The mannose receptor (MR/CLEC13D/CD206/MMR/MRC1/Macrophage Mannose Receptor 1) is an endocytic receptor expressed on dendritic cells, macrophages, and avascular endothelium. It is a highly glycosylated type I transmembrane protein featuring three distinct types of extracellular domains and a short carboxyl-terminal cytoplasmic tail that lacks obvious signaling motifs. The extracellular portion of the protein comprises an N-terminal cysteine-rich (CR) domain that binds sulfated sugar chains, a single fibronectin type II (FNII) domain that binds collagen, and eight C-type lectin domains (CTLDs) that recognize carbohydrate ligands containing mannose, fucose, and N-acetylglucosamine (GlcNAc). The receptor continuously cycles between the plasma membrane and early endosomes. Its functions include mediating antigen cross-presentation, facilitating the clearance of endogenous glycoproteins (e.g., maintaining glycoprotein homeostasis), and detecting and transporting pathogens via the lymphatics. The mannose receptor is a canonical marker for M2 macrophages.