| IED ID | IndEnz0002014130 |
| Enzyme Type ID | protease014130 |
| Protein Name |
Endoprotease aex-5 EC 3.4.21.- Subtilisin-like protease |
| Gene Name | aex-5 kpc-3 F32A7.6 |
| 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 | MKLIFLLLLFGVSPIVCQDFEDGVFLAKITSIDEHDARKIGRRFGFEAQWKLQSYTDVYVGRRLRRRKRGIEDEIVAEMMLSQQVQFIEKLQGFRRYKRAPMTNKGYPVHVWNLTPSLYIREAWEDGFNASRVTVAVVDDGVDIKHVDLKSAFSPRVSFDFVRFGDLPTPKNSKEFEHGTQCAGLVAMEGQQCGLGVGHGATLGAIKLLGQDFLNDALEGDALAFQKDLIDIYSVSWGPKDDGKSAEKPAKFTEEAIKNGALHGRNGKGNIFVWASGNGGVNGDNCAYDGYVSNEYTLSFGVIDASGAPAAYGEGCSSVLAAVSGGDAMIQTTGLESTCSSISGSSASAAIASGIISLVLDANPTLSQRDIQHLIARTSNASAIRDVELYENSAGLNFHPKVGFGLLNAQKLVVMAATWENVAPQVTCEKMNLANGIIDNSDCDVTKVERVIVSGSIIHPHRGQVQIRLESPRGTISELLPLRPKDTSRDLLDWNFVSVNFFGENSRGIWKLHVTSEEDDVDFRVEMKMFKVVGTMS |
| Enzyme Length | 537 |
| Uniprot Accession Number | P91863 |
| Absorption | |
| Active Site | ACT_SITE 139; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 346; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Probable serine endoprotease which cleaves preproteins at paired basic amino acids (PubMed:16945111). May process FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides (PubMed:16945111). In muscles, involved in neuronal retrograde signaling by regulating presynaptic activity and localization of synaptic vesicle fusion protein unc-13 at the neuromuscular junction (NMJ) (PubMed:11804572). Acts in the intestine to regulate anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP) (PubMed:2323555, PubMed:11804572, PubMed:18852466, PubMed:25849533). Probably by regulating DMP, required for fatty acid uptake by intestinal cells and therefore regulates the levels of triglycerides in the intestine (PubMed:25849533). Plays a role in locomotion (PubMed:11804572). {ECO:0000269|PubMed:11804572, ECO:0000269|PubMed:16945111, ECO:0000269|PubMed:18852466, ECO:0000269|PubMed:2323555, ECO:0000269|PubMed:25849533}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (2); Mutagenesis (3); Propeptide (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18852466}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 11099033; 14551910; 15489339; 15990870; 17164286; 19343510; 20308279; 20439774; 20439776; 21085631; 21367940; 21980350; 22267497; 22286215; 22347378; 22500807; 22560298; 23665919; 23800452; 24884423; 25487147; 30827896; 6593563; 8962114; |
| Motif | |
| Gene Encoded By | |
| Mass | 58,705 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |