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O15455

- TLR3_HUMAN

UniProt

O15455 - TLR3_HUMAN

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Protein
Toll-like receptor 3
Gene
TLR3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.9 Publications

GO - Molecular functioni

  1. double-stranded RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. receptor activity Source: ProtInc
  4. transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  1. I-kappaB kinase/NF-kappaB signaling Source: Reactome
  2. I-kappaB phosphorylation Source: BHF-UCL
  3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  4. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  5. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  6. cellular response to drug Source: Ensembl
  7. cellular response to exogenous dsRNA Source: Ensembl
  8. cellular response to interferon-beta Source: Ensembl
  9. cellular response to interferon-gamma Source: Ensembl
  10. cellular response to mechanical stimulus Source: UniProtKB
  11. defense response to bacterium Source: ProtInc
  12. defense response to virus Source: BHF-UCL
  13. detection of virus Source: UniProtKB
  14. extrinsic apoptotic signaling pathway Source: UniProtKB
  15. hyperosmotic response Source: UniProtKB
  16. inflammatory response Source: UniProtKB-KW
  17. innate immune response Source: BHF-UCL
  18. male gonad development Source: Ensembl
  19. microglial cell activation involved in immune response Source: Ensembl
  20. necroptotic signaling pathway Source: UniProtKB
  21. negative regulation of osteoclast differentiation Source: UniProtKB
  22. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
  23. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  24. positive regulation of JNK cascade Source: Ensembl
  25. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  26. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  27. positive regulation of apoptotic process Source: Ensembl
  28. positive regulation of chemokine biosynthetic process Source: Ensembl
  29. positive regulation of chemokine production Source: BHF-UCL
  30. positive regulation of inflammatory response Source: BHF-UCL
  31. positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
  32. positive regulation of interferon-beta biosynthetic process Source: UniProtKB
  33. positive regulation of interferon-beta production Source: BHF-UCL
  34. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
  35. positive regulation of interleukin-12 production Source: BHF-UCL
  36. positive regulation of interleukin-6 production Source: BHF-UCL
  37. positive regulation of interleukin-8 production Source: BHF-UCL
  38. positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
  39. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  40. positive regulation of tumor necrosis factor production Source: BHF-UCL
  41. positive regulation of type III interferon production Source: Ensembl
  42. response to exogenous dsRNA Source: MGI
  43. signal transduction Source: ProtInc
  44. toll-like receptor 3 signaling pathway Source: Reactome
  45. toll-like receptor 4 signaling pathway Source: Reactome
  46. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_150361. TRIF-mediated programmed cell death.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_6783. Toll Like Receptor 3 (TLR3) Cascade.
SignaLinkiO15455.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 3
Alternative name(s):
CD_antigen: CD283
Gene namesi
Name:TLR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11849. TLR3.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 704681Lumenal Reviewed prediction
Add
BLAST
Transmembranei705 – 72521Helical; Reviewed prediction
Add
BLAST
Topological domaini726 – 904179Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. cytoplasm Source: BHF-UCL
  3. endolysosome membrane Source: Reactome
  4. endoplasmic reticulum membrane Source: Reactome
  5. endosome membrane Source: Reactome
  6. integral component of plasma membrane Source: ProtInc
  7. lysosomal membrane Source: UniProtKB
  8. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti554 – 5541P → S in HSE2; causes TLR3 deficiency and predisposition to herpes simplex encephalitis. 1 Publication
VAR_054887

