InterPro: IPR016186 C-type lectin-like

Lectins occur in plants, animals, bacteria and viruses. Initially described for their carbohydrate-binding activity [1], they are now recognised as a more diverse group of proteins, some of which are involved in protein-protein, protein-lipid or protein-nucleic acid interactions [2]. There are at least twelve structural families of lectins, of which C-type (Ca+-dependent) lectins is one. C-type lectins can be further divided into seven subgroups based on additional non-lectin domains and gene structure: (I) hyalectans, (II) asialoglycoprotein receptors, (III) collectins, (IV) selectins, (V) NK group transmembrane receptors, (VI) macrophage mannose receptors, and (VII) simple (single domain) lectins [3].

This entry represents a structural domain found in C-type lectins, as well as in other proteins, including:

• The C-terminal domain of invasin [4] and intimin [5].
• Link domain, which includes the Link module of TSG-6 [6] (a hyaladherin with important roles in inflammation and ovulation) and the hyaluronan binding domain of CD44 (which contains extra N-terminal beta-strand and C-terminal beta-hairpin) [7].
• Endostatin [8] and the endostatin domain of collagen alpha 1 (XV) [9], these domains being decorated with many insertions in the common fold.