| IED ID | IndEnz0002018931 |
| Enzyme Type ID | protease018931 |
| Protein Name |
Cathepsin D EC 3.4.23.5 |
| Gene Name | ctsd |
| Organism | Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Neoteleostei Eurypterygia Ctenosquamata Acanthomorphata Euacanthomorphacea Percomorphaceae Eupercaria Perciformes (perches and others) Notothenioidei Channichthyidae (crocodile icefishes) Chionodraco Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus) |
| Enzyme Sequence | MKMLLLCVFSALALTNDALVRIPLKKFRSIRRQLTDSGKRAEELLADHHSLKYNLSFPASNAPTPETLKNYLDAQYYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMCLSGFMGLDIPAPAGPLWILGDVFMGQYYTVFDRDANRVGFAKAK |
| Enzyme Length | 396 |
| Uniprot Accession Number | O93428 |
| Absorption | |
| Active Site | ACT_SITE 94; /evidence="ECO:0000250|UniProtKB:P07339, ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 281; /evidence="ECO:0000250|UniProtKB:P07339, ECO:0000255|PROSITE-ProRule:PRU10094" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin. {ECO:0000269|PubMed:10209280}. |
| 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; Evidence={ECO:0000305}; |
| DNA Binding | |
| EC Number | 3.4.23.5 |
| Enzyme Function | FUNCTION: Acid protease active in intracellular protein breakdown. {ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Enzyme activity is maintained up to 45 degrees Celsius. Active at 50 degrees Celsius but with reduced catalytic activity. {ECO:0000269|PubMed:10209280}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0. {ECO:0000269|PubMed:10209280}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Glycosylation (2); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q9DEX3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,958 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |