| IED ID | IndEnz0002005894 |
| Enzyme Type ID | protease005894 |
| Protein Name |
Cathepsin K EC 3.4.22.38 Protein OC-2 |
| Gene Name | CTSK |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MWGLKVLLLPVVSFALHPEEILDTQWELWKKTYSKQYNSKVDEISRRLIWEKNLKHISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPPSRSHSNDTLYIPDWEGRTPDSIDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENYGCGGGYMTNAFQYVQRNRGIDSEDAYPYVGQDESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDENCSSDNVNHAVLAVGYGIQKGNKHWIIKNSWGESWGNKGYILMARNKNNACGIANLASFPKM |
| Enzyme Length | 329 |
| Uniprot Accession Number | P43236 |
| 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. {ECO:0000250|UniProtKB:P43235}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Disulfide bond (3); Glycosylation (2); Helix (10); Propeptide (1); Signal peptide (1) |
| Keywords | 3D-structure;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Membrane;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P43235}. Secreted {ECO:0000250|UniProtKB:P43235}. Apical cell membrane {ECO:0000250|UniProtKB:P43235}; Peripheral membrane protein {ECO:0000250|UniProtKB:P43235}; Extracellular side {ECO:0000250|UniProtKB:P43235}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000250|UniProtKB:P43235}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2F7D; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,870 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |