MGP Database

MGP000728

UniProt Annotations

Entry Information
Gene Namecathepsin E
Protein EntryCATE_HUMAN
UniProt IDP14091
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=3; IsoId=P14091-3; Sequence=Displayed; Name=1; IsoId=P14091-1; Sequence=VSP_009729; Name=2; IsoId=P14091-2; Sequence=VSP_009729, VSP_009730, VSP_009731;
Biophysicochemical PropertiesKinetic 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};
Catalytic ActivitySimilar to cathepsin D, but slightly broader specificity. {ECO:0000269|PubMed:7789521, ECO:0000269|PubMed:8765029}.
FunctionMay 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}.
PtmGlycosylated. 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}.
PtmTwo forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.
SimilarityBelongs to the peptidase A1 family. {ECO:0000305}.
Subcellular LocationEndosome {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.
SubunitHomodimer; disulfide-linked. {ECO:0000269|PubMed:7789521}.
Tissue SpecificityExpressed 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. {ECO:0000269|PubMed:11322887, ECO:0000269|PubMed:1370478, ECO:0000269|PubMed:8765029}.
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