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951C → A: Reduced response to ds-RNA. 1 Publication
Mutagenesisi122 – 1221C → A: Reduced response to ds-RNA. 1 Publication
Mutagenesisi196 – 1961N → G: Reduced expression levels; when associated with R-247. 1 Publication
Mutagenesisi247 – 2471N → R: Reduced response to ds-RNA. Reduced expression levels; when associated with G-196. 1 Publication
Mutagenesisi539 – 5391H → A: No effect. 1 Publication
Mutagenesisi539 – 5391H → E: Loss of RNA binding. Constitutive activation of NF-kappa-B. 1 Publication
Mutagenesisi541 – 5411N → A: Loss of RNA binding. Abolishes activation of NF-kappa-B. 1 Publication
Mutagenesisi759 – 7591Y → F: Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613002. phenotype.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA36551.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 904881Toll-like receptor 3
PRO_0000034715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 373 Publications
Glycosylationi52 – 521N-linked (GlcNAc...)3 Publications
Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)2 Publications
Disulfide bondi95 ↔ 1223 Publications
Glycosylationi124 – 1241N-linked (GlcNAc...)2 Publications
Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
Glycosylationi247 – 2471N-linked (GlcNAc...)1 Publication
Glycosylationi252 – 2521N-linked (GlcNAc...)3 Publications
Glycosylationi265 – 2651N-linked (GlcNAc...)2 Publications
Glycosylationi275 – 2751N-linked (GlcNAc...)3 Publications
Glycosylationi291 – 2911N-linked (GlcNAc...)3 Publications
Glycosylationi398 – 3981N-linked (GlcNAc...)3 Publications
Glycosylationi413 – 4131N-linked (GlcNAc...)3 Publications
Glycosylationi507 – 5071N-linked (GlcNAc...)3 Publications
Glycosylationi636 – 6361N-linked (GlcNAc...)1 Publication
Disulfide bondi649 ↔ 6773 Publications
Disulfide bondi651 ↔ 6963 Publications
Glycosylationi662 – 6621N-linked (GlcNAc...) Reviewed prediction
Modified residuei759 – 7591Phosphotyrosine1 Publication
Modified residuei858 – 8581Phosphotyrosine1 Publication

Post-translational modificationi

Heavily N-glycosylated, except on that part of the surface of the ectodomain that is involved in ligand binding.3 Publications
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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO15455.
PaxDbiO15455.
PRIDEiO15455.

PTM databases

PhosphoSiteiO15455.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiO15455.
BgeeiO15455.
CleanExiHS_TLR3.
GenevestigatoriO15455.

Organism-specific databases

HPAiCAB025658.

Interactioni

Subunit structurei

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 TICAM1 (via the TIR domain); mediates TLR3 signaling. Interacts with SRC; upon binding of double-stranded RNA.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R1P279862EBI-6116630,EBI-79464

Protein-protein interaction databases

BioGridi112953. 15 interactions.
DIPiDIP-29660N.
IntActiO15455. 6 interactions.
MINTiMINT-2840066.
STRINGi9606.ENSP00000296795.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 366
Beta strandi47 – 493
Beta strandi54 – 574
Helixi68 – 747
Beta strandi78 – 814
Helixi94 – 974
Beta strandi103 – 1053
Turni118 – 1214
Beta strandi126 – 1294
Turni142 – 1454
Beta strandi151 – 1533
Beta strandi166 – 1683
Beta strandi175 – 1773
Helixi188 – 1914
Helixi192 – 1943
Beta strandi198 – 2036
Helixi216 – 2194
Beta strandi220 – 2234
Beta strandi225 – 2273
Helixi234 – 24512
Beta strandi252 – 2543
Turni265 – 2684
Helixi269 – 2735
Beta strandi278 – 2803
Turni291 – 2966
Beta strandi302 – 3043
Beta strandi310 – 3134
Turni315 – 3206
Beta strandi326 – 3283
Beta strandi338 – 3403
Turni348 – 3536
Beta strandi359 – 3613
Turni372 – 3776
Beta strandi383 – 3853
Turni398 – 4014
Helixi402 – 4043
Beta strandi411 – 4133
Turni424 – 4296
Beta strandi435 – 4373
Beta strandi444 – 4463
Helixi450 – 4523
Beta strandi460 – 4623
Beta strandi467 – 4704
Turni473 – 4786
Beta strandi484 – 4863
Turni501 – 5044
Beta strandi510 – 5123
Turni523 – 5286
Beta strandi534 – 5363
Helixi543 – 5464
Turni557 – 5604
Beta strandi566 – 5683
Turni579 – 5846
Beta strandi590 – 5923
Turni603 – 6086
Beta strandi614 – 6163
Helixi627 – 6348
Beta strandi638 – 6414
Beta strandi655 – 6584
Helixi671 – 6744
Beta strandi676 – 6805
Helixi688 – 6903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZIWX-ray2.10A27-700[»]
2A0ZX-ray2.40A22-703[»]
3ULUX-ray3.52A22-702[»]
3ULVX-ray3.52A22-702[»]
ProteinModelPortaliO15455.
SMRiO15455. Positions 26-897.

