Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment

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The human elafin gene was cloned and its entire nucleotide sequence was determined to deduce the amino acid sequence for the precursor of elafin, an elastase-specific inhibitor. The gene spans approximately 1.7 kb and is divided into 3 exons. The gene product preproelafin consists of 117 amino acids: the initiator Met, a putative 25-amino acid signal peptide, a pro-sequence of about 34 amino acids, and the C-terminal 57 amino acids for mature elafin. Possible covalent clotting of the prosegment and its physiological significance have been pointed out based on a remarkable sequence similarity between the pro-sequence and the guinea pig seminal clotting protein SVP-1.