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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | 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 [ ]. Unlike cadherins, nectins are Ca2+-independent cell adhesion molecules that mediate not only homotypic but also heterotypic cell-cell adhesion []. 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 [, , ].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 [, ]. Nectin-3 and nectin-2 also interact to promote lymphocyte transendothelial migration []. Nectin-3 and nectin-1 interactions play a critical role in selective axo-dendritic adhesion [].This entry represents the first immunoglobulin variable (IgV) domain of Nectin-3. | Name | Nectin-3, immunoglobulin variable domain 1 |
| Short Name | Nectin-3_IgV_dom | Type | Domain |
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