Molecular cloning and sequencing of cDNA for rat cathepsin L.
A near full-length cDNA for rat cathepsin L was isolated. The deduced protein comprises 334 amino acid residues (Mr 37,685) containing a typical signal sequence (N-terminal 17 residues), pro-peptide (96 residues), and the sequence for mature cathepsin L (221 residues). Rat cathepsin L shows 94% amino acid identity with mouse cysteine proteinase. Amino acid sequence homologies of rat cathepsin L with rat cathepsins H and B are 45 and 25%, respectively. These facts indicate that mouse cysteine proteinase is probably mouse cathepsin L and that cathepsin L is more closely related to cathepsin H than cathepsin B.
Ishidoh
K
K
Department of Enzyme Chemistry, University of Tokushima, Japan.
Towatari
T
T
Imajoh
S
S
Kawasaki
H
H
Kominami
E
E
Katunuma
N
N
Suzuki
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D056668:Cathepsin L; D002403:Cathepsins / Q000235:genetics*; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases; D004247:DNA / Q000235:genetics; D010450:Endopeptidases; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D004247:DNA; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; C534278:Ctsl protein, mouse; C534280:Ctsl protein, rat