Toll-like receptor 3 precursor - Homo sapiens (Human)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Toll-like receptor 3

Alternative name(s):
CD_antigen=CD283

Gene names

Name:

TLR3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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, cytokine secretion and the inflammatory response. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15
Subunit structure	Monomer and homodimer; dimerization is triggered by ligand-binding and is required for TLR3 signaling. Interacts (via transmembrane domain) with UNC93B1 By similarity. Interacts with TICAM1 (via the TIR domain); mediates TLR3 signaling. Interacts with SRC; upon binding of double-stranded RNA. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane Ref.10.
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. Ref.2
Domain	ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18 By similarity.
Post-translational modification	Heavily N-glycosylated, except on that part of the surface of the ectodomain that is involved in ligand binding. Ref.15 Ref.16
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.
Involvement in 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. 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. Ref.17
Sequence similarities	Belongs to the Toll-like receptor family. Contains 22 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 LRRNT domain. Contains 1 TIR domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Endoplasmic reticulum Endosome Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	RNA-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB phosphorylation Inferred from direct assay PubMed 19740627. Source: BHF-UCL TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome activation of NF-kappaB-inducing kinase activity Non-traceable author statement PubMed 12054664. Source: UniProtKB cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB defense response to bacterium Traceable author statement PubMed 10426995. Source: ProtInc defense response to virus Traceable author statement PubMed 15356140. Source: BHF-UCL detection of virus Non-traceable author statement PubMed 12054664. Source: UniProtKB hyperosmotic response Non-traceable author statement PubMed 12054664. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement PubMed 15356140. Source: BHF-UCL negative regulation of osteoclast differentiation Non-traceable author statement PubMed 12133979. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of JNK cascade Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB import into nucleus Inferred from direct assay PubMed 19740627. Source: BHF-UCL positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of chemokine biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of chemokine production Inferred from direct assay PubMed 19740627. Source: BHF-UCL positive regulation of inflammatory response Inferred by curator PubMed 19740627. Source: BHF-UCL positive regulation of interferon-alpha biosynthetic process Inferred from direct assay PubMed 16286015. Source: UniProtKB positive regulation of interferon-beta biosynthetic process Inferred from direct assay PubMed 16286015. Source: UniProtKB positive regulation of interferon-beta production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of interferon-gamma biosynthetic process Inferred from direct assay PubMed 16286015. Source: UniProtKB positive regulation of interleukin-12 production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of interleukin-6 production Inferred from direct assay PubMed 19740627. Source: BHF-UCL positive regulation of interleukin-8 production Inferred from direct assay PubMed 17128265. Source: BHF-UCL positive regulation of toll-like receptor signaling pathway Inferred from direct assay PubMed 17128265. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of tumor necrosis factor production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of type III interferon production Inferred from electronic annotation. Source: Compara response to exogenous dsRNA Inferred from electronic annotation. Source: Compara toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endolysosome membrane Traceable author statement. Source: Reactome endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	double-stranded RNA binding Inferred from direct assay PubMed 16111635. Source: UniProtKB transmembrane signaling receptor activity Non-traceable author statement PubMed 12054664. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Chain

24 – 904

881

Toll-like receptor 3

PRO_0000034715

Regions

Topological domain

24 – 704

681

Lumenal Potential

Transmembrane

705 – 725

21

Helical; Potential

Topological domain

726 – 904

179

Cytoplasmic Potential

Domain

24 – 51

28

LRRNT

Repeat

52 – 73

22

LRR 1

Repeat

76 – 97

22

LRR 2

Repeat

100 – 121

22

LRR 3

Repeat

124 – 145

22

LRR 4

Repeat

148 – 168

21

LRR 5

Repeat

172 – 193

22

LRR 6

Repeat

198 – 219

22

LRR 7

Repeat

222 – 244

23

LRR 8

Repeat

249 – 270

22

LRR 9

Repeat

275 – 296

22

LRR 10

Repeat

299 – 320

22

LRR 11

Repeat

323 – 344

22

LRR 12

Repeat

356 – 377

22

LRR 13

Repeat

380 – 400

21

LRR 14

Repeat

408 – 429

22

LRR 15

Repeat

432 – 454

23

LRR 16

Repeat

465 – 486

22

LRR 17

Repeat

507 – 528

22

LRR 18

Repeat

531 – 552

22

LRR 19

Repeat

563 – 584

22

LRR 20

Repeat

587 – 608

22

LRR 21

Repeat

611 – 632

22

LRR 22

Domain

645 – 698

54

LRRCT

Domain

754 – 896

143

TIR

Amino acid modifications

Modified residue

759

1

Phosphotyrosine Ref.12

Modified residue

858

1

Phosphotyrosine Ref.12

Glycosylation

52

1

N-linked (GlcNAc...) Ref.14 Ref.15

Glycosylation

57

1

N-linked (GlcNAc...) Ref.14

Glycosylation

70

1

N-linked (GlcNAc...) Ref.15

Glycosylation

124

1

N-linked (GlcNAc...) Ref.16

Glycosylation

196

1

N-linked (GlcNAc...) Ref.15

Glycosylation

247

1

N-linked (GlcNAc...) Potential

Glycosylation

252

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

265

1

N-linked (GlcNAc...) Ref.15

Glycosylation

275

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

291

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

398

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

413

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

507

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

636

1

N-linked (GlcNAc...) Ref.15

Glycosylation

662

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

284

1

N → I.
Corresponds to variant rs5743316 [ dbSNP | Ensembl ].

VAR_052361

Natural variant

307

1

Y → D.
Corresponds to variant rs5743317 [ dbSNP | Ensembl ].

VAR_052362

Natural variant

412

1

L → F. Ref.18 Ref.20
Corresponds to variant rs3775291 [ dbSNP | Ensembl ].

VAR_021976

Natural variant

554

1

P → S in HSE2; causes TLR3 deficiency and predisposition to herpes simplex encephalitis. Ref.17

VAR_054887

Natural variant

737

1

S → T.
Corresponds to variant rs5743318 [ dbSNP | Ensembl ].

VAR_024664

Experimental info

Mutagenesis

95

1

C → A: Reduced response to ds-RNA. Ref.9

Mutagenesis

122

1

C → A: Reduced response to ds-RNA. Ref.9

Mutagenesis

196

1

N → G: Reduced expression levels; when associated with R-247. Ref.9

Mutagenesis

247

1

N → R: Reduced response to ds-RNA. Reduced expression levels; when associated with G-196. Ref.9

Mutagenesis

539

1

H → A: No effect. Ref.11

Mutagenesis

539

1

H → E: Loss of RNA binding. Constitutive activation of NF-kappa-B. Ref.11

Mutagenesis

541

1

N → A: Loss of RNA binding. Abolishes activation of NF-kappa-B. Ref.11

Mutagenesis

759

1

Y → F: Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA. Ref.12

Secondary structure

1

.

904

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O15455 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 034E05ECA7A4D2F7
Show »

FASTA

904

103,829

        10         20         30         40         50         60 
MRQTLPCIYF WGGLLPFGML CASSTTKCTV SHEVADCSHL KLTQVPDDLP TNITVLNLTH 

        70         80         90        100        110        120 
NQLRRLPAAN FTRYSQLTSL DVGFNTISKL EPELCQKLPM LKVLNLQHNE LSQLSDKTFA 

       130        140        150        160        170        180 
FCTNLTELHL MSNSIQKIKN NPFVKQKNLI TLDLSHNGLS STKLGTQVQL ENLQELLLSN 

       190        200        210        220        230        240 
NKIQALKSEE LDIFANSSLK KLELSSNQIK EFSPGCFHAI GRLFGLFLNN VQLGPSLTEK 

       250        260        270        280        290        300 
LCLELANTSI RNLSLSNSQL STTSNTTFLG LKWTNLTMLD LSYNNLNVVG NDSFAWLPQL 

       310        320        330        340        350        360 
EYFFLEYNNI QHLFSHSLHG LFNVRYLNLK RSFTKQSISL ASLPKIDDFS FQWLKCLEHL 

       370        380        390        400        410        420 
NMEDNDIPGI KSNMFTGLIN LKYLSLSNSF TSLRTLTNET FVSLAHSPLH ILNLTKNKIS 

       430        440        450        460        470        480 
KIESDAFSWL GHLEVLDLGL NEIGQELTGQ EWRGLENIFE IYLSYNKYLQ LTRNSFALVP 

       490        500        510        520        530        540 
SLQRLMLRRV ALKNVDSSPS PFQPLRNLTI LDLSNNNIAN INDDMLEGLE KLEILDLQHN 

       550        560        570        580        590        600 
NLARLWKHAN PGGPIYFLKG LSHLHILNLE SNGFDEIPVE VFKDLFELKI IDLGLNNLNT 

       610        620        630        640        650        660 
LPASVFNNQV SLKSLNLQKN LITSVEKKVF GPAFRNLTEL DMRFNPFDCT CESIAWFVNW 

       670        680        690        700        710        720 
INETHTNIPE LSSHYLCNTP PHYHGFPVRL FDTSSCKDSA PFELFFMINT SILLIFIFIV 

       730        740        750        760        770        780 
LLIHFEGWRI SFYWNVSVHR VLGFKEIDRQ TEQFEYAAYI IHAYKDKDWV WEHFSSMEKE 

       790        800        810        820        830        840 
DQSLKFCLEE RDFEAGVFEL EAIVNSIKRS RKIIFVITHH LLKDPLCKRF KVHHAVQQAI 

       850        860        870        880        890        900 
EQNLDSIILV FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERIGAFR HKLQVALGSK 


NSVH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of human receptors structurally related to Drosophila Toll." Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F. Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The innate immune facet of brain: human neurons express TLR-3 and sense viral dsRNA." Lafon M., Megret F., Lafage M., Prehaud C. J. Mol. Neurosci. 29:185-194(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Neuron.
[3]	"Natural selection in the TLR-related genes in the course of primate evolution." Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A. Immunogenetics 60:727-735(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-38.
[7]	"A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling." Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S. J. Immunol. 169:6668-6672(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TICAM1.
[8]	"TICAM-1, an adapter molecule that participates in Toll-like receptor 3 mediated interferon-beta induction." Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T. Nat. Immunol. 4:161-167(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TICAM1. Tissue: Lung.
[9]	"Recognition of double-stranded RNA by human toll-like receptor 3 and downstream receptor signaling requires multimerization and an acidic pH." de Bouteiller O., Merck E., Hasan U.A., Hubac S., Benguigui B., Trinchieri G., Bates E.E., Caux C. J. Biol. Chem. 280:38133-38145(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-95; CYS-122; ASN-196 AND ASN-247.
[10]	"Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling." Johnsen I.B., Nguyen T.T., Ringdal M., Tryggestad A.M., Bakke O., Lien E., Espevik T., Anthonsen M.W. EMBO J. 25:3335-3346(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRC.
[11]	"The dsRNA binding site of human Toll-like receptor 3." Bell J.K., Askins J., Hall P.R., Davies D.R., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 103:8792-8797(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-539 AND ASN-541.
[12]	"Two tyrosine residues of Toll-like receptor 3 trigger different steps of NF-kappa B activation." Sarkar S.N., Elco C.P., Peters K.L., Chattopadhyay S., Sen G.C. J. Biol. Chem. 282:3423-3427(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-759 AND TYR-858, FUNCTION, MUTAGENESIS OF TYR-759.
[13]	"The TLR3 signaling complex forms by cooperative receptor dimerization." Leonard J.N., Ghirlando R., Askins J., Bell J.K., Margulies D.H., Davies D.R., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 105:258-263(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOUBLE-STRANDED RNA-BINDING, HOMODIMERIZATION.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-57, MASS SPECTROMETRY. Tissue: Liver.
[15]	"The molecular structure of the Toll-like receptor 3 ligand-binding domain." Bell J.K., Botos I., Hall P.R., Askins J., Shiloach J., Segal D.M., Davies D.R. Proc. Natl. Acad. Sci. U.S.A. 102:10976-10980(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-703, FUNCTION, MASS SPECTROMETRY, 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.
[16]	"Crystal structure of human toll-like receptor 3 (TLR3) ectodomain." Choe J., Kelker M.S., Wilson I.A. Science 309:581-585(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-700, DISULFIDE BONDS, GLYCOSYLATION AT ASN-124; ASN-252; ASN-275; ASN-291; ASN-398; ASN-413 AND ASN-507.
[17]	"TLR3 deficiency in patients with herpes simplex encephalitis." 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. Casanova J.-L. Science 317:1522-1527(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HSE2 SER-554.
[18]	"Toll-like receptor 3 and geographic atrophy in age-related macular degeneration." 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. Zhang K. N. Engl. J. Med. 359:1456-1463(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHE-412.
[19]	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. Zhang K. N. Engl. J. Med. 359:1859-1859(2008)
[20]	"A common polymorphism in TLR3 confers natural resistance to HIV-1 infection." 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. J. Immunol. 188:818-823(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHE-412.
+	Additional computationally mapped references.

