PVRL1

Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1, is a human is_associated_with::gene that encodes a protein of is_associated_with::immunoglobulin superfamily (IgSF) also considered a member of the is_associated_with::nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent is_associated_with::cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).

Function
PVRL1 is adhesion molecule found in a wide range of tissues where is localizes in various junctions such as the is_associated_with::adherens junction of is_associated_with::epithelial tissue or the is_associated_with::chemical synapse of is_associated_with::neurons. The cytoplasmic tail of PVRL1 can bind the protein afadin which is a scaffolding protein that binds is_associated_with::actin.

In the chemical synapse PVRL1 interacts with is_associated_with::PVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. Inerestingly the two proteins have been found to localize asymmetrically along the chemical synapse, with PVRL1 primarily on the is_associated_with::axonal side and PVRL3 on the dendritic side.

The protein has been revealed as one of the key playerse in mediating cellular entry of the is_associated_with::Herpes simplex virus by interacting with the viral glycoprotein D (gD).

Interactions
PVRL1 has been shown to interact with is_associated_with::MLLT4.