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Protein

Toll-like receptor 3

Gene

TLR3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 3
Alternative name(s):
CD_antigen: CD283
Gene namesi
Name:TLR3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 705LumenalSequence analysisAdd BLAST679
Transmembranei706 – 726HelicalSequence analysisAdd BLAST21
Topological domaini727 – 904CytoplasmicSequence analysisAdd BLAST178

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000025349627 – 904Toll-like receptor 3Add BLAST878

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 38By similarity
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Glycosylationi58N-linked (GlcNAc...)Sequence analysis1
Glycosylationi71N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi96 ↔ 123By similarity
Glycosylationi125N-linked (GlcNAc...)Sequence analysis1
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Glycosylationi248N-linked (GlcNAc...)Sequence analysis1
Glycosylationi253N-linked (GlcNAc...)Sequence analysis1
Glycosylationi276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi399N-linked (GlcNAc...)Sequence analysis1
Glycosylationi637N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi650 ↔ 678By similarity
Disulfide bondi652 ↔ 697By similarity
Glycosylationi663N-linked (GlcNAc...)Sequence analysis1
Glycosylationi668N-linked (GlcNAc...)Sequence analysis1
Modified residuei759PhosphotyrosineBy similarity1
Modified residuei858PhosphotyrosineBy similarity1

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ5TJ59.
PRIDEiQ5TJ59.

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) in response to poly(I:C) and this interaction is enhanced in the presence of WDFY1. Interacts with SRC; upon binding of double-stranded RNA. The tyrosine-phosphorylated form (via TIR domain) interacts with WDFY1 (via WD repeat 2) in response to poly(I:C).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011445.

Structurei

3D structure databases

ProteinModelPortaliQ5TJ59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 52LRRNTAdd BLAST26
Repeati53 – 74LRR 1Add BLAST22
Repeati77 – 98LRR 2Add BLAST22
Repeati101 – 122LRR 3Add BLAST22
Repeati125 – 146LRR 4Add BLAST22
Repeati149 – 170LRR 5Add BLAST22
Repeati173 – 194LRR 6Add BLAST22
Repeati199 – 220LRR 7Add BLAST22
Repeati223 – 245LRR 8Add BLAST23
Repeati250 – 271LRR 9Add BLAST22
Repeati276 – 297LRR 10Add BLAST22
Repeati300 – 321LRR 11Add BLAST22
Repeati324 – 345LRR 12Add BLAST22
Repeati357 – 378LRR 13Add BLAST22
Repeati381 – 401LRR 14Add BLAST21
Repeati409 – 430LRR 15Add BLAST22
Repeati433 – 455LRR 16Add BLAST23
Repeati466 – 487LRR 17Add BLAST22
Repeati508 – 529LRR 18Add BLAST22
Repeati532 – 553LRR 19Add BLAST22
Repeati564 – 585LRR 20Add BLAST22
Repeati588 – 609LRR 21Add BLAST22
Repeati612 – 633LRR 22Add BLAST22
Domaini646 – 699LRRCTAdd BLAST54
Domaini754 – 896TIRPROSITE-ProRule annotationAdd BLAST143

Domaini

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

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 22 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
HOVERGENiHBG023181.
InParanoidiQ5TJ59.
KOiK05401.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027173. TLR3.
[Graphical view]
PANTHERiPTHR24365:SF5. PTHR24365:SF5. 2 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 16 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 20 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5TJ59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPLPYHIH FFSGLLTCWI LCTSSAHKCT VRHEVADCSH LKLTQIPDDL
60 70 80 90 100
PTNITVLNLT HNQLRRLPPA NFTRYSQLTT LDGGFNSISK LEPELCQSLP
110 120 130 140 150
WLEILNLQHN EISQLSDKTF IFCMNLTELH LMSNSIQKIK NDPFKNLKNL
160 170 180 190 200
IKLDLSHNGL SSTKLGTQLQ LENLQELLLS NNKISSLTPG EFDFLGNSSL
210 220 230 240 250
KRLELSSNQI KEFSPGCFHT LGELSGLSLN NAKLSPSLTE KLCLELSNTS
260 270 280 290 300
IENLSLSSNQ LDTISHTTFD GLKQTNLTTL DLSRNSLRVM GNDSFAWLPH
310 320 330 340 350
LEYLSLEYNN IEHLSSRSFY GLSNLRRLDL RRSFTRQSIS LTSLPKIDDF
360 370 380 390 400
SFQWLKCLEY LNMDDNNFPG IKRNTFTGLV RLKFLSLSNS FSSLRTLTNE
410 420 430 440 450
TFLSLAGCPL LLLDLTKNKI SKIQSGAFSW LGHLEVLDLG LNEIGQELTG
460 470 480 490 500
QEWRGLDNIV EIYLSYNKYL ELTTNSFTSV PSLQRLMLRR VALKNVDCSP
510 520 530 540 550
SPFRPLPNLV ILDLSNNNIA NINDELLKGL EKLEILDLQH NNLARLWKHA
560 570 580 590 600
NPGGPVQFLK GLFHLHILNL GSNGFDEIPV EAFKDLRELK SIDLGMNNLN
610 620 630 640 650
ILPQSVFDNQ VSLKSLSLQK NLITSVQKTV FGPAFRNLSY LDMRFNPFDC
660 670 680 690 700
TCESIAWFVN WINITHTNIS ELSNHYLCNT PPQYHGYPVM LFDVSPCKDS
710 720 730 740 750
APFELLFMIN INILLIFIFI VLLIHFEGWR ISFYWNVSVH RVLGFKEIDR
760 770 780 790 800
AEQFEYAAYI IHAYKDRDWV WKHSSPMEDE DHTLRFCLEE RDFEAGVLEL
810 820 830 840 850
EAIVNSIRRS RKIIFVVTQN LLKDPLCKRF KVHHAVQQAI EQNLDSIILI
860 870 880 890 900
FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERVNAFH HKLKVALGSR

NSAH
Length:904
Mass (Da):103,658
Last modified:December 21, 2004 - v1
Checksum:i609CD7BEDA5C6C2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ812026 mRNA. Translation: CAH19226.1.
RefSeqiNP_001008664.1. NM_001008664.1.
UniGeneiBt.12298.

Genome annotation databases

GeneIDi281535.
KEGGibta:281535.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ812026 mRNA. Translation: CAH19226.1.
RefSeqiNP_001008664.1. NM_001008664.1.
UniGeneiBt.12298.

3D structure databases

ProteinModelPortaliQ5TJ59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011445.

Proteomic databases

PaxDbiQ5TJ59.
PRIDEiQ5TJ59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281535.
KEGGibta:281535.

Organism-specific databases

CTDi7098.

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
HOVERGENiHBG023181.
InParanoidiQ5TJ59.
KOiK05401.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027173. TLR3.
[Graphical view]
PANTHERiPTHR24365:SF5. PTHR24365:SF5. 2 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 16 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 20 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTLR3_BOVIN
AccessioniPrimary (citable) accession number: Q5TJ59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.