Q0GC71 · TLR2_CAPHI
- ProteinToll-like receptor 2
- GeneTLR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids784 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 349 | Interaction with bacterial lipopeptide | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | membrane raft | |
Cellular Component | phagocytic vesicle membrane | |
Molecular Function | NAD+ nucleotidase, cyclic ADP-ribose generating | |
Molecular Function | transmembrane signaling receptor activity | |
Molecular Function | triacyl lipopeptide binding | |
Biological Process | cellular response to diacyl bacterial lipopeptide | |
Biological Process | cellular response to triacyl bacterial lipopeptide | |
Biological Process | inflammatory response | |
Biological Process | innate immune response | |
Biological Process | toll-like receptor signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameToll-like receptor 2
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Capra
Accessions
- Primary accessionQ0GC71
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Cytoplasmic vesicle, phagosome membrane ; Single-pass type I membrane protein
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-587 | Extracellular | ||||
Sequence: ASHQASSLSCDPTGVCDGHSRSLNSIPSGLTDGVKSLDLSNNEITYVSNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYALKFLNLLGNVYKTLGETSLFSHLPNLRTLKVGNSNSFTEIHEKDFTGLIFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFHDLSSIYPLTGKVKRVTIESSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHR | ||||||
Transmembrane | 588-608 | Helical | ||||
Sequence: AAVVSAVCCALFLLLLLTGVL | ||||||
Topological domain | 609-784 | Cytoplasmic | ||||
Sequence: CHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAIRS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MPRALWTAWVWAVIILSMEG | ||||||
Chain | PRO_0000363775 | 21-784 | Toll-like receptor 2 | |||
Sequence: ASHQASSLSCDPTGVCDGHSRSLNSIPSGLTDGVKSLDLSNNEITYVSNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYALKFLNLLGNVYKTLGETSLFSHLPNLRTLKVGNSNSFTEIHEKDFTGLIFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFHDLSSIYPLTGKVKRVTIESSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAIRS | ||||||
Disulfide bond | 30↔36 | |||||
Sequence: CDPTGVC | ||||||
Glycosylation | 114 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 199 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 248 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 353↔382 | |||||
Sequence: CLLSQHLKSLEYLDLSENLMSEETLKNSAC | ||||||
Disulfide bond | 432↔454 | |||||
Sequence: CQWPGKMKQLNLSSTRIHSLTQC | ||||||
Glycosylation | 442 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Cross-link | 754 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
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
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 54-77 | LRR 1 | ||||
Sequence: VKSLDLSNNEITYVSNRDLQRCVN | ||||||
Repeat | 78-101 | LRR 2 | ||||
Sequence: LKTLRLGANEIHTVEEDSFFHLRN | ||||||
Repeat | 102-125 | LRR 3 | ||||
Sequence: LEYLDLSYNRLSNLSSSWFRSLYA | ||||||
Repeat | 126-150 | LRR 4 | ||||
Sequence: LKFLNLLGNVYKTLGETSLFSHLPN | ||||||
Repeat | 151-175 | LRR 5 | ||||
Sequence: LRTLKVGNSNSFTEIHEKDFTGLIF | ||||||
Repeat | 176-199 | LRR 6 | ||||
Sequence: LEELEISAQNLQIYVPKSLKSIQN | ||||||
Repeat | 200-223 | LRR 7 | ||||
Sequence: ISHLILHLKQPVLLVDILVDIVSS | ||||||
Repeat | 224-250 | LRR 8 | ||||
Sequence: LDCLELRDTNLHTFHFSEASISEMNTS | ||||||
Repeat | 251-278 | LRR 9 | ||||
Sequence: VKKLIFRNVQFTDESFVEVVKLFNYVSG | ||||||
Repeat | 279-308 | LRR 10 | ||||
Sequence: ILEVEFDDCTHDGIGDFRALSLDRIRHLGN | ||||||
Repeat | 309-337 | LRR 11 | ||||
Sequence: VETLTIRKLHIPQFFLFHDLSSIYPLTGK | ||||||
Repeat | 338-361 | LRR 12 | ||||
Sequence: VKRVTIESSKVFLVPCLLSQHLKS | ||||||
Repeat | 362-388 | LRR 13 | ||||
Sequence: LEYLDLSENLMSEETLKNSACKDAWPF | ||||||
Repeat | 389-414 | LRR 14 | ||||
Sequence: LQTLVLRQNRLKSLEKTGELLLTLKN | ||||||
Repeat | 415-437 | LRR 15 | ||||
Sequence: LNNLDISKNNFLSMPETCQWPGK | ||||||
Repeat | 438-457 | LRR 16 | ||||
Sequence: MKQLNLSSTRIHSLTQCLPQ | ||||||
Repeat | 458-478 | LRR 17 | ||||
Sequence: TLEILDVSNNNLDSFSLILPQ | ||||||
Repeat | 479-500 | LRR 18 | ||||
Sequence: LKELYISRNKLKTLPDASFLPV | ||||||
Repeat | 501-524 | LRR 19 | ||||
Sequence: LSVMRISGNIINTFSKEQLDSFPQ | ||||||
Domain | 525-579 | LRRCT | ||||
Sequence: LKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDAR | ||||||
Domain | 639-782 | TIR | ||||
Sequence: LCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAI | ||||||
Motif | 761-778 | ATG16L1-binding motif | ||||
Sequence: YLEWPTDETQQEAFWLNL |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length784
- Mass (Da)90,067
- Last updated2006-10-03 v1
- ChecksumC3434B760BB92E6A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ872435 EMBL· GenBank· DDBJ | ABI31733.1 EMBL· GenBank· DDBJ | mRNA |