Detail Information for IndEnz0002018934
IED ID IndEnz0002018934
Enzyme Type ID protease018934
Protein Name Cathepsin D
EC 3.4.23.5
Fragment
Gene Name CTSD
Organism Ovis aries (Sheep)
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 Ruminantia Pecora Bovidae Caprinae Ovis Ovis aries (Sheep)
Enzyme Sequence LHKFTSNRRTMSEAMGPVEHLIAKGPISKYATREPAVRQGPIPELLTNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMRQKLVDKNVFSFFLNRDPKAQPGEELMLGGTDSKYYRGSLTYHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLMVGPVDEVRELHKAIGAVPLIQGEYMIPCEKVSSLPQVTLKLGGKDYTLSPEDYTLKVSQAGTTVCLSGFMGMDIPPPGGPLWILGDVFIGR
Enzyme Length 365
Uniprot Accession Number Q9MZS8
Absorption
Active Site ACT_SITE 72; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 268; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
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 (1); Disulfide bond (4); Domain (1); Glycosylation (2); Natural variant (1); Non-terminal residue (2); Propeptide (1)
Keywords Aspartyl protease;Disease variant;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 39,815
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda