D
IPR001304

C-type lectin-like

InterPro entry
Short nameC-type_lectin-like
Overlapping
homologous
superfamilies
 
C-type lectin fold (IPR016187)
domain relationships

Description

A number of different families of proteins share a conserved domain which was first characterised in some animal lectins and which seem to function as a calcium-dependent carbohydrate-recognition domain
[2, 5]
. This domain, which is known as the C-type lectin domain (CTL) or as the carbohydrate-recognition domain (CRD), consists of about 110 to 130 residues. There are four cysteines which are perfectly conserved and involved in two disulphide bonds.

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 C-type lectin and C-type lectin-like are sometimes used interchangeably
[1]
.

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]
. Lectins are a diverse group of proteins, both in terms of structure and activity. Carbohydrate binding ability may have evolved independently and sporadically in numerous unrelated families, where each evolved a structure that was conserved to fulfil some other activity and function. In general, animal lectins act as recognition molecules within the immune system, their functions involving defence against pathogens, cell trafficking, immune regulation and the prevention of autoimmunity
[4]
.

This entry also includes alpha-type phospholipase A2 inhibitors (PLI-alpha), a group of proteins that have been found in a number of Viperidae snakes
[7, 6]
. Most PLI-alpha proteins are homomultimers composed of 3-5 subunits, except in Trimeresurus flavoviridis (Habu), where PLI-alpha consists of a trimer of two homologous subunits (PLI-alpha-A and PLI-alpha-B), each of which contains one C-type lectin-like domain and exhibiting significant homology to serum mannose-binding protein and lung-surfactant apoprotein
[9]
. A PLI-alpha homologue that lacks inhibitory activity was found in the non-venomous snake Elaphe quadrivirgata (Japanese four-lined ratsnake)
[8]
.

References

1.The C-type lectin-like domain superfamily. Zelensky AN, Gready JE. FEBS J. 272, 6179-217, (2005). View articlePMID: 16336259

2.Two distinct classes of carbohydrate-recognition domains in animal lectins. Drickamer K. J. Biol. Chem. 263, 9557-60, (1988). View articlePMID: 3290208

3.Divergent roles for C-type lectins expressed by cells of the innate immune system. McGreal EP, Martinez-Pomares L, Gordon S. Mol. Immunol. 41, 1109-21, (2004). View articlePMID: 15476922

4.Dual function of C-type lectin-like receptors in the immune system. Cambi A, Figdor CG. Curr. Opin. Cell Biol. 15, 539-46, (2003). View articlePMID: 14519388

5.Evolution of Ca(2+)-dependent animal lectins. Drickamer K. Prog. Nucleic Acid Res. Mol. Biol. 45, 207-32, (1993). PMID: 8341801

6.Alpha-type phospholipase A<sub>2</sub> inhibitors from snake blood. Santos-Filho NA, Santos CT. J Venom Anim Toxins Incl Trop Dis 23, 19, (2017). PMID: 28344595

7.Mapping the region of the alpha-type phospholipase A2 inhibitor responsible for its inhibitory activity. Okumura K, Ohno A, Nishida M, Hayashi K, Ikeda K, Inoue S. J. Biol. Chem. 280, 37651-9, (2005). View articlePMID: 16150695

8.Identification and characterization of a serum protein homologous to alpha-type phospholipase A2 inhibitor (PLIalpha) from a nonvenomous snake, Elaphe quadrivirgata. Okumura K, Inoue S, Ikeda K, Hayashi K. IUBMB Life 55, 539-45, (2003). View articlePMID: 14658760

9.Subunit structure and inhibition specificity of alpha-type phospholipase A2 inhibitor from Protobothrops flavoviridis. Shimada A, Ohkura N, Hayashi K, Samejima Y, Omori-Satoh T, Inoue S, Ikeda K. Toxicon 51, 787-96, (2008). View articlePMID: 18243268

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.