Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases.
A new mouse cysteine protease, termed cathepsin R, has been identified. The complete nucleotide sequence of this gene was derived from a set of cDNAs generated from 15.5-day mouse placenta. Sequence analysis revealed an open reading frame encoding a 334 amino acid long polypeptide closely related to placentally expressed cathepsins P, Q, and M. RT-PCR analysis indicated that cathepsin R is only expressed in placenta and thus is a new member of the emerging family of cathepsins whose expression is regulated during mouse embryonic development. Modeling and structural analysis suggests that cathepsin R will have a restricted substrate specificity when compared to that of cathepsin L.
Sol-Church
K
K
Laboratory of Clinical Biochemistry, Department of Research, Alfred I duPont Hospital for Children, Wilmington, DE 19899, USA. ksolchur@nemours.org
Frenck
J
J
Bertenshaw
G
G
Mason
R W
RW
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics; D018076:DNA, Complementary / Q000032:analysis; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010920:Placenta / Q000201:enzymology*; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics*; D013379:Substrate Specificity
D018076:DNA, Complementary; C035145:ribosomal neutral proteinase; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases