PVR
Domain
Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Function
Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration.
(Microbial infection) Acts as a receptor for poliovirus. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport.
(Microbial infection) Acts as a receptor for Pseudorabies virus.
(Microbial infection) Is prevented to reach cell surface upon infection by Human cytomegalovirus /HHV-5, presumably to escape immune recognition of infected cell by NK cells.
Post-translational modifications
N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4.
Phosphorylated by Src kinases on tyrosine residues in the ITIM motif upon ligation. Interaction with TIGIT is required for Phosphorylation.
Sequence Similarities
Belongs to the nectin family.
Cellular localization
- Isoform Alpha
- Cell membrane
- Single-pass type I membrane protein
- Isoform Delta
- Cell membrane
- Single-pass type I membrane protein
- Isoform Beta
- Secreted
- Isoform Gamma
- Secreted
Alternative names
CD155, PVS, PVR, Poliovirus receptor, Nectin-like protein 5, NECL-5