Fibrinogen C domain containing 1 (FIBCD1)

Fibrinogen C domain containing 1 (FIBCD1) is a type II transmembrane endocytic receptor primarily expressed on the apical surface of epithelial cells, such as enterocytes in the intestine and airway epithelial cells[3][4][6][7]. The protein is composed of a short cytoplasmic tail, a transmembrane helix, and an extracellular region featuring a coiled-coil domain, polycationic stretch, and a C-terminal fibrinogen-like recognition domain (FReD)[1][2][3][4]. FIBCD1 forms homo-tetramers in the plasma membrane[1][2][3][4]. Its C-terminal domain binds acetylated structures such as chitin and N-acetylated carbohydrates with high affinity in a calcium-dependent manner, playing a likely role in endocytosis and removal of such materials from the extracellular space, and thus contributing to host defense, gut homeostasis, and possibly skin immune surveillance[2][3][4][5]. FIBCD1 is homologous to ficolins, which are well-characterized pattern recognition molecules involved in the innate immune response[3][4][5]. To date, there are no reported drugs specifically targeting FIBCD1, and its potential as a therapeutic target remains to be defined. FIBCD1 may have diagnostic or physiological significance in some settings, as it has been associated with fungal infection susceptibility, but concrete roles as a biomarker or drug target are not established[5].

Other names

Fibrinogen C domain-containing protein 1FIBCD1UNQ701/PRO1346FLJ14810