Detail Information for IndEnz0002005964
IED ID IndEnz0002005964
Enzyme Type ID protease005964
Protein Name Cathepsin D
EC 3.4.23.5
Gene Name Ctsd
Organism Mus musculus (Mouse)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MKTPGVLLLILGLLASSSFAIIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPKTTEPVSELLKNYLDAQYYGDIGIGTPPQCFTVVFDTGSSNLWVPSIHCKILDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDQSKARGIKVEKQIFGEATKQPGIVFVAAKFDGILGMGYPHISVNNVLPVFDNLMQQKLVDKNIFSFYLNRDPEGQPGGELMLGGTDSKYYHGELSYLNVTRKAYWQVHMDQLEVGNELTLCKGGCEAIVDTGTSLLVGPVEEVKELQKAIGAVPLIQGEYMIPCEKVSSLPTVYLKLGGKNYELHPDKYILKVSQGGKTICLSGFMGMDIPPPSGPLWILGDVFIGSYYTVFDRDNNRVGFANAVVL
Enzyme Length 410
Uniprot Accession Number P18242
Absorption
Active Site ACT_SITE 97; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 293; /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); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Signal;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, ECO:0000269|PubMed:16170054}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10523518; 10591619; 10633857; 10856224; 10995834; 11567042; 11813165; 11821259; 12062453; 12117300; 12350228; 12440525; 12676526; 12676993; 12775715; 12904583; 1372572; 14651853; 14739942; 15126630; 15452145; 15518240; 15582152; 15588329; 15592854; 15665831; 15699105; 15860733; 15883644; 15958652; 15992379; 16123398; 16141072; 16177003; 16242638; 16259009; 16314482; 16423528; 16424157; 16602821; 16615898; 16920965; 16959874; 16966329; 16987511; 16997486; 17289576; 17314303; 17500053; 17548631; 17553802; 17570679; 18001291; 18091563; 18202773; 18299403; 18337546; 18498441; 18596167; 18702517; 19021916; 19026003; 19116891; 19119233; 19125694; 19176312; 19203374; 19293336; 19710420; 19799774; 19819948; 19845830; 20017393; 20489146; 20541250; 20551175; 20560835; 20592493; 21116106; 21123180; 21267068; 21311773; 21474794; 21648018; 21677750; 21862448; 21960143; 21966382; 22008266; 22053177; 22245096; 22337873; 22439866; 22718342; 22854957; 22904094; 22964611; 23069676; 23177142; 23250759; 23258225; 23279039; 23315080; 23338040; 23391753; 23516607; 23707513; 24154525; 24598201; 25054204; 25496868; 25830414; 25852735; 25915474; 26232697; 26370502; 26467158; 26682926; 26718887; 26823550; 26831567; 27573911; 27626380; 27634010; 27880732; 27997605; 28071719; 28429406; 28493053; 28502476; 28615690; 28835281; 29229780; 29719249; 30959855; 30985297; 31340140; 33046706; 33153072; 33340069; 33758261; 33800998; 34335574; 7498407; 7641679; 7788526; 9034150; 9539769; 9645704; 9916995;
Motif
Gene Encoded By
Mass 44,954
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.5;