Signature sequences for the galectin-4 subfamily

Galectins are a distinct family of animal lectins that have a cation-independent affinity for beta-galactoside sugars and share characteristic amino acid sequences. The cDNA encoding rabbit bladder galectin-4 has been cloned and sequenced (GenBank accession no. AF091738). The deduced 328 amino acid sequence predicts a multidomain structure consisting of an N-terminal peptide (19 residues) and two carbohydrate recognition domains (130 residues each) connected by a linker region (49 residues). Comparison of rabbit galectin-4 with related proteins reveals that two peptide motifs, M-A-F/Y-V-P-A-P-G-Y-Q-P-T-Y-N-P-T-L-P-Y in the N terminus and A-F-H-F-N-P-R-F-D-G-W-D-K-V-V-F in the first carbohydrate recognition domain are highly conserved in human, pig, rat, and mouse galectin-4 as well as in mouse galectin-6. The two peptide motifs are proposed here as the signature sequences to identify new members of the galectin-4 subfamily.