Nectin-3 (IPR033319)

Short name: Nectin-3

Overlapping homologous superfamilies


Family relationships



Nectins are single-pass type I membrane glycoproteins belonging to the immunoglobulin superfamily. They are characterised by three Ig-like domains (a distal IgV domain and two IgC domains) in the ectodomain, followed by a transmembrane region and a cytoplasmic tail [PMID: 18593353]. Unlike cadherins, nectins are Ca2+-independent cell adhesion molecules that mediate not only homotypic but also heterotypic cell-cell adhesion [PMID: 25733141]. The cytoplasmic tail of nectins possesses a conserved afadin-binding motif, except for nectin-4 which binds the PDZ domain of afadin at its carboxyl terminus. Afadin connects nectins to F-actin and the actin cytoskeleton [PMID: 9334353, PMID: 10225955, PMID: 18593353].

This entry represents nectin-3 [PMID: 10744716]. Nectin-3 plays a role in cell-cell adhesion through heterophilic transinteractions with other nectins. Nectin-2 and nectin-3 are expressed in Sertoli cells and spermatids, respectively, and their transinteraction regulates the organization of the Sertoli cell-spermatid junctions that plays a critical role in spermatid development [PMID: 12121624, PMID: 16923130]. Nectin-3 and nectin-2 also interact to promote lymphocyte transendothelial migration [PMID: 24116228]. Nectin-3 and nectin-1 interactions play a critical role in selective axo-dendritic adhesion [PMID: 16801389].

GO terms

Biological Process

GO:0007155 cell adhesion
GO:0007286 spermatid development

Molecular Function

GO:0050839 cell adhesion molecule binding
GO:0042803 protein homodimerization activity

Cellular Component

GO:0005911 cell-cell junction

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.