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NECTIN4

Nectin cell adhesion molecule 4 (NECTIN4), also known as LNIR, PRR4, EDSS1, PVRL4 or nectin-4, is a type I transmembrane glycoprotein that belongs to the Nectin family of Ig superfamily proteins. Besides nectin-4, other three nectins have been identified in human: nectin-1, nectin-2 and nectin-3. All nectins share the same overall structure defined by three extracellular immunoglobulin-like domains (two immunoglobulin-like (Ig-like) C2-type domains and one Ig-like V-type domain), a single transmembrane helix and an intracellular domain. The extracellular domain of human Nectin-4 shares 90% and 92% amino acid sequence homology with the corresponding regions of mouse and rat Nectin-4, respectively.

The soluble form of nectin-4 protein is produced by proteolytic cleavage at the cell surface by the metalloproteinase ADAM17/TACE. The secreted form of this protein is found to be highly expressed in placenta and breast carcinoma. What's more, it is reported that this protein may be involved in cell adhesion through trans-homophilic and -heterophilic interactions, and any mutations of NECTIN4 may cause an ectodermal dysplasia disease, ectodermal dysplasia-syndactyly syndrome type 1 (EDSS1).

Gene ID: 81607
UniProt ID: Q96NY8