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Nectin1

Domain

The Ig-like V-type domain is involved in homophilic interaction in cis, a prerequisite for cell adhesion (By similarity). Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR (PubMed:22955284).

Function

Cell adhesion molecule that promotes cell-cell contacts and plays important roles in the development of the nervous system (PubMed:11827984, PubMed:15328010, PubMed:18703497, PubMed:21798896, PubMed:22955284). Acts by forming homophilic or heterophilic trans-dimers (PubMed:11827984). Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4 (PubMed:11827984, PubMed:21798896). Involved in axon guidance by promoting contacts between the commissural axons and the floor plate cells (PubMed:15328010). Involved in synaptogegesis (PubMed:11827984). Has some neurite outgrowth-promoting activity (PubMed:22955284). Promotes formation of checkerboard-like cellular pattern of hair cells and supporting cells in the auditory epithelium via heterophilic interaction with NECTIN3: NECTIN1 is present in the membrane of hair cells and associates with NECTIN3 on supporting cells, thereby mediating heterotypic adhesion between these two cell types (PubMed:21798896). Required for enamel mineralization (PubMed:18703497).

(Microbial infection) Acts as a receptor for pseudorabies virus/PRV.

Sequence Similarities

Belongs to the nectin family.

Cellular localization

Alternative names

CD111, Hvec, Prr1, Pvrl1, Nectin1, Nectin-1, Herpes virus entry mediator C, Nectin cell adhesion molecule 1, Poliovirus receptor-related protein 1, Herpesvirus entry mediator C, HveC

swissprot:Q9JKF6 entrezGene:58235