NDLI: Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

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Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

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Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	San Segundo, B. Steiner, D. F. Mccormick, M. B. Chan, S. J.
Abstract	Cathepsin B is a lysosomal thiol proteinase that may have additional extralysosomal functions. To further our investigations on the structure, mode of biosynthesis, and intracellular sorting of this enzyme, we have determined the complete coding sequences for human and mouse preprocathepsin B by using cDNA clones isolated from human hepatoma and kidney phage libraries. The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus. A comparison of procathepsin B sequences from three species (human, mouse, and rat) reveals that the homology between the propeptides is relatively conserved with a minimum of 68% sequence identity. In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59. Comparative analysis of the three sequences also suggests that processing of procathepsin B is a multistep process, during which enzymatically active intermediate forms may be generated. The availability of the cDNA clones will facilitate the identification of possible active or inactive intermediate processive forms as well as studies on the transcriptional regulation of the cathepsin B gene.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cathepsin B Genetics DNA Enzyme Precursors Amino Acid Sequence Animals Biosynthesis Chromosome Mapping Cloning, Molecular Cysteine Glycosylation Mice Sequence Homology, Nucleic Acid Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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