| IED ID | IndEnz0002007665 |
| Enzyme Type ID | protease007665 |
| Protein Name |
Cathepsin L-like EC 3.4.22.15 |
| Gene Name | cpl-1 T03E6.7 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MNRFILLALVAAVVAVNSAKLSRQIESAIEKWDDYKEDFDKEYSESEEQTYMEAFVKNMIHIENHNRDHRLGRKTFEMGLNHIADLPFSQYRKLNGYRRLFGDSRIKNSSSFLAPFNVQVPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKYGNHGCNGGLMDQAFEYIRDNHGVDTEESYPYKGRDMKCHFNKKTVGADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHRSFQLYKKGVYYDEECSSEELDHGVLLVGYGTDPEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHCGVATKASYPLV |
| Enzyme Length | 337 |
| Uniprot Accession Number | O45734 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 283; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 304; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000250|UniProtKB:P06797}; |
| DNA Binding | |
| EC Number | 3.4.22.15 |
| Enzyme Function | FUNCTION: Cysteine protease which plays an essential role in the degradation of proteins in lysosomes (PubMed:15456850, PubMed:24829385). During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome-like structure where a slow and controlled degradation of yolk proteins occurs (PubMed:15456850, PubMed:24829385). In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes (PubMed:24829385). In embryos, required for the degradation of endocytic and autophagic cargos (PubMed:24829385). In embryos, may play a role in the degradation of lipid-containing droplets (PubMed:26773047). Required for larval development (PubMed:11707440, PubMed:15456850). {ECO:0000269|PubMed:11707440, ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:24829385, ECO:0000269|PubMed:26773047}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (1); Mutagenesis (7); Propeptide (1); Signal peptide (1) |
| Keywords | Alternative splicing;Cytoplasmic vesicle;Disulfide bond;Endosome;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | Q9U9Y8 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11707440, ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Lysosome {ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:24829385}. Endosome {ECO:0000269|PubMed:22768338}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:24829385}. Note=The zymogen form localizes to yolk platelets/granules in the developing oocyte and in the pseudocoelom (PubMed:15456850, PubMed:16857685). Following cell corpse phagocytosis, recruited to phagosomes during the late stages of phagolysosome formation (PubMed:24829385). {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24829385}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 11381264; 11559592; 11778048; 12097347; 12529635; 12679813; 14551910; 14704431; 15338614; 15791247; 16854972; 17164286; 17267812; 17486083; 17850180; 17889653; 18692475; 19343510; 20182512; 20439774; 20439776; 21085631; 21110867; 21177967; 21367940; 22267497; 22286215; 22347378; 22560298; 22562797; 23800452; 24884423; 25487147; 26780296; 26904949; 26912668; 27457958; 30078731; 30642431; 31216475; 31283754; 31771567; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,117 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |