We have isolated nectin3/PRR3, the fourth human member of the nectin/PRR fa
mily, also described as the alpha herpes virus receptor family. Nectin/PRR
members are adhesion molecules expressed at intercellular junctions. Nectin
3/PRR3 is a transmembrane protein, whose extracellular region contains thre
e Ig-like domains (V, C and C) and shares approximately 30% identity with t
he other members. It is mainly expressed in testis and placental tissues. S
DS-PAGE analyses demonstrate that nectin3/PRR3 has a molecular weight of 83
kDa. Nectin1/PRR1L and nectin2/PRR2S and L were found to be specifically e
xpressed at the intercellular junctions. This localization is in part due t
o the interaction of the C-terminal part of these receptors (ended by the c
onsensus sequence A/EXYV) and the PDZ domain of afadin. In this report we d
emonstrate that the nectin3/PRR3 receptor carries the A/EXYV consensus sequ
ence and interacts in vivo with both long and short isoforms of afadin. The
se results suggest that the human nectin3/PRR3 is a new afadin-associated m
olecule. (C) 2000 Elsevier Science B.V. All rights reserved.