CLEC4F

CLEC4F, or C-type lectin domain family 4 member F, is a protein-coding gene that encodes a member of the C-type lectin receptor (CLR) family. The protein is a type II transmembrane receptor that contains a single C-type lectin-like carbohydrate recognition domain in its extracellular region and a short cytoplasmic tail equipped for endocytosis, enabling the internalization of bound ligands.

Expression of CLEC4F is strongest in tissue-resident macrophages, particularly Kupffer cells in the liver. In humans, CLEC4F shows a similar macrophage-associated expression pattern, though cross-species differences in distribution and regulation are noted. The receptor is generally considered part of the liver’s scavenger system, contributing to immune surveillance and clearance processes carried out by hepatic macrophages.

Ligands and function are centered on glycan recognition. CLEC4F binds glycoproteins that display terminal galactose or N-acetylgalactosamine residues, especially when desialylated. Upon binding, the receptor mediates endocytosis and removal of these glycoproteins from circulation, contributing to the turnover of circulating glycoproteins and the clearance of aged or altered cells and particles.

Research context and relevance: CLEC4F has been studied primarily in mouse models, where its activity supports liver macrophage function and glycoprotein clearance. In humans, the precise physiological and clinical roles of CLEC4F are still under investigation, but the receptor is regarded as a component of hepatic immune homeostasis and glycoprotein metabolism.