| IED ID | IndEnz0002004465 |
| Enzyme Type ID | protease004465 |
| Protein Name |
Cathepsin E EC 3.4.23.34 Cleaved into: Cathepsin E form I; Cathepsin E form II |
| Gene Name | CTSE |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP |
| Enzyme Length | 396 |
| Uniprot Accession Number | P14091 |
| Absorption | |
| Active Site | ACT_SITE 96; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 281; /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:7789521, ECO:0000269|PubMed:8765029}; |
| 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. {ECO:0000269|PubMed:8765029}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Beta strand (24); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (1); Helix (11); Mutagenesis (1); Natural variant (2); Propeptide (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;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:7983070}. 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 fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide. {ECO:0000269|PubMed:2334440, ECO:0000269|PubMed:7983070, ECO:0000269|PubMed:8346912}.; PTM: Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:8346912 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TZS; |
| Mapped Pubmed ID | 10072072; 10631941; 10748235; 10809954; 11684289; 11813165; 11853874; 12078484; 12631277; 12742663; 12748383; 14769879; 15342244; 15699105; 15845357; 16169070; 16181339; 17888866; 17947645; 18006832; 18996084; 19172291; 1959628; 20600629; 21664991; 22068166; 22718633; 23451082; 24242330; 24464956; 25239563; 25348778; 30278264; 8687433; 9539769; 9545226; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,794 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for hemoglobin {ECO:0000269|PubMed:8346912}; KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu {ECO:0000269|PubMed:8346912}; KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu {ECO:0000269|PubMed:8346912}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.34; |