cDNA cloning of granzyme C, a granule-associated serine protease of cytolytic T lymphocytes.
A cDNA clone corresponding to the complete amino acid sequence of a putative protease CCP2 of murine cytotoxic T lymphocytes was isolated and sequenced. The clone encodes a 248-residue long serine esterase. The deduced N-terminal amino acid sequence is identical over 40 residues to that of granzyme C, a protease of unknown function present in granules of cytotoxic lymphocytes. Analysis of the sequence of granzyme C/CCP2 reveals high homology to other granzyme proteases, i.e. granzyme A (40%) and granzyme B (67%) and to rat mast cell protease II (46%). The amino acids lining the specificity pocket are well conserved between granzyme B, C, and rat mast cell protease II, but not granzyme A, suggesting a similar general specificity of these three proteases.
Jenne
D
D
Institute of Biochemistry, University of Lausanne, Switzerland.
Rey
C
C
Masson
D
D
Stanley
K K
KK
Herz
J
J
Plaetinck
G
G
Tschopp
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003594:Cytoplasmic Granules / Q000201:enzymology*; D004247:DNA / Q000235:genetics; D053804:Granzymes; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000235:genetics*; D013602:T-Lymphocytes, Cytotoxic / Q000201:enzymology*
D004247:DNA; D053804:Granzymes; C509217:Gzmc protein, rat; D012697:Serine Endopeptidases