
-   Size: 412 amino acids
-   Molecular mass: 44552 Da
-   Protein Accession: P07339
-   Blocks: Pepsin (A1) aspartic protease family signature
-   Domains: Aspartic_peptidase_A1, Aspartic_peptidase_AS, Aspartic_peptidase_N, Cathepsin_D, PEPTIDASE_A1, Peptidase_aspartic_dom_sf
-   Family: Belongs to the peptidase A1 family
-   Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease [PubMed:2733303]
-   The combined substitution of two noncontinuous sequences of cathepsin D (lysine 203 and amino acids 265-292) into the analogous positions of glycopepsinogen resulted in phosphorylation of the oligosaccharides of the expressed chimeric molecule [PMID: 2170024].
-   The lysosomal targeting region of cathepsin D includes the putative binding site of the cis-Golgi phosphotransferase which is responsible for the initial sorting step for soluble proteins destined for lysosomes by phosphorylating the carbohydrates on these molecules [PMID: 8467789].
