Vertebrate endogenous lectins have been implicated in cellular interactions that contribute to embryonic development. We have isolated a cloned segment of the gene for chick 14K type beta-galactoside-binding lectin from a genomic DNA library. Analysis of the structure of the cloned gene as well as the results of genomic Southern blot hybridization revealed that the gene is unique and that the mRNA for the lectin is encoded by four exons separated by three introns. The whole sequence spans 3.1 kilobases in the gene. The first exon encodes only two amino acid residues of the N-terminus of the mature protein and the other three exons encode, respectively, one of the three repeating sequences found in this lectin. These facts strongly support the idea that gene duplications have occurred during the evolution of this lectin. The previous study (Y. Ohyama et al. (1986) Biochem. Biophys. Res. Commun. 134, 51-56) suggested that this lectin is not synthesized as a precursor molecule with a cleavable signal sequence at its amino terminus, although it is known to be secreted into the extracellular matrix. Sequence determination of the upstream region of the mRNA indicated that the ATG located just before the codon for the N-terminal amino acid of the mature protein is the actual translation initiator. Thus it was proved that this lectin is synthesized without an N-terminal cleavable signal sequence, as suggested before.
Animals Base Sequence