| IED ID | IndEnz0002018930 |
| Enzyme Type ID | protease018930 |
| Protein Name |
Cathepsin D EC 3.4.23.5 Cleaved into: Cathepsin D 12 kDa light chain; Cathepsin D 9 kDa light chain; Cathepsin D 34 kDa heavy chain; Cathepsin D 30 kDa heavy chain |
| Gene Name | Ctsd |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MQTPGVLLLILGLLDASSSALIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPRTKEPVSELLKNYLDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDLGGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFAKAATL |
| Enzyme Length | 407 |
| Uniprot Accession Number | P24268 |
| Absorption | |
| Active Site | ACT_SITE 97; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 290; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5; |
| DNA Binding | |
| EC Number | 3.4.23.5 |
| Enzyme Function | FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (25); Chain (5); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (10); Propeptide (1); Sequence conflict (4); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5UX4; |
| Mapped Pubmed ID | 11687729; 12666874; 16396496; 17665967; 30108829; 8702598; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,681 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.5; |