Detail Information for IndEnz0002005871
IED ID IndEnz0002005871
Enzyme Type ID protease005871
Protein Name Cathepsin D
EC 3.4.23.5

Cleaved into: Cathepsin D light chain; Cathepsin D heavy chain
Gene Name CTSD
Organism Sus scrofa (Pig)
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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSGKSSTYVKNGTTFAIHYGSGSLSGYLSSQDTVSVPCNSALSGVGGIKVERQTFGEATKQPGLTFIAAKFDGILGMAYPRISVNNVVPVFDNLMQQKLVDKDIFSFYLNRDPGAQPGGELMLGGIDSKYYKGSLDYHNVTRKAYWQIHMNQVAVGSSLTLCKGGCEAIVDTGTSLIVGQPEEVRELGKAIGAVPLIQGEYMIPCEKVPSLPDVTVTLGGKKYKLSSENYTLKVSQAGQTICLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDLNRVGLAEAA
Enzyme Length 345
Uniprot Accession Number P00795
Absorption
Active Site ACT_SITE 33; ACT_SITE 230
Activity Regulation
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;
DNA Binding
EC Number 3.4.23.5
Enzyme Function FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (2); Disulfide bond (3); Domain (1); Glycosylation (2); Natural variant (2); Propeptide (1); Sequence conflict (2)
Keywords Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 37,295
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda