| IED ID | IndEnz0002018938 | 
| Enzyme Type ID | protease018938 | 
| Protein Name | 
                        
                            
                                Carboxypeptidase E  CPE EC 3.4.17.10 Egg-laying defective protein 21  | 
                    
| Gene Name | egl-21 F01D4.4 | 
| 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 | MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLATNAMEITLELSCEKMPEGSQLPRFWEDNQKSIFEYVWKSHSGVKGMVVDAMTGEPIKRAVVWIