Toll-like receptor 2; Toll/interleukin-1 receptor-like protein 4; CD282 (TLR2, TIL4)

Function: 1) cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins & other microbial cell wall components (peptigoglycan, Pan-3) 2) acts via MyD88 & TRAF6 a) NF-kappa-B activation b) cytokine secretion c) inflammatory response 3) promotes apoptosis in response to lipoproteins (putative) 4) recognizes pathogen antigens cooperatively with TLR6 a) mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2) b) soluble tuberculosis factor (STF) c) phenol-soluble modulin (PSM) c) B. burgdorferi outer surface protein A lipoprotein (OspA-L) 5) binds LY96, TLR2 & TLR6 via the extracellular domain 6) binds MyD88 via their respective TIR domains 7) interacts with TICAM1. 8) ligand binding induces the formation of a heterodimer with TLR1 Structure: - glycosylation of Asn-442 involved in secretion of N-terminal ectodomain - belongs to the Toll-like receptor family - contains 14 LRR repeats (leucine-rich repeats) - contains 1 TIR domain Compartment: membrane Expression: - expressed in peripheral blood leukocytes, especially monocytes, bone marrow, lymph node, spleen > lung, fetal liver Polymorphism: - genetic variations in TLR2 are associated with suceptibility to leprosy - Trp-677 polymorphism in the intracellular domain of TLR2 has a role in susceptibility to lepromatous leprosy - wild-type TLR2 mediates CD14-enhanced Mycobacterium leprae- dependent activation of NFKB1, but TLR2 containing the Trp-677 polymorphism des not - impaired function of the Trp-677 polymorphism provides a molecular mechanism for the poor cellular immune response associated with lepromatous leprosy

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen glycoprotein leucine-rich repeat-containing protein (LRRC) toll-like receptor

Properties

SIZE: entity length = 784 aa MW = 90 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-18} cysteine residue {C30} MODIFICATION: cysteine residue {C36} cysteine residue {C36} MODIFICATION: cysteine residue {C30} leucine-rich repeat SITE: 51-74 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 75-98 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 99-122 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N114} leucine-rich repeat SITE: 124-147 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 148-172 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 173-196 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N199} leucine-rich repeat SITE: 221-244 MOTIF: leucine residue (SEVERAL) phenylalanine residue {349} cysteine residue {C353} MODIFICATION: cysteine residue {C382} leucine-rich repeat SITE: 359-384 MOTIF: leucine residue (SEVERAL) cysteine residue {C382} MODIFICATION: cysteine residue {C353} leucine-rich repeat SITE: 386-411 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 412-436 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N414} cysteine residue {C432} MODIFICATION: cysteine residue {C454} leucine-rich repeat SITE: 438-456 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N442} cysteine residue {C454} MODIFICATION: cysteine residue {C432} leucine-rich repeat SITE: 457-476 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 477-499 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 501-521 MOTIF: leucine residue (SEVERAL) transmembrane domain {589-609} TIR domain {639-784}

Database Correlations

OMIM correlations UniProt O60603 PFAM correlations Entrez Gene 7097 Kegg hsa:7097