Detail Information for IndEnz0002018932
IED ID IndEnz0002018932
Enzyme Type ID protease018932
Protein Name Cathepsin D
EC 3.4.23.5
Gene Name ctsd
Organism Clupea harengus (Atlantic herring)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Clupei Clupeiformes (herrings and anchovies) Clupeoidei Clupeidae (herrings) Clupeinae Clupea Clupea harengus (Atlantic herring)
Enzyme Sequence MKFLYLFLFAVFAWTSDAIVRIPLKKFRSIRRTLSDSGLNVEQLLAGTNSLQHNQGFPSSNAPTPETLKNYMDAQYYGEIGLGTPVQMFTVVFDTGSSNLWLPSIHCSFTDIACLLHHKYNGAKSSTYVKNGTEFAIQYGSGSLSGYLSQDSCTIGDIVVEKQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVPPVFDMMMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVPVTRQAYWQIHMDGMSIGSQLTLCKDGCEAIVDTGTSLITGPPAEVRALQKAIGAIPLIQGEYMIDCKKVPTLPTISFNVGGKTYSLTGEQYVLKESQGGKTICLSGLMGLEIPPPAGPLWILGDVFIGQYYTVFDRESNRVGFAKST
Enzyme Length 396
Uniprot Accession Number Q9DEX3
Absorption
Active Site ACT_SITE 94; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 281; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation ACTIVITY REGULATION: Inhibited by pepstatin. {ECO:0000269|PubMed:11207447}.
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:0000269|PubMed:11207447};
DNA Binding
EC Number 3.4.23.5
Enzyme Function FUNCTION: Acid protease active in intracellular protein breakdown.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.5 with hemoglobin as substrate.;
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome.
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 43,316
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.5;