Poliovirus receptor-related 3 (PVRL3), also known as Nectin-3 and CD113, is a member of the nectin family. PVRL3/Nectin-3 is an 83 kDa, type I transmembrane glycoprotein. Its precursor is 549 amino acids (aa) in length and contains an extended signal sequence of 57 aa, an extracellular domain (ECD) of 347 aa, a transmembrane segment of 21 aa, and a cytoplasmic region of 124 aa. Nectin-3 has three splicing variants, nectin-3alpha (biggest), -3beta (middle), and -3gamma (smallest). It is predominantly expressed in testis and placenta as well as in various cell lines, including epithelial cell lines. PVRL3/Nectin-3 plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/Nectin-2 at Sertoli-spermatid junctions. PVRL3/Nectin-3 is thus involved in the formation of cell-cell junctions, including adherens junctions and synapses. It has been shown to induce endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation.
Nectin-3 is a type I transmembrane glycoprotein that belongs to the nectin family. Its precursor is 549 amino acids in length and contains an extended signal sequence of 57 amino acids, an extracellular domain (ECD) of 347 amino acids, a transmembrane segment of 21 amino acids, and a cytoplasmic region of 124 amino acids. It is predominantly expressed in testis and placenta as well as in various cell lines, including epithelial cell lines. Nectin-3 plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/Nectin-2 at Sertoli-spermatid junctions. Nectin-3 is also involved in the formation of cell-cell junctions, including adherens junctions and synapses.
Nectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and-heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.
Nectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.
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