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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.
22-APR-2020, entry version 200.
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 IIAE2 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 OF PUBMED:18753640.
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:
O15455; O15455; NbExp=5; IntAct=EBI-6116630, EBI-6116630;
O15455; 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;
-!- 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: Encephalopathy, acute, infection-induced, Herpes-specific, 2
(IIAE2) [MIM:613002]: A rare complication of human herpesvirus 1 (HHV-
1) infection, occurring in only a small minority of HHV-1 infected
individuals. It 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.
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; -.
SMR; O15455; -.
BioGrid; 112953; 34.
DIP; DIP-29660N; -.
IntAct; O15455; 14.
MINT; O15455; -.
STRING; 9606.ENSP00000296795; -.
BindingDB; O15455; -.
ChEMBL; CHEMBL1075113; -.
iPTMnet; O15455; -.
PhosphoSitePlus; O15455; -.
BioMuta; TLR3; -.
EPD; O15455; -.
jPOST; O15455; -.
MassIVE; O15455; -.
MaxQB; O15455; -.
PaxDb; O15455; -.
PeptideAtlas; O15455; -.
PRIDE; O15455; -.
ProteomicsDB; 20320; -.
ProteomicsDB; 48678; -. [O15455-1]
ABCD; O15455; -.
Antibodypedia; 17502; 1092 antibodies.
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; -.
GeneCards; TLR3; -.
HGNC; HGNC:11849; TLR3.
HPA; ENSG00000164342; Tissue enhanced (placenta).
MalaCards; TLR3; -.
MIM; 603029; gene.
MIM; 613002; phenotype.
neXtProt; NX_O15455; -.
OpenTargets; ENSG00000164342; -.
Orphanet; 1930; Herpes simplex virus encephalitis.
PharmGKB; PA36551; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000159678; -.
HOGENOM; CLU_006000_4_1_1; -.
InParanoid; O15455; -.
KO; K05401; -.
OMA; FAWLPHL; -.
OrthoDB; 737804at2759; -.
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.
SignaLink; O15455; -.
SIGNOR; O15455; -.
ChiTaRS; TLR3; human.
EvolutionaryTrace; O15455; -.
GeneWiki; TLR_3; -.
GenomeRNAi; 7098; -.
Pharos; O15455; Tbio.
PRO; PR:O15455; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O15455; protein.
Bgee; ENSG00000164342; Expressed in placenta and 178 other tissues.
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:0031012; C:extracellular matrix; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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:0038023; F:signaling 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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
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:0043331; P:response to dsRNA; IBA:GO_Central.
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; IPR041015; TLR3_TMD.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24365:SF524; PTHR24365:SF524; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 6.
Pfam; PF01582; TIR; 1.
Pfam; PF17968; Tlr3_TMD; 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; 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
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 24..904
/note="Toll-like receptor 3"
/id="PRO_0000034715"
TOPO_DOM 24..704
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 705..725
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 726..904
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 24..51
/note="LRRNT"
REPEAT 52..73
/note="LRR 1"
REPEAT 76..97
/note="LRR 2"
REPEAT 100..121
/note="LRR 3"
REPEAT 124..145
/note="LRR 4"
REPEAT 148..168
/note="LRR 5"
REPEAT 172..193
/note="LRR 6"
REPEAT 198..219
/note="LRR 7"
REPEAT 222..244
/note="LRR 8"
REPEAT 249..270
/note="LRR 9"
REPEAT 275..296
/note="LRR 10"
REPEAT 299..320
/note="LRR 11"
REPEAT 323..344
/note="LRR 12"
REPEAT 356..377
/note="LRR 13"
REPEAT 380..400
/note="LRR 14"
REPEAT 408..429
/note="LRR 15"
REPEAT 432..454
/note="LRR 16"
REPEAT 465..486
/note="LRR 17"
REPEAT 507..528
/note="LRR 18"
REPEAT 531..552
/note="LRR 19"
REPEAT 563..584
/note="LRR 20"
REPEAT 587..608
/note="LRR 21"
REPEAT 611..632
/note="LRR 22"
DOMAIN 645..698
/note="LRRCT"
DOMAIN 754..897
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
MOD_RES 759
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:17178723"
MOD_RES 858
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:17178723"
CARBOHYD 52
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22579623"
CARBOHYD 57
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 70
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623"
CARBOHYD 124
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:22579623"
CARBOHYD 196
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16043704"
CARBOHYD 247
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22579623"
CARBOHYD 252
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 265
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16043704,
ECO:0000269|PubMed:22579623"
CARBOHYD 275
