The Toll-like receptor (TLR) family in mammal comprises a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain and IL-1 receptor motif in the cytoplasmic domain. Like its counterparts in Drosophila, TLRs signal through adaptor molecules. The TRL family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition. TLRs characterized so far activate the MyD88/interleukin-1 receptor-associated kinase (IRAK) signaling pathway. Ten human homologs of TLRs (TLR1-10) have been described. The amino acid sequence of human TLR6 is most similar to hTLR1 with 69% identity at the amino acid level. Human TLR6 consists of a predicted 807 amino acids with a molecular weight of approximately 92 kDa. Human and mouse TLR6 share an amino acid identity of 73%. TLR6 activates both NF-kB and c-Jun N-terminal Kinase (JNK). The amino acids in the cytoplasmic domain of IL-1 receptor, which are critical for NF-kB activation, are conserved in TLR6. It has also been shown that TLR2-mediated response to a phenol-soluble factor from staphylococcus epidermidis is enhanced by TLR6. TLR6 is predominantly expressed in spleen, thymus, ovary, and lung.
Synonyms
CD286
Note
Immunohistochemistry-Paraffin and Flow cytometry/(Intracellular)
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