Miscellaneous databases

EvolutionaryTraceiO15455.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5128LRRNT
Add
BLAST
Repeati52 – 7322LRR 1
Add
BLAST
Repeati76 – 9722LRR 2
Add
BLAST
Repeati100 – 12122LRR 3
Add
BLAST
Repeati124 – 14522LRR 4
Add
BLAST
Repeati148 – 16821LRR 5
Add
BLAST
Repeati172 – 19322LRR 6
Add
BLAST
Repeati198 – 21922LRR 7
Add
BLAST
Repeati222 – 24423LRR 8
Add
BLAST
Repeati249 – 27022LRR 9
Add
BLAST
Repeati275 – 29622LRR 10
Add
BLAST
Repeati299 – 32022LRR 11
Add
BLAST
Repeati323 – 34422LRR 12
Add
BLAST
Repeati356 – 37722LRR 13
Add
BLAST
Repeati380 – 40021LRR 14
Add
BLAST
Repeati408 – 42922LRR 15
Add
BLAST
Repeati432 – 45423LRR 16
Add
BLAST
Repeati465 – 48622LRR 17
Add
BLAST
Repeati507 – 52822LRR 18
Add
BLAST
Repeati531 – 55222LRR 19
Add
BLAST
Repeati563 – 58422LRR 20
Add
BLAST
Repeati587 – 60822LRR 21
Add
BLAST
Repeati611 – 63222LRR 22
Add
BLAST
Domaini645 – 69854LRRCT
Add
BLAST
Domaini754 – 896143TIR
Add
BLAST

Domaini

ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18.

Sequence similaritiesi

Contains 1 LRRCT domain.
Contains 1 LRRNT domain.
Contains 1 TIR domain.

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4886.
HOGENOMiHOG000251618.
HOVERGENiHBG023181.
InParanoidiO15455.
KOiK05401.
OMAiIANINDD.
OrthoDBiEOG79SDZG.
PhylomeDBiO15455.
TreeFamiTF325595.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. 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]
PANTHERiPTHR24365:SF5. PTHR24365:SF5. 1 hit.
PfamiPF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 19 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15455-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MRQTLPCIYF WGGLLPFGML CASSTTKCTV SHEVADCSHL KLTQVPDDLP    50
TNITVLNLTH NQLRRLPAAN FTRYSQLTSL DVGFNTISKL EPELCQKLPM 100
LKVLNLQHNE LSQLSDKTFA FCTNLTELHL MSNSIQKIKN NPFVKQKNLI 150
TLDLSHNGLS STKLGTQVQL ENLQELLLSN NKIQALKSEE LDIFANSSLK 200
KLELSSNQIK EFSPGCFHAI GRLFGLFLNN VQLGPSLTEK LCLELANTSI 250
RNLSLSNSQL STTSNTTFLG LKWTNLTMLD LSYNNLNVVG NDSFAWLPQL 300
EYFFLEYNNI QHLFSHSLHG LFNVRYLNLK RSFTKQSISL ASLPKIDDFS 350
FQWLKCLEHL NMEDNDIPGI KSNMFTGLIN LKYLSLSNSF TSLRTLTNET 400
FVSLAHSPLH ILNLTKNKIS KIESDAFSWL GHLEVLDLGL NEIGQELTGQ 450
EWRGLENIFE IYLSYNKYLQ LTRNSFALVP SLQRLMLRRV ALKNVDSSPS 500
PFQPLRNLTI LDLSNNNIAN INDDMLEGLE KLEILDLQHN NLARLWKHAN 550
PGGPIYFLKG LSHLHILNLE SNGFDEIPVE VFKDLFELKI IDLGLNNLNT 600
LPASVFNNQV SLKSLNLQKN LITSVEKKVF GPAFRNLTEL DMRFNPFDCT 650
CESIAWFVNW INETHTNIPE LSSHYLCNTP PHYHGFPVRL FDTSSCKDSA 700
PFELFFMINT SILLIFIFIV LLIHFEGWRI SFYWNVSVHR VLGFKEIDRQ 750
TEQFEYAAYI IHAYKDKDWV WEHFSSMEKE DQSLKFCLEE RDFEAGVFEL 800
EAIVNSIKRS RKIIFVITHH LLKDPLCKRF KVHHAVQQAI EQNLDSIILV 850
FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERIGAFR HKLQVALGSK 900
NSVH 904
Length:904
Mass (Da):103,829
Last modified:January 1, 1998 - v1
Checksum:i034E05ECA7A4D2F7
GO
Isoform 2 (identifier: O15455-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-277: Missing.

Note: No experimental confirmation available.

Show »
Length:627
Mass (Da):72,937
Checksum:i0D376D88306EBEFC
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti284 – 2841N → I.
Corresponds to variant rs5743316 [ dbSNP | Ensembl ].
VAR_052361
Natural varianti307 – 3071Y → D.
Corresponds to variant rs5743317 [ dbSNP | Ensembl ].
VAR_052362
Natural varianti412 – 4121L → F.4 Publications
Corresponds to variant rs3775291 [ dbSNP | Ensembl ].
VAR_021976
Natural varianti554 – 5541P → S in HSE2; causes TLR3 deficiency and predisposition to herpes simplex encephalitis. 1 Publication
VAR_054887
Natural varianti737 – 7371S → T.
Corresponds to variant rs5743318 [ dbSNP | Ensembl ].
VAR_024664

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 277277Missing in isoform 2.
VSP_054188Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901G → R in BAG36884. 1 Publication
Sequence conflicti575 – 5751D → N in AAH94737. 1 Publication
Sequence conflicti605 – 6051V → A in BAG36884. 1 Publication
Sequence conflicti663 – 6631E → G in BAG36884. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88879 mRNA. Translation: AAC34134.1.
DQ445682 mRNA. Translation: ABE01399.1.
AB445631 mRNA. Translation: BAG55028.1.
DQ360814 Genomic DNA. Translation: ABC86908.1.
DQ360815 Genomic DNA. Translation: ABC86909.1.
DQ360816 Genomic DNA. Translation: ABC86910.1.
AK302143 mRNA. Translation: BAH13636.1.
AK314208 mRNA. Translation: BAG36884.1.
AC104070 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04628.1.
BC094737 mRNA. Translation: AAH94737.1.
BC096333 mRNA. Translation: AAH96333.1.
BC096334 mRNA. Translation: AAH96334.1.
BC096335 mRNA. Translation: AAH96335.1.
CCDSiCCDS3846.1. [O15455-1]
RefSeqiNP_003256.1. NM_003265.2. [O15455-1]
XP_006714357.1. XM_006714294.1. [O15455-1]
UniGeneiHs.657724.

Genome annotation databases

EnsembliENST00000296795; ENSP00000296795; ENSG00000164342.
ENST00000504367; ENSP00000423684; ENSG00000164342.
GeneIDi7098.
KEGGihsa:7098.
UCSCiuc003iyq.3. human. [O15455-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

TLR3base

TLR3 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88879 mRNA. Translation: AAC34134.1 .
DQ445682 mRNA. Translation: ABE01399.1 .
AB445631 mRNA. Translation: BAG55028.1 .
DQ360814 Genomic DNA. Translation: ABC86908.1 .
DQ360815 Genomic DNA. Translation: ABC86909.1 .
DQ360816 Genomic DNA. Translation: ABC86910.1 .
AK302143 mRNA. Translation: BAH13636.1 .
AK314208 mRNA. Translation: BAG36884.1 .
AC104070 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04628.1 .
BC094737 mRNA. Translation: AAH94737.1 .
BC096333 mRNA. Translation: AAH96333.1 .
BC096334 mRNA. Translation: AAH96334.1 .
BC096335 mRNA. Translation: AAH96335.1 .
CCDSi CCDS3846.1. [O15455-1 ]
RefSeqi NP_003256.1. NM_003265.2. [O15455-1 ]
XP_006714357.1. XM_006714294.1. [O15455-1 ]
UniGenei Hs.657724.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O15455.
SMRi O15455. Positions 26-897.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112953. 15 interactions.
DIPi DIP-29660N.
IntActi O15455. 6 interactions.
MINTi MINT-2840066.
STRINGi 9606.ENSP00000296795.

Chemistry

ChEMBLi CHEMBL1075113.
GuidetoPHARMACOLOGYi 1753.

PTM databases

PhosphoSitei O15455.

Proteomic databases

MaxQBi O15455.
PaxDbi O15455.
PRIDEi O15455.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296795 ; ENSP00000296795 ; ENSG00000164342 .
ENST00000504367 ; ENSP00000423684 ; ENSG00000164342 .
GeneIDi 7098.
KEGGi hsa:7098.
UCSCi uc003iyq.3. human. [O15455-1 ]

Organism-specific databases

CTDi 7098.
GeneCardsi GC04P186990.
HGNCi HGNC:11849. TLR3.
HPAi CAB025658.
MIMi 603029. gene.
613002. phenotype.
neXtProti NX_O15455.
Orphaneti 1930. Herpetic encephalitis.
PharmGKBi PA36551.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000251618.
HOVERGENi HBG023181.
InParanoidi O15455.
KOi K05401.
OMAi IANINDD.
OrthoDBi EOG79SDZG.
PhylomeDBi O15455.
TreeFami TF325595.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_150361. TRIF-mediated programmed cell death.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_6783. Toll Like Receptor 3 (TLR3) Cascade.
SignaLinki O15455.

Miscellaneous databases

EvolutionaryTracei O15455.
GeneWikii TLR_3.
GenomeRNAii 7098.
NextBioi 27769.
PROi O15455.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15455.
Bgeei O15455.
CleanExi HS_TLR3.
Genevestigatori O15455.

Family and domain databases

Gene3Di 3.40.50.10140. 1 hit.
InterProi 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 ]
PANTHERi PTHR24365:SF5. PTHR24365:SF5. 1 hit.
Pfami PF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view ]
SMARTi SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS51450. LRR. 19 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  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] (ISOFORM 1), 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] (ISOFORM 1).
  4. "TLR polymorphism."
    Macquin C., Bahram S.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-412.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT PHE-412.
    Tissue: Testis and Thymus.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. Cited for: FUNCTION, MUTAGENESIS OF HIS-539 AND ASN-541.
  15. "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.
  16. Cited for: FUNCTION, DOUBLE-STRANDED RNA-BINDING, HOMODIMERIZATION.
  17. "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.
    Tissue: Liver.
  18. Cited for: FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, INTERACTION WITH UNC93B1.
  19. "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, 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, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "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.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 22-702 IN COMPLEX WITH ANTIBODY, DISULFIDE BONDS, SUBUNIT, DS-RNA BINDING REGIONS, 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.
  22. Cited for: VARIANT HSE2 SER-554.
  23. Cited for: VARIANT PHE-412.
  24. Cited for: VARIANT PHE-412.

Entry informationi

Entry nameiTLR3_HUMAN
AccessioniPrimary (citable) accession number: O15455
Secondary accession number(s): B2RAI7
, B7Z7K0, E6Y0F0, E6Y0F1, E9PGH4, Q4VAL2, Q504W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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