Abstract
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.
Copyright 1999 Academic Press.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Blotting, Northern
-
Cathepsin F
-
Cathepsins / chemistry
-
Cathepsins / genetics*
-
Cloning, Molecular
-
Cystatins / chemistry*
-
Cystatins / genetics
-
Cysteine Proteinase Inhibitors / chemistry
-
Cysteine Proteinase Inhibitors / genetics
-
Databases, Factual
-
Enzyme Precursors / chemistry*
-
Enzyme Precursors / genetics
-
Expressed Sequence Tags
-
Glycosylation
-
Humans
-
Models, Molecular
-
Molecular Sequence Data
-
Papain / chemistry
-
Papain / genetics
-
Protein Folding
-
Protein Sorting Signals / genetics
-
Protein Structure, Secondary
-
RNA, Messenger / metabolism
-
Sequence Alignment
Substances
-
Cystatins
-
Cysteine Proteinase Inhibitors
-
Enzyme Precursors
-
Protein Sorting Signals
-
RNA, Messenger
-
Cathepsins
-
Papain
-
CTSF protein, human
-
Cathepsin F