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). 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. 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. 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. 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. Belongs to the Toll-like receptor family. 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. A natural deletion may however lead to truncated protein which lacks transmembrane or intracellular domain.