LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| 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 [, , ].This entry represents the second Ig domain of nectin-3 and 4. 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-1 interactions play a critical role in selective axo-dendritic adhesion []. Nectin-4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions []. It acts as a receptor for measles virus [, , ]. Nectin 4 plays a significant role in cancer cell growth and invasion [, ]. |
| Short Name | IgC1_2_Nectin-3-4-like |
