Tlr7

Domain

Contains two binding domains, first site for small ligands and second site for ssRNA.

Function

Endosomal receptor that plays a key role in innate and adaptive immunity. Controls host immune response against pathogens through recognition of uridine-containing single strand RNAs (ssRNAs) of viral origin or guanosine analogs (PubMed:21402738). Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction. In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively (By similarity) (PubMed:14976261).

Post-translational modifications

The first cleavage is performed by asparagine endopeptidase or cathepsin family members. This initial cleavage event is followed by a trimming event that is solely cathepsin mediated and required for optimal receptor signaling.

Sequence Similarities

Belongs to the Toll-like receptor family.

Cellular localization

• Endosome membrane
• Endoplasmic reticulum membrane
• Single-pass type I membrane protein
• Lysosome
• Cytoplasmic vesicle
• Phagosome
• Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist.

Alternative names

Toll-like receptor 7, Tlr7

Database links

swissprot:P58681 entrezGene:170743

Other research areas

• Immuno-oncology