Pathways & interactions
C-type lectin-like/link domain superfamily (IPR016186)
Short name: C-type_lectin-like/link_sf
- Link domain (IPR000538)
- CD44 antigen (IPR001231)
- C-type lectin-like (IPR001304)
- Polycystin cation channel (IPR006228)
- Chordopoxvirus A33R (IPR009238)
- Collagenase NC10/endostatin (IPR010515)
- Intimin, C-terminal (IPR013117)
- C-type lectin fold (IPR016187)
- L-selectin (IPR016348)
- Eosinophil major basic protein, C-type lectin-like domain (IPR033816)
- CEL-1-like C-type lectin-like domain (IPR033988)
- CD209-like, C-type lectin-like domain (IPR033989)
- Collectin, C-type lectin-like domain (IPR033990)
- Selectin, C-type lectin-like domain (IPR033991)
- Natural killer cell receptor-like, C-type lectin-like domain (IPR033992)
- C-type lectin-like domain, bacterial (IPR034007)
- TC14-like, C-type lectin-like domain (IPR034008)
- DGCR2-like, C-type lectin-like domain (IPR034010)
- Attractin-like, C-type lectin-like domain (IPR034011)
- Mannose-binding protein (IPR037570)
Lectins occur in plants, animals, bacteria and viruses. Initially described for their carbohydrate-binding activity [PMID: 14533786], 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 [PMID: 12223269]. 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 [PMID: 15476922].
The term 'C-type lectin domain' was introduced to distinguish a carbohydrate-recognition domain (CRD) which is present in all Ca2+-dependent lectins, but not in other types of animal lectins. However, there are proteins with modules similar in overall structure to CRDs that serve functions other than sugar binding. Therefore, a more general term C-type lectin-like domain was introduced to refer to such domains, although both terms are sometimes used interchangeably [PMID: 16336259].
This superfamily represents a structural domain found in C-type lectins, as well as in other proteins, including:
- The C-terminal domain of invasin [PMID: 10514372] and intimin [PMID: 10890451].
- Link domain, which includes the Link module of tumor necrosis factor-inducible gene 6 protein (TSG-6) [PMID: 12972412] (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) [PMID: 14992719]. The Link domain may have emerged as a result of a deletion of the long loop region from an ancestral canonical C-type lectin domain [PMID: 8690089].
- Endostatin [PMID: 9724722] and the endostatin domain of collagen alpha 1 (XV) [PMID: 10966814], these domains being decorated with many insertions in the common fold.
- G3DSA:126.96.36.199 (G3DSA:188.8.131.52)