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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 705679LumenalSequence analysisAdd
BLAST
Transmembranei706 – 72621HelicalSequence analysisAdd
BLAST
Topological domaini727 – 904178CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 904878Toll-like receptor 3PRO_0000253496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 38By similarity
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence analysis
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence analysis
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi96 ↔ 123By similarity
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence analysis
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence analysis
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi650 ↔ 678By similarity
Disulfide bondi652 ↔ 697By similarity
Glycosylationi663 – 6631N-linked (GlcNAc...)Sequence analysis
Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence analysis
Modified residuei759 – 7591PhosphotyrosineBy similarity
Modified residuei858 – 8581PhosphotyrosineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 5226LRRNTAdd
BLAST
Repeati53 – 7422LRR 1Add
BLAST
Repeati77 – 9822LRR 2Add
BLAST
Repeati101 – 12222LRR 3Add
BLAST
Repeati125 – 14622LRR 4Add
BLAST
Repeati149 – 17022LRR 5Add
BLAST
Repeati173 – 19422LRR 6Add
BLAST
Repeati199 – 22022LRR 7Add
BLAST
Repeati223 – 24523LRR 8Add
BLAST
Repeati250 – 27122LRR 9Add
BLAST
Repeati276 – 29722LRR 10Add
BLAST
Repeati300 – 32122LRR 11Add
BLAST
Repeati324 – 34522LRR 12Add
BLAST
Repeati357 – 37822LRR 13Add
BLAST
Repeati381 – 40121LRR 14Add
BLAST
Repeati409 – 43022LRR 15Add
BLAST
Repeati433 – 45523LRR 16Add
BLAST
Repeati466 – 48722LRR 17Add
BLAST
Repeati508 – 52922LRR 18Add
BLAST
Repeati532 – 55322LRR 19Add
BLAST
Repeati564 – 58522LRR 20Add
BLAST
Repeati588 – 60922LRR 21Add
BLAST
Repeati612 – 63322LRR 22Add
BLAST
Domaini646 – 69954LRRCTAdd
BLAST
Domaini754 – 896143TIRPROSITE-ProRule annotationAdd
BLAST

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.