| IED ID | IndEnz0002018914 |
| Enzyme Type ID | protease018914 |
| Protein Name |
Cathepsin B EC 3.4.22.1 BCSB Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain |
| Gene Name | CTSB |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MWRLLATLSCLLVLTSARSSLYFPPLSDELVNFVNKQNTTWKAGHNFYNVDLSYVKKLCGAILGGPKLPQRDAFAADVVLPESFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHSNGRVNVEVSAEDMLTCCGGECGDGCNGGFPSGAWNFWTKKGLVSGGLYNSHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKTCEPGYSPSYKEDKHFGCSSYSVANNEKEIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVSGEIMGGHAIRILGWGVENGTPYWLVGNSWNTDWGDNGFFKILRGQDHCGIESEIVAGMPCTHQY |
| Enzyme Length | 335 |
| Uniprot Accession Number | P07688 |
| Absorption | |
| Active Site | ACT_SITE 108; /evidence="ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:10739956, ECO:0000269|PubMed:7106283"; ACT_SITE 278; /evidence="ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:10739956"; ACT_SITE 298; /evidence="ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:10739956" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.; EC=3.4.22.1; Evidence={ECO:0000269|PubMed:1856234}; |
| DNA Binding | |
| EC Number | 3.4.22.1 |
| Enzyme Function | FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:1856234). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis (By similarity). {ECO:0000250|UniProtKB:P07858, ECO:0000250|UniProtKB:P10605, ECO:0000269|PubMed:1856234}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (11); Chain (3); Disulfide bond (7); Glycosylation (1); Helix (11); Modified residue (1); Propeptide (2); Sequence conflict (4); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Acetylation;Cell membrane;Direct protein sequencing;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:1856234}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000250|UniProtKB:P10605}. |
| Modified Residue | MOD_RES 220; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P10605 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 1ITO; 1QDQ; 1SP4; 2DC6; 2DC7; 2DC8; 2DC9; 2DCA; 2DCB; 2DCC; 2DCD; |
| Mapped Pubmed ID | 12044902; 15084146; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,661 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.1; |