Q0GC71 · TLR2_CAPHI

  • Protein
    Toll-like receptor 2
  • Gene
    TLR2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).
May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity).

Caution

In some plant proteins and in human SARM1, the TIR domain has NAD+ hydrolase (NADase) activity (By similarity).
However, despite the presence of the catalytic Asp residue, the isolated TIR domain of human TLR4 lacks NADase activity (By similarity).
Based on this, it is unlikely that Toll-like receptors have NADase activity

Features

Showing features for site.

1784100200300400500600700
TypeIDPosition(s)Description
Site349Interaction with bacterial lipopeptide

GO annotations

AspectTerm
Cellular ComponentGolgi apparatus
Cellular Componentmembrane raft
Cellular Componentphagocytic vesicle membrane
Molecular FunctionNAD+ nucleotidase, cyclic ADP-ribose generating
Molecular Functiontransmembrane signaling receptor activity
Molecular Functiontriacyl lipopeptide binding
Biological Processcellular response to diacyl bacterial lipopeptide
Biological Processcellular response to triacyl bacterial lipopeptide
Biological Processinflammatory response
Biological Processinnate immune response
Biological Processtoll-like receptor signaling pathway

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Toll-like receptor 2
  • CD Antigen Name
    • CD282

Gene names

    • Name
      TLR2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Capra

Accessions

  • Primary accession
    Q0GC71

Proteomes

Subcellular Location

Membrane
; Single-pass type I membrane protein
Cytoplasmic vesicle, phagosome membrane
; Single-pass type I membrane protein
Membrane raft
Note: Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain21-587Extracellular
Transmembrane588-608Helical
Topological domain609-784Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, cross-link.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000036377521-784Toll-like receptor 2
Disulfide bond30↔36
Glycosylation114N-linked (GlcNAc...) asparagine
Glycosylation199N-linked (GlcNAc...) asparagine
Glycosylation248N-linked (GlcNAc...) asparagine
Disulfide bond353↔382
Disulfide bond432↔454
Glycosylation442N-linked (GlcNAc...) asparagine
Cross-link754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2.
Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2.

Keywords

PTM databases

Interaction

Subunit

Interacts with LY96, TLR1 and TLR6 (via extracellular domain). TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before stimulation by the ligand. The heterodimers form bigger oligomers in response to their corresponding ligands as well as further heterotypic associations with other receptors such as CD14 and/or CD36. Binds MYD88 (via TIR domain). Interacts with TICAM1. Interacts with CNPY3. Interacts with ATG16L1. Interacts with PPP1R11. Interacts with TICAM2. Interacts with TIRAP (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, domain, motif.

TypeIDPosition(s)Description
Repeat54-77LRR 1
Repeat78-101LRR 2
Repeat102-125LRR 3
Repeat126-150LRR 4
Repeat151-175LRR 5
Repeat176-199LRR 6
Repeat200-223LRR 7
Repeat224-250LRR 8
Repeat251-278LRR 9
Repeat279-308LRR 10
Repeat309-337LRR 11
Repeat338-361LRR 12
Repeat362-388LRR 13
Repeat389-414LRR 14
Repeat415-437LRR 15
Repeat438-457LRR 16
Repeat458-478LRR 17
Repeat479-500LRR 18
Repeat501-524LRR 19
Domain525-579LRRCT
Domain639-782TIR
Motif761-778ATG16L1-binding motif

Domain

Ester-bound lipid substrates are bound through a crevice formed between the LRR 11 and LRR 12.
The ATG16L1-binding motif mediates interaction with ATG16L1.

Sequence similarities

Belongs to the Toll-like receptor family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    784
  • Mass (Da)
    90,067
  • Last updated
    2006-10-03 v1
  • Checksum
    C3434B760BB92E6A
MPRALWTAWVWAVIILSMEGASHQASSLSCDPTGVCDGHSRSLNSIPSGLTDGVKSLDLSNNEITYVSNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYALKFLNLLGNVYKTLGETSLFSHLPNLRTLKVGNSNSFTEIHEKDFTGLIFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFHDLSSIYPLTGKVKRVTIESSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAIRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ872435
EMBL· GenBank· DDBJ
ABI31733.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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