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poliovirus receptor; nectin-like protein 5; necl-5; CD155 (PVR, PVS)
Function:
- mediates NK cell adhesion & triggers NK cell effector functions
- binds 2 different NK cell receptors: CD96 & CD226
- these interactions
a) accumulate at the cell-cell contact site, leading to formation of a mature immunological synapse between NK cell & target cell
b) may trigger adhesion & secretion of lytic granules & IFN-gamma & activate cytoxicity of activated NK cells
c) may also promote NK cell-target cell modular exchange, & PVR transfer to the NK cell
- can form trans-heterodimers with PVRL3/nectin-3.
- extracellular domain interacts with VTN, CD226 & CD96
- cytoplasmic domain interacts with DYNLT1
- interacts with HHV-5 UL141
Kinetic parameters:
- KM=72 nM for VTN
Structure:
- belongs to the nectin family
- contains 2 Ig-like C2-type domains (immunoglobulin-like)
- contains 1 Ig-like V-type domain (immunoglobulin-like); V-type domain is necessary & sufficient for virus binding & uptake
Compartment:
- isoforms alpha, delta: cell membrane
- isoforms beta, gamma: secreted
Alternative splicing: named isoforms=4
Expression:
- transcriptionally regulated by SHH
Miscellaneous: The V-type domain is necessary & sufficient for virus binding & uptake
Pathology:
- role in mediating tumor cell invasion & migration
- PVR transfer to the NK cell may be important in tumor cells expressing a lot of PVR, & may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion
- receptor for poliovirus attachment to target cells
- 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
- interacts with poliovirus capsid composed of VP1, VP2 & VP3, mainly through VP3
Related
polio virus
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
cell surface receptor
glycoprotein
Properties
SIZE: entity length = 417 aa
MW = 45 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-20}
immunoglobulin superfamily domain {24-139}
MOTIF: cysteine residue {C49}
MODIFICATION: cysteine residue {C123}
N-glycosylation site {N105}
N-glycosylation site {N120}
cysteine residue {C123}
MODIFICATION: cysteine residue {C49}
immunoglobulin superfamily domain {145-237}
MOTIF: cysteine residue {C166}
MODIFICATION: cysteine residue {C221}
N-glycosylation site {N188}
N-glycosylation site {N218}
cysteine residue {C221}
MODIFICATION: cysteine residue {C166}
N-glycosylation site {N237}
immunoglobulin superfamily domain {244-328}
MOTIF: cysteine residue {C266}
MODIFICATION: cysteine residue {C312}
N-glycosylation site {N278}
N-glycosylation site {N307}
cysteine residue {C312}
MODIFICATION: cysteine residue {C266}
N-glycosylation site {N313}
transmembrane domain {344-367}
DYNLT1 binding {368-372}
N-glycosylation site {N405}
Database Correlations
OMIM 173850
UniProt P15151
PFAM correlations
Kegg hsa:5817
References
- UniProt :accession P15151
- Protein Spotlight; The accidental crippler
- Issue 75 of October 2006
http://www.expasy.org/spotlight/back_issues/sptlt075.shtml