LRRNT.
REPEAT 52 73 LRR 1.
REPEAT 76 97 LRR 2.
REPEAT 100 121 LRR 3.
REPEAT 124 145 LRR 4.
REPEAT 148 168 LRR 5.
REPEAT 172 193 LRR 6.
REPEAT 198 219 LRR 7.
REPEAT 222 244 LRR 8.
REPEAT 249 270 LRR 9.
REPEAT 275 296 LRR 10.
REPEAT 299 320 LRR 11.
REPEAT 323 344 LRR 12.
REPEAT 356 377 LRR 13.
REPEAT 380 400 LRR 14.
REPEAT 408 429 LRR 15.
REPEAT 432 454 LRR 16.
REPEAT 465 486 LRR 17.
REPEAT 507 528 LRR 18.
REPEAT 531 552 LRR 19.
REPEAT 563 584 LRR 20.
REPEAT 587 608 LRR 21.
REPEAT 611 632 LRR 22.
DOMAIN 645 698 LRRCT.
DOMAIN 754 896 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOD_RES 759 759 Phosphotyrosine.
{ECO:0000269|PubMed:17178723}.
MOD_RES 858 858 Phosphotyrosine.
{ECO:0000269|PubMed:17178723}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22579623}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:22579623}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16043704}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22579623}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 507 507 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16043704}.
CARBOHYD 662 662 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 37
DISULFID 95 122
DISULFID 649 677
DISULFID 651 696
VAR_SEQ 1 277 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054188.
VARIANT 284 284 N -> I (in dbSNP:rs5743316).
/FTId=VAR_052361.
VARIANT 307 307 Y -> D (in dbSNP:rs5743317).
/FTId=VAR_052362.
VARIANT 412 412 L -> F (in dbSNP:rs3775291).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:18753640,
ECO:0000269|PubMed:22174453,
ECO:0000269|Ref.4}.
/FTId=VAR_021976.
VARIANT 554 554 P -> S (in HSE2; causes TLR3 deficiency
and predisposition to herpes simplex
encephalitis; dbSNP:rs121434431).
{ECO:0000269|PubMed:17872438}.
/FTId=VAR_054887.
VARIANT 737 737 S -> T (in dbSNP:rs5743318).
/FTId=VAR_024664.
MUTAGEN 95 95 C->A: Reduced response to ds-RNA.
{ECO:0000269|PubMed:16144834}.
MUTAGEN 122 122 C->A: Reduced response to ds-RNA.
{ECO:0000269|PubMed:16144834}.
MUTAGEN 196 196 N->G: Reduced expression levels; when
associated with R-247.
{ECO:0000269|PubMed:16144834}.
MUTAGEN 247 247 N->R: Reduced response to ds-RNA. Reduced
expression levels; when associated with
G-196. {ECO:0000269|PubMed:16144834}.
MUTAGEN 539 539 H->A: No effect.
{ECO:0000269|PubMed:16720699}.
MUTAGEN 539 539 H->E: Loss of RNA binding. Constitutive
activation of NF-kappa-B.
{ECO:0000269|PubMed:16720699}.
MUTAGEN 541 541 N->A: Loss of RNA binding. Abolishes
activation of NF-kappa-B.
{ECO:0000269|PubMed:16720699}.
MUTAGEN 759 759 Y->F: Reduced activation of NF-kappa-B in
response to ds-RNA. Reduced induction of
IL-8 in response to ds-RNA. Loss of
interaction with WDFY1.
{ECO:0000269|PubMed:17178723,
ECO:0000269|PubMed:25736436}.
MUTAGEN 858 858 Y->F: Loss of interaction with WDFY1.
{ECO:0000269|PubMed:25736436}.
CONFLICT 290 290 G -> R (in Ref. 5; BAG36884).
{ECO:0000305}.
CONFLICT 575 575 D -> N (in Ref. 8; AAH94737).
