Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen.
A novel human cDNA encoding a cysteine protease of the papain family named cathepsin F is reported. The mature part of the predicted protease precursor displays between 26% and 42% identity to other human cysteine proteases while the proregion is unique by means of length and sequence. The very long proregion of the cathepsin F precursor (251 amino acid residues) can be divided into three regions: a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50 residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. Cathepsin F would therefore be the first cysteine protease zymogen containing a cystatin-like domain.
Nägler
D K
DK
Biotechnology Research Institute, National Research Council of Canada, 6100 Avenue Royalmount, Montréal, Québec, H4P 2R2, Canada.
Sulea
T
T
Ménard
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D056646:Cathepsin F; D002403:Cathepsins / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D015891:Cystatins / Q000737:chemistry* / Q000235:genetics; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics; D016208:Databases, Factual; D004792:Enzyme Precursors / Q000737:chemistry* / Q000235:genetics; D020224:Expressed Sequence Tags; D006031:Glycosylation; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry / Q000235:genetics; D017510:Protein Folding; D021382:Protein Sorting Signals / Q000235:genetics; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000378:metabolism; D016415:Sequence Alignment
D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D004792:Enzyme Precursors; D021382:Protein Sorting Signals; D012333:RNA, Messenger; D002403:Cathepsins; D010206:Papain; C534090:CTSF protein, human; D056646:Cathepsin F