A new opioid receptor-like (ZFOR2) has been cloned and characterized in an
anamniote vertebrate, the teleost zebrafish (Danio rerio). ZFOR2 encodes a
384-amino-acid protein with seven potential transmembrane domains, and its
predicted amino acid sequence presents an overall 74% degree of identity to
mammalian mu opioid receptors, Its inclusion in a dendrogram generated fro
m the alignment of the opioid receptor's protein sequences, confirms its cl
assification as a mu opioid receptor. Divergences in sequence are greater i
n the regions corresponding to extracellular loops, suggesting possible dif
ferences in ligand selectivity with respect to the classical mu opioid rece
ptors. The genomic structure of ZFOR2 is also highly conserved throughout t
he phylogenetic scale, supporting the origin of opioid receptors early in e
volution. Nevertheless, ZFOR2 lacks the fourth exon found in human and rode
nt mu opioid receptors, that is known to be involved in desensibilization a
nd internalization processes. (C) 2000 Elsevier Science B.V. All rights res
erved.