Detail Information for IndEnz0002018952
IED ID IndEnz0002018952
Enzyme Type ID protease018952
Protein Name Cathepsin K
EC 3.4.22.38
Cathepsin O
Cathepsin O2
Cathepsin X
Gene Name CTSK CTSO CTSO2
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM
Enzyme Length 329
Uniprot Accession Number P43235
Absorption
Active Site ACT_SITE 139; /evidence=ECO:0000250; ACT_SITE 276; /evidence=ECO:0000250; ACT_SITE 296; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.; EC=3.4.22.38;
DNA Binding
EC Number 3.4.22.38
Enzyme Function FUNCTION: Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:11082042). {ECO:0000269|PubMed:11082042}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (13); Chain (1); Disulfide bond (3); Glycosylation (1); Helix (14); Natural variant (6); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Cell membrane;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Membrane;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11082042}. Secreted {ECO:0000269|PubMed:11082042}. Apical cell membrane {ECO:0000269|PubMed:11082042}; Peripheral membrane protein {ECO:0000269|PubMed:11082042}; Extracellular side {ECO:0000269|PubMed:11082042}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000269|PubMed:11082042}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000255
Structure 3D X-ray crystallography (64)
Cross Reference PDB 1ATK; 1AU0; 1AU2; 1AU3; 1AU4; 1AYU; 1AYV; 1AYW; 1BGO; 1BY8; 1MEM; 1NL6; 1NLJ; 1Q6K; 1SNK; 1TU6; 1U9V; 1U9W; 1U9X; 1VSN; 1YK7; 1YK8; 1YT7; 2ATO; 2AUX; 2AUZ; 2BDL; 2R6N; 3C9E; 3H7D; 3KW9; 3KWB; 3KWZ; 3KX1; 3O0U; 3O1G; 3OVZ; 4DMX; 4DMY; 4N79; 4N8W; 4X6H; 4X6I; 4X6J; 4YV8; 4YVA; 5J94; 5JA7; 5JH3; 5TDI; 5TUN; 5Z5O; 6ASH; 6HGY; 6PXF; 6QBS; 6QL8; 6QLM; 6QLW; 6QLX; 6QM0; 7NXL; 7NXM; 7PCK;
Mapped Pubmed ID 10072072; 10229672; 10631941; 10719280; 10748235; 10809954; 11119712; 11311061; 11684289; 11733367; 11813165; 11853874; 12039963; 12078484; 12081494; 12125807; 12492488; 12504904; 12568399; 12652657; 12742663; 12748383; 12887056; 14645229; 14684342; 14753734; 15161653; 15177446; 15304486; 15341947; 15537340; 15737607; 15780613; 15797245; 15826870; 15837295; 15878337; 15896958; 15929988; 15950618; 15982880; 16169070; 16181339; 16290936; 16337236; 16354158; 16376075; 16413777; 16774752; 16831915; 16912123; 16946716; 17227755; 17230547; 17338641; 17683065; 17728092; 17882010; 17889653; 17911019; 17991740; 18053985; 18163891; 18166152; 18368130; 18511517; 18664495; 18664521; 18692071; 18765527; 18820679; 18931679; 18949742; 18979635; 19060845; 19194656; 19338743; 19371798; 19396149; 19428782; 19433310; 19446361; 19453261; 19469903; 19674475; 19700761; 19750481; 19800993; 19913121; 20149657; 20153187; 20305575; 20430722; 20450492; 20494937; 20628086; 20628624; 20711500; 20727023; 20837372; 20843687; 21030256; 21086906; 21099701; 21193413; 21402738; 21602817; 21715684; 21756348; 21784848; 21874011; 21880134; 22562303; 22569264; 22569910; 22614014; 22730330; 22742641; 22974233; 23152410; 23326535; 23355199; 23369704; 23529168; 23689398; 23871919; 23951042; 24088021; 24134756; 24269275; 24342995; 24518821; 24583396; 24696729; 24719048; 24767306; 24835450; 24954318; 24958728; 25184245; 25279554; 25304337; 25356585; 25422423; 25558848; 25626674; 25725806; 25809793; 26219353; 26241216; 26280490; 26302400; 26458004; 26988144; 27498895; 27558267; 27709599; 27859061; 28040478; 28049758; 28085175; 28087412; 28117540; 28216213; 28623674; 28766739; 28887075; 29029096; 29088253; 29618339; 29796728; 29859187; 30046941; 30072716; 30199612; 30450725; 30628449; 30689386; 30931961; 32007579; 32117071; 32368981; 32819572; 33227497; 33429075; 33445732; 33764165; 33945887; 34103584; 34183355; 34473502; 34755658; 34831087; 7896811; 8576151; 8687433; 9033588; 9539769; 9545226; 9733481;
Motif
Gene Encoded By
Mass 36,966
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.38;