ID:CATE_HUMAN DESCRIPTION: RecName: Full=Cathepsin E; EC=3.4.23.34; Contains: RecName: Full=Cathepsin E form I; Contains: RecName: Full=Cathepsin E form II; Flags: Precursor; 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. CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader specificity. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for hemoglobin; KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu; KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu; SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Endosome. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B- lymphocytes. 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. PTM: Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57. SIMILARITY: Belongs to the peptidase A1 family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P14091
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006508 proteolysis GO:0016540 protein autoprocessing GO:0019886 antigen processing and presentation of exogenous peptide antigen via MHC class II GO:0030163 protein catabolic process