| IED ID | IndEnz0002005880 |
| Enzyme Type ID | protease005880 |
| Protein Name |
Cathepsin E EC 3.4.23.34 |
| Gene Name | Ctse |
| 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 | MKPLFVLLLLLLLLDLAQAQGVLHRVPLRRHQSLRKKLRAQGQLSDFWRSHNLDMIEFSESCNVDKGINEPLINYLDMEYFGTVSIGSPSQNFTVIFDTGSSNLWVPSVYCTSPACKAHPVFHPSQSSTYMEVGNHFSIQYGTGSLTGIIGADQVSVEGLTVEGQQFGESVKEPGQTFVNAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVALPMFSVYLSSDPQGGSGSELTFGGYDPSHFSGSLNWIPVTKQGYWQIALDGIQVGDTVMFCSEGCQAIVDTGTSLITGPPKKIKQLQEAIGATPMDGEYAVDCATLNMMPNVTFLINGVSYTLSPTAYILPDLVDGMQFCGSGFQGLDIQPPAGPLWILGDVFIRKFYSVFDRGNNQVGLAPAVP |
| Enzyme Length | 398 |
| Uniprot Accession Number | P16228 |
| Absorption | |
| Active Site | ACT_SITE 98; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 283; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Similar to cathepsin D, but slightly broader specificity.; EC=3.4.23.34; Evidence={ECO:0000269|PubMed:8157122}; |
| DNA Binding | |
| EC Number | 3.4.23.34 |
| Enzyme Function | FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Natural variant (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Alternative splicing;Aspartyl protease;Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Endosome;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:8491674, ECO:0000269|PubMed:9572291}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In brain microglia, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In stomach and spleen, the mature enzyme contains a high mannose-type oligosaccharide. In erythrocyte membranes, the mature enzyme contains a complex-type oligosaccharide. {ECO:0000269|PubMed:2105725, ECO:0000269|PubMed:8346912, ECO:0000269|PubMed:9572291}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16367762; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,021 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.34; |