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poliovirus receptor-related protein 3 (nectin-3, CD113 antigen, CDw113, PVRL3, PRR3)
Function:
- role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins
- trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid junctions
- trans-interaction with PVR induces activation of CDC42 & RAC small G proteins through common signaling molecules. i.e. SRC & RAP1
- role in formation of cell-cell junctions, including adherens junctions & synapses
- induces endocytosis-mediated down-regulation of PVR from cell surface, resulting in reduction of cell movement & proliferation
- role in morphology of ciliary body
- can form trans-heterodimers with PVRL1/nectin-1, PVRL2/nectin-2, PVR, IGSF4B/Necl-1 & with IGSF4
- interacts with MLLT4/afadin
Structure:
- cis- & trans-homodimer
- belongs to the nectin family
- contains 2 Ig-like C2-type domains (immunoglobulin-like)
- contains 1 Ig-like V-type domain (immunoglobulin-like)
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- predominantly expressed in testis & placenta
- expressed in many cell lines, including epithelial cell lines
General
adhesion protein
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
Properties
SIZE: MW = 61 kD
entity length = 549 aa
COMPARTMENT: plasma membrane
MOTIF: signal sequence {1-57}
immunoglobulin superfamily domain {59-165}
MOTIF: N-glycosylation site {N73}
cysteine residue {C78}
MODIFICATION: cysteine residue {C148}
N-glycosylation site {N83}
N-glycosylation site {N125}
cysteine residue {C148}
MODIFICATION: cysteine residue {C78}
immunoglobulin superfamily domain {170-258}
MOTIF: N-glycosylation site {N186}
cysteine residue {C193}
MODIFICATION: cysteine residue {C246}
N-glycosylation site {N222}
cysteine residue {C246}
MODIFICATION: cysteine residue {C193}
immunoglobulin superfamily domain {269-354}
MOTIF: cysteine residue {C291}
MODIFICATION: cysteine residue {C338}
N-glycosylation site {N331}
cysteine residue {C338}
MODIFICATION: cysteine residue {C291}
transmembrane domain {405-425}
Database Correlations
OMIM 607147
UniProt Q9NQS3
PFAM correlations
References
UniProt :accession Q9NQS3