Molecular cloning of a rat submandibular gland apomucin.

Overlapping cDNA clones which encode the protein core of a rat submandibular gland mucin-glycoprotein have been isolated and characterized. Sequence analysis revealed a translated region of 966 nucleotides encoding a protein of 322 amino acid residues. The translational start site begins with a putative signal sequence comprising the initial 22 N-terminal residues. The predicted secreted portion of the apomucin revealed three distinct domains: an N-terminal domain which is enriched in glutamine (14%), proline (13%), and tyrosine (10%); a central region which consisted of eleven, 39-base pair tandem repeats with the consensus sequence PTTDSTTPAPTTK; and a C-terminal domain which is enriched in threonine and serine residues (47%) which are not part of a repeat motif. The expression of apomucin transcript appears restricted to the rat submandibular and sublingual glands. Southern blot analysis of rat genomic DNAs suggested a low copy number (1, 2) for this apomucin gene and a limited polymorphism in the number of tandem repeats. Collectively, our sequence and expression data indicate that the cloned rat submandibular gland apomucin is distinct from any of the other salivary (bovine, porcine, or human) or rat apomucins reported thus far.