The catfish nonspecific cytotoxic cell receptor
protein (NCCRP-1) provides an important function in target cell recognition and activation of cytotoxicity. This report identifies and characterizes a zebrafish orthologue of the catfish
NCCRP-1. The zebrafish
NCCRP-1 cDNA contains an open reading frame that encodes a predicted
protein of 237
amino acids with a MW of 27 kDa and a pI of 5.5. Sequence similarities comparisons show that the
NCCRP-1 receptors from these two phylogenetically distant species share a high degree of identity. These results suggested that
NCCRP-1 performs a crucial function in innate immunity in teleosts. Further, a zebrafish 17-mer
peptide corresponding to the catfish
NCCRP-1 antigen-binding domain inhibited (catfish) cytotoxicity toward conventional
tumor target cells (HL-60). These data appeared to indicate that the zebrafish
NCCRP-1 protein may function as an
antigen recognition molecule and, as such, may participate in innate immunity in teleosts. A homology search of the zebrafish
NCCRP-1 protein revealed that it shares a significant level of identity with another group of
proteins belonging to an F-box subfamily. These
proteins share an F-box domain in the N terminus (not present in NCCRP-1) and an extremely conserved C-terminal region that has been termed the F-box-associated domain (FBA). The FBA is currently of unknown function. A new gene family is proposed in this work, based on similarities in the FBA sequences with the catfish and zebrafish
NCCRP-1 peptides. This new gene family includes several F-box domain-containing
proteins and a predicted C. elegans
protein.