Detail Information for IndEnz0002018931
IED ID IndEnz0002018931
Enzyme Type ID protease018931
Protein Name Cathepsin D
EC 3.4.23.5
Gene Name ctsd
Organism Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Neoteleostei Eurypterygia Ctenosquamata Acanthomorphata Euacanthomorphacea Percomorphaceae Eupercaria Perciformes (perches and others) Notothenioidei Channichthyidae (crocodile icefishes) Chionodraco Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Enzyme Sequence MKMLLLCVFSALALTNDALVRIPLKKFRSIRRQLTDSGKRAEELLADHHSLKYNLSFPASNAPTPETLKNYLDAQYYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMCLSGFMGLDIPAPAGPLWILGDVFMGQYYTVFDRDANRVGFAKAK
Enzyme Length 396
Uniprot Accession Number O93428
Absorption
Active Site ACT_SITE 94; /evidence="ECO:0000250|UniProtKB:P07339, ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 281; /evidence="ECO:0000250|UniProtKB:P07339, ECO:0000255|PROSITE-ProRule:PRU10094"
Activity Regulation ACTIVITY REGULATION: Inhibited by pepstatin. {ECO:0000269|PubMed:10209280}.
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; Evidence={ECO:0000305};
DNA Binding
EC Number 3.4.23.5
Enzyme Function FUNCTION: Acid protease active in intracellular protein breakdown. {ECO:0000305}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Enzyme activity is maintained up to 45 degrees Celsius. Active at 50 degrees Celsius but with reduced catalytic activity. {ECO:0000269|PubMed:10209280};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0. {ECO:0000269|PubMed:10209280};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Glycosylation (2); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q9DEX3}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 42,958
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda