Protein sequence and gene structure for mouse leukosialin (CD43), a T lymphocyte mucin without introns in the coding sequence.

A partial cDNA clone for mouse leukosialin was isolated by use of a rat leukosialin cDNA probe. The mouse cDNA was then used to isolate genomic clones that corresponded to the two mouse genes detected in Southern blots. One gene encoded an open reading frame for the homologue of rat leukosialin and this gene was notable for the absence of introns within the coding sequence. A lack of introns has previously been observed for the human leukosialin gene (Shelley, C. S., Remold-O'Donnell, E., Rosen, F. S. and Whitehead, A. S., Biochem. J., submitted). The other mouse gene was an intronless pseudogene for a leukosialin-related sequence. The presence of only one functional gene that lacked coding-region introns established that molecular heterogeneity in mouse leukosialin could not arise from multiple genes or alternative splicing of exons. The sequence of mouse leukosialin suggested an extracellular segment with a high content of O-linked carbohydrate, as is the case in the rat and human. In addition the mouse molecule had one possible N-linked glycosylation site. The cytoplasmic domain of 124 amino acids was highly conserved between rodent and human leukosialins for the functional genes but not for the pseudogene. This suggests an important functional role for the cytoplasmic domain.