| IED ID | IndEnz0002005887 |
| Enzyme Type ID | protease005887 |
| Protein Name |
Cathepsin F CATSF EC 3.4.22.41 |
| Gene Name | CTSF |
| 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 | MAPWLQLLSLLGLLPGAVAAPAQPRAASFQAWGPPSPELLAPTRFALEMFNRGRAAGTRAVLGLVRGRVRRAGQGSLYSLEATLEEPPCNDPMVCRLPVSKKTLLCSFQVLDELGRHVLLRKDCGPVDTKVPGAGEPKSAFTQGSAMISSLSQNHPDNRNETFSSVISLLNEDPLSQDLPVKMASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEFRTIYLNTLLRKEPGNKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD |
| Enzyme Length | 484 |
| Uniprot Accession Number | Q9UBX1 |
| Absorption | |
| Active Site | ACT_SITE 295; /evidence=ECO:0000269|PubMed:12225749; ACT_SITE 431; /evidence=ECO:0000269|PubMed:12225749; ACT_SITE 451; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L.; EC=3.4.22.41; |
| DNA Binding | |
| EC Number | 3.4.22.41 |
| Enzyme Function | FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Disulfide bond (3); Glycosylation (5); Helix (9); Natural variant (5); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Neurodegeneration;Neuronal ceroid lipofuscinosis;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1M6D; |
| Mapped Pubmed ID | 10072072; 10631941; 10748235; 10809954; 11684289; 11813165; 11853874; 12078484; 12742663; 12748383; 15184381; 15989693; 16181339; 16963053; 19913121; 20628086; 24255036; 25576872; 27524508; 28474574; 30561534; 33236952; 8687433; 9539769; 9545226; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,366 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.41; |