Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases.
A cDNA for rat cathepsin H was isolated and sequenced. The deduced protein comprising 333 amino acid residues is composed of a typical signal sequence (21 residues), a pro-peptide region (92 residues) and a mature enzyme region (220 residues). The amino acid sequence in the pro-peptide region, in particular, residues Phe-(-41) to Ser-(-29) of cathepsin H, is highly homologous to the pro-peptide regions of other cysteine proteinases. This homologous region may play a role in the processing of cysteine proteinases.
Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
K
K
Ishidoh
S
S
Imajoh
Y
Y
Emori
S
S
Ohno
H
H
Kawasaki
Y
Y
Minami
E
E
Kominami
N
N
Katunuma
K
K
Suzuki
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D056655:Cathepsin H; D002403:Cathepsins / Q000235:genetics*; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics*; D004247:DNA / Q000378:metabolism*; D004792:Enzyme Precursors / Q000235:genetics; D008969:Molecular Sequence Data; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D004792:Enzyme Precursors; D004247:DNA; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056655:Cathepsin H; C534128:Ctsh protein, rat