{ECO:0000305}.
CONFLICT 605 605 V -> A (in Ref. 5; BAG36884).
{ECO:0000305}.
CONFLICT 663 663 E -> G (in Ref. 5; BAG36884).
{ECO:0000305}.
STRAND 31 36 {ECO:0000244|PDB:1ZIW}.
STRAND 47 49 {ECO:0000244|PDB:2A0Z}.
STRAND 54 57 {ECO:0000244|PDB:1ZIW}.
HELIX 68 74 {ECO:0000244|PDB:1ZIW}.
STRAND 78 81 {ECO:0000244|PDB:1ZIW}.
HELIX 94 97 {ECO:0000244|PDB:1ZIW}.
STRAND 103 105 {ECO:0000244|PDB:1ZIW}.
STRAND 108 110 {ECO:0000244|PDB:5GS0}.
TURN 118 121 {ECO:0000244|PDB:1ZIW}.
STRAND 126 129 {ECO:0000244|PDB:1ZIW}.
TURN 142 145 {ECO:0000244|PDB:1ZIW}.
STRAND 151 153 {ECO:0000244|PDB:1ZIW}.
STRAND 166 168 {ECO:0000244|PDB:1ZIW}.
STRAND 175 177 {ECO:0000244|PDB:1ZIW}.
HELIX 188 191 {ECO:0000244|PDB:1ZIW}.
HELIX 192 194 {ECO:0000244|PDB:1ZIW}.
STRAND 198 203 {ECO:0000244|PDB:1ZIW}.
HELIX 216 219 {ECO:0000244|PDB:1ZIW}.
STRAND 220 223 {ECO:0000244|PDB:1ZIW}.
STRAND 225 227 {ECO:0000244|PDB:1ZIW}.
HELIX 234 245 {ECO:0000244|PDB:1ZIW}.
STRAND 252 254 {ECO:0000244|PDB:1ZIW}.
TURN 265 268 {ECO:0000244|PDB:1ZIW}.
HELIX 269 273 {ECO:0000244|PDB:1ZIW}.
STRAND 278 280 {ECO:0000244|PDB:1ZIW}.
TURN 291 296 {ECO:0000244|PDB:1ZIW}.
STRAND 302 304 {ECO:0000244|PDB:1ZIW}.
STRAND 310 313 {ECO:0000244|PDB:1ZIW}.
TURN 315 320 {ECO:0000244|PDB:1ZIW}.
STRAND 326 328 {ECO:0000244|PDB:1ZIW}.
STRAND 338 340 {ECO:0000244|PDB:2A0Z}.
TURN 348 353 {ECO:0000244|PDB:1ZIW}.
STRAND 359 361 {ECO:0000244|PDB:1ZIW}.
TURN 372 377 {ECO:0000244|PDB:1ZIW}.
STRAND 383 385 {ECO:0000244|PDB:1ZIW}.
TURN 398 401 {ECO:0000244|PDB:1ZIW}.
HELIX 402 404 {ECO:0000244|PDB:1ZIW}.
STRAND 411 413 {ECO:0000244|PDB:1ZIW}.
TURN 424 429 {ECO:0000244|PDB:1ZIW}.
STRAND 435 437 {ECO:0000244|PDB:1ZIW}.
STRAND 444 446 {ECO:0000244|PDB:1ZIW}.
HELIX 450 452 {ECO:0000244|PDB:1ZIW}.
STRAND 460 462 {ECO:0000244|PDB:1ZIW}.
STRAND 467 470 {ECO:0000244|PDB:1ZIW}.
TURN 473 478 {ECO:0000244|PDB:1ZIW}.
STRAND 484 486 {ECO:0000244|PDB:1ZIW}.
TURN 501 504 {ECO:0000244|PDB:1ZIW}.
STRAND 510 512 {ECO:0000244|PDB:1ZIW}.
TURN 523 528 {ECO:0000244|PDB:1ZIW}.
