Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.
We have determined the complete sequence of the cDNA clone representing the full size human skin collagenase mRNA. Collagenase is synthesized in preproenzyme form, Mr 54,092, with a 19 amino acid long signal peptide. The primary secretion products of the enzyme consist of a minor glycosylated form, Mr 57,000, and a major unmodified polypeptide of predicted Mr 51,929. Proteolytic activation of human skin procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme. Both potential N-glycosylation sites are contained within the proteolytically activated form of the enzyme. The primary structure of the coding region of the presented clone is homologous to an oncogene-induced rat protein whose function is still unknown, although preliminary observations suggest that it is not rat skin collagenase.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D017364:Collagenases; D004247:DNA / Q000032:analysis; D004792:Enzyme Precursors / Q000032:analysis / Q000235:genetics; D004815:Epidermal Growth Factor / Q000494:pharmacology; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D003012:Microbial Collagenase / Q000032:analysis / Q000235:genetics*; D009363:Neoplasm Proteins / Q000032:analysis / Q000235:genetics*; D009857:Oncogenes; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D012867:Skin / Q000201:enzymology*
D004792:Enzyme Precursors; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D004815:Epidermal Growth Factor; D004247:DNA; D017364:Collagenases; C022440:procollagenase; D003012:Microbial Collagenase