Web resources

TLR3base

TLR3 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U88879 mRNA. Translation: AAC34134.1.
DQ445682 mRNA. Translation: ABE01399.1.
AB445631 mRNA. Translation: BAG55028.1.
CH471056 Genomic DNA. Translation: EAX04628.1.
BC096333 mRNA. Translation: AAH96333.1.
BC096334 mRNA. Translation: AAH96334.1.
BC096335 mRNA. Translation: AAH96335.1.

IPI

IPI00019007.

RefSeq

NP_003256.1. NM_003265.2.

UniGene

Hs.657724.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZIW	X-ray	2.10	A	27-700	[»]
2A0Z	X-ray	2.40	A	22-703	[»]
3ULU	X-ray	3.52	A	22-702	[»]
3ULV	X-ray	3.52	A	22-702	[»]

ProteinModelPortal

O15455.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29660N.

IntAct

O15455. 1 interaction.

MINT

MINT-2840066.

STRING

9606.ENSP00000296795.

PTM databases

PhosphoSite

O15455.

Proteomic databases

PaxDb

O15455.

PRIDE

O15455.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296795; ENSP00000296795; ENSG00000164342.

GeneID

7098.

KEGG

hsa:7098.

UCSC

uc003iyq.3. human.

Organism-specific databases

CTD

7098.

GeneCards

GC04P186990.

HGNC

HGNC:11849. TLR3.

HPA

CAB025658.

MIM

603029. gene.
613002. phenotype.

neXtProt

NX_O15455.

Orphanet

1930. Herpetic encephalitis.

PharmGKB

PA36551.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4886.

HOGENOM

HOG000251618.

HOVERGEN

HBG023181.

InParanoid

O15455.

KO

K05401.

OMA

IANINDD.

OrthoDB

EOG4N30N8.

PhylomeDB

O15455.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O15455.

Bgee

O15455.

CleanEx

HS_TLR3.

Genevestigator

O15455.

GermOnline

ENSG00000164342. Homo sapiens.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
IPR027173. TLR3.
[Graphical view]

PANTHER

PTHR24365:SF5. PTHR24365:SF5. 1 hit.

Pfam

PF01582. TIR. 1 hit.
[Graphical view]

SMART

SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF52200. TIR. 1 hit.

PROSITE

PS51450. LRR. 19 hits.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075113.

EvolutionaryTrace

O15455.

GenomeRNAi

7098.

NextBio

27769.

SOURCE

Search...

Entry information

Entry name

TLR3_HUMAN

Accession

Primary (citable) accession number: O15455
Secondary accession number(s): Q4VAL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.