STRAND 534 536 {ECO:0000244|PDB:1ZIW}.
HELIX 543 546 {ECO:0000244|PDB:1ZIW}.
TURN 557 560 {ECO:0000244|PDB:1ZIW}.
STRAND 566 568 {ECO:0000244|PDB:1ZIW}.
TURN 579 584 {ECO:0000244|PDB:1ZIW}.
STRAND 590 592 {ECO:0000244|PDB:1ZIW}.
TURN 603 608 {ECO:0000244|PDB:1ZIW}.
STRAND 614 616 {ECO:0000244|PDB:1ZIW}.
HELIX 627 634 {ECO:0000244|PDB:1ZIW}.
STRAND 638 641 {ECO:0000244|PDB:1ZIW}.
STRAND 655 658 {ECO:0000244|PDB:1ZIW}.
HELIX 671 674 {ECO:0000244|PDB:2A0Z}.
STRAND 676 680 {ECO:0000244|PDB:2A0Z}.
HELIX 688 690 {ECO:0000244|PDB:2A0Z}.
HELIX 700 727 {ECO:0000244|PDB:2MK9}.
SEQUENCE 904 AA; 103829 MW; 034E05ECA7A4D2F7 CRC64;
MRQTLPCIYF WGGLLPFGML CASSTTKCTV SHEVADCSHL KLTQVPDDLP TNITVLNLTH
NQLRRLPAAN FTRYSQLTSL DVGFNTISKL EPELCQKLPM LKVLNLQHNE LSQLSDKTFA
FCTNLTELHL MSNSIQKIKN NPFVKQKNLI TLDLSHNGLS STKLGTQVQL ENLQELLLSN
NKIQALKSEE LDIFANSSLK KLELSSNQIK EFSPGCFHAI GRLFGLFLNN VQLGPSLTEK
LCLELANTSI RNLSLSNSQL STTSNTTFLG LKWTNLTMLD LSYNNLNVVG NDSFAWLPQL
EYFFLEYNNI QHLFSHSLHG LFNVRYLNLK RSFTKQSISL ASLPKIDDFS FQWLKCLEHL
NMEDNDIPGI KSNMFTGLIN LKYLSLSNSF TSLRTLTNET FVSLAHSPLH ILNLTKNKIS
KIESDAFSWL GHLEVLDLGL NEIGQELTGQ EWRGLENIFE IYLSYNKYLQ LTRNSFALVP
SLQRLMLRRV ALKNVDSSPS PFQPLRNLTI LDLSNNNIAN INDDMLEGLE KLEILDLQHN
NLARLWKHAN PGGPIYFLKG LSHLHILNLE SNGFDEIPVE VFKDLFELKI IDLGLNNLNT
LPASVFNNQV SLKSLNLQKN LITSVEKKVF GPAFRNLTEL DMRFNPFDCT CESIAWFVNW
INETHTNIPE LSSHYLCNTP PHYHGFPVRL FDTSSCKDSA PFELFFMINT SILLIFIFIV
LLIHFEGWRI SFYWNVSVHR VLGFKEIDRQ TEQFEYAAYI IHAYKDKDWV WEHFSSMEKE
DQSLKFCLEE RDFEAGVFEL EAIVNSIKRS RKIIFVITHH LLKDPLCKRF KVHHAVQQAI
EQNLDSIILV FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERIGAFR HKLQVALGSK
NSVH


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20-321-175146 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175163 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175150 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.1 mg
20-321-175151 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.05 mg
18-661-15147 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.05 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
20-321-175149 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.1 mg
20-321-175167 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 9 (TLR9. CD289); CD289 antigen Monoclonal 0.05 mg
20-321-175166 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 9 (TLR9. CD289); CD289 antigen Monoclonal 0.1 mg
P-TLR13 Toll Receptor 13, Antigen blocking peptide 100ul


 

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