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 291
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 398
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 413
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 507
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15961631,
ECO:0000269|PubMed:16043704, ECO:0000269|PubMed:22579623"
CARBOHYD 636
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16043704"
CARBOHYD 662
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 28..37
DISULFID 95..122
DISULFID 649..677
DISULFID 651..696
VAR_SEQ 1..277
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_054188"
VARIANT 284
/note="N -> I (in dbSNP:rs5743316)"
/id="VAR_052361"
VARIANT 307
/note="Y -> D (in dbSNP:rs5743317)"
/id="VAR_052362"
VARIANT 412
/note="L -> F (in dbSNP:rs3775291)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:18753640, ECO:0000269|PubMed:22174453,
ECO:0000269|Ref.4"
/id="VAR_021976"
VARIANT 554
/note="P -> S (in IIAE2; causes TLR3 deficiency and
predisposition to herpes simplex encephalitis;
dbSNP:rs121434431)"
/evidence="ECO:0000269|PubMed:17872438"
/id="VAR_054887"
VARIANT 737
/note="S -> T (in dbSNP:rs5743318)"
/id="VAR_024664"
MUTAGEN 95
/note="C->A: Reduced response to ds-RNA."
/evidence="ECO:0000269|PubMed:16144834"
MUTAGEN 122
/note="C->A: Reduced response to ds-RNA."
/evidence="ECO:0000269|PubMed:16144834"
MUTAGEN 196
/note="N->G: Reduced expression levels; when associated
with R-247."
/evidence="ECO:0000269|PubMed:16144834"
MUTAGEN 247
/note="N->R: Reduced response to ds-RNA. Reduced expression
levels; when associated with G-196."
/evidence="ECO:0000269|PubMed:16144834"
MUTAGEN 539
/note="H->A: No effect."
/evidence="ECO:0000269|PubMed:16720699"
MUTAGEN 539
/note="H->E: Loss of RNA binding. Constitutive activation
of NF-kappa-B."
/evidence="ECO:0000269|PubMed:16720699"
MUTAGEN 541
/note="N->A: Loss of RNA binding. Abolishes activation of
NF-kappa-B."
/evidence="ECO:0000269|PubMed:16720699"
MUTAGEN 759
/note="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."
/evidence="ECO:0000269|PubMed:17178723,
ECO:0000269|PubMed:25736436"
MUTAGEN 858
/note="Y->F: Loss of interaction with WDFY1."
/evidence="ECO:0000269|PubMed:25736436"
CONFLICT 290
/note="G -> R (in Ref. 5; BAG36884)"
/evidence="ECO:0000305"
CONFLICT 575
/note="D -> N (in Ref. 8; AAH94737)"
/evidence="ECO:0000305"
CONFLICT 605
/note="V -> A (in Ref. 5; BAG36884)"
/evidence="ECO:0000305"
CONFLICT 663
/note="E -> G (in Ref. 5; BAG36884)"
/evidence="ECO:0000305"
STRAND 31..36
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 47..49
/evidence="ECO:0000244|PDB:2A0Z"
STRAND 54..57
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 68..74
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 78..81
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 94..97
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 103..105
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 108..110
/evidence="ECO:0000244|PDB:5GS0"
TURN 118..121
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 126..129
/evidence="ECO:0000244|PDB:1ZIW"
TURN 142..145
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 151..153
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 166..168
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 175..177
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 188..191
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 192..194
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 198..203
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 216..219
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 220..223
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 225..227
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 234..245
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 252..254
/evidence="ECO:0000244|PDB:1ZIW"
TURN 265..268
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 269..273
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 278..280
/evidence="ECO:0000244|PDB:1ZIW"
TURN 291..296
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 302..304
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 310..313
/evidence="ECO:0000244|PDB:1ZIW"
TURN 315..320
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 326..328
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 338..340
/evidence="ECO:0000244|PDB:2A0Z"
TURN 348..353
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 359..361
/evidence="ECO:0000244|PDB:1ZIW"
TURN 372..377
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 383..385
/evidence="ECO:0000244|PDB:1ZIW"
TURN 398..401
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 402..404
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 411..413
/evidence="ECO:0000244|PDB:1ZIW"
TURN 424..429
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 435..437
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 444..446
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 450..452
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 460..462
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 467..470
/evidence="ECO:0000244|PDB:1ZIW"
TURN 473..478
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 484..486
/evidence="ECO:0000244|PDB:1ZIW"
TURN 501..504
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 510..512
/evidence="ECO:0000244|PDB:1ZIW"
TURN 523..528
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 534..536
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 543..546
/evidence="ECO:0000244|PDB:1ZIW"
TURN 557..560
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 566..568
/evidence="ECO:0000244|PDB:1ZIW"
TURN 579..584
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 590..592
/evidence="ECO:0000244|PDB:1ZIW"
TURN 603..608
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 614..616
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 627..634
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 638..641
/evidence="ECO:0000244|PDB:1ZIW"
STRAND 655..658
/evidence="ECO:0000244|PDB:1ZIW"
HELIX 671..674
/evidence="ECO:0000244|PDB:2A0Z"
STRAND 676..680
/evidence="ECO:0000244|PDB:2A0Z"
HELIX 688..690
/evidence="ECO:0000244|PDB:2A0Z"
HELIX 700..727
/evidence="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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15-288-22788A Toll-like receptor 3 - CD283 antigen Polyclonal 0.1 mg
15-288-22788A Toll-like receptor 3 - CD283 antigen Polyclonal 0.05 mg
GWB-7E13B4 TOLL-LIKE RECEPTOR 3 (TLR3. CD283), Antibody
GWB-5D0F40 FITC CONJUGATED TOLL-LIKE RECEPTOR 3 (TLR3. CD283), Antibody
20-321-175147 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175164 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175144 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175165 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.05 mg
20-321-175148 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.05 mg
20-321-175145 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.05 mg
20-321-175143 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
20-321-175146 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
Pathways :
WP1067: Toll-like receptor signaling pathway
WP1384: Toll-like receptor signaling pathway
WP88: Toll Like Receptor signaling
WP1271: Toll-like receptor signaling pathway
WP75: Toll-like receptor signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1183: Toll-like receptor signaling pathway
WP2328: Allograft rejection
WP1449: Regulation of toll-like receptor signaling pathway
WP1309: Toll-like receptor signaling pathway
WP949: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP1004: Kit Receptor Signaling Pathway
WP1781: Advanced glycosylation endproduct receptor signaling
WP590: Cardiovascular Signaling
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP252: Androgen Receptor Signaling Pathway
WP886: Kit Receptor Signaling Pathway
WP1284: EPO Receptor Signaling
WP274: B Cell Receptor Signaling Pathway
WP908: B Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1918: Signaling by Robo receptor
WP733: Serotonin Receptor 2 and STAT3 Signaling
WP1965: VEGF-receptor Signal Transduction

Related Genes :
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[TLR2 TIL4] Toll-like receptor 2 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282)
[Tlr1] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[Tlr2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[Tlr4 Lps] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (hToll) (CD antigen CD284)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[CD36 GP3B GP4] Platelet glycoprotein 4 (Fatty acid translocase) (FAT) (Glycoprotein IIIb) (GPIIIB) (Leukocyte differentiation antigen CD36) (PAS IV) (PAS-4) (Platelet collagen receptor) (Platelet glycoprotein IV) (GPIV) (Thrombospondin receptor) (CD antigen CD36)
[TLR1 KIAA0012] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[Tlr4] Toll-like receptor 4 (Toll4) (EC 3.2.2.6) (CD antigen CD284)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[Tlr6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[Cd44 Ly-24] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[CD44 LHR MDU2 MDU3 MIC4] CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[Cd300lf Clm1 Lmir3] CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Leukocyte mono-Ig-like receptor 3) (Myeloid-associated immunoglobulin-like receptor 5) (MAIR-5) (MAIR-V) (CD antigen CD300f)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[Cd44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[CD44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HAM1 antigen) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[ITGAM CD11B CR3A] Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (Neutrophil adherence receptor) (CD antigen CD11b)

Bibliography :
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