NECTIN4

NECTIN4 is a member of the nectin family. The encoded protein contains two immunoglobulin-like (Ig-like) C2-type domains and one Ig-like V-type domain. It is involved in cell adhesion through trans-homophilic and-heterophilic interactions. It is a single-pass type I membrane protein. The soluble form is produced by proteolytic cleavage at the cell surface by the metalloproteinase ADAM17/TACE. The secreted form is found in both breast tumor cell lines and breast tumor patients. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder. Alternatively spliced transcript variants have been found but the full-length nature of the variant has not been determined.

Full Name

Nectin Cell Adhesion Molecule 4

Function

Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells.

(Microbial infection) Acts as a receptor for measles virus.

Biological Process

Heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: GO_Central
Homophilic cell adhesion via plasma membrane adhesion molecules Source: GO_Central

Cellular Location

Plasma membrane
Cell membrane
Other locations
adherens junction
Note: Colocalizes with AFDN at cadherin-based adherens junctions (PubMed:11544254).
Processed poliovirus receptor-related protein 4:
Secreted 1 Publication
Note: The secreted form is found in breast tumor patients (PubMed:15784625).

Involvement in disease

Ectodermal dysplasia-syndactyly syndrome 1 (EDSS1):
A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSS1 is characterized by the association of hair and teeth abnormalities with cutaneous syndactyly of the hands and/or feet. Hair morphologic abnormalities include twists at irregular intervals (pilli torti) and swelling along the shafts, particularly associated with areas of breakage. Dental findings consist of abnormally widely spaced teeth, with peg-shaped and conical crowns. Patients have normal sweating.

Topology

Extracellular: 32-349
Helical: 350-370
Cytoplasmic: 371-510

PTM

The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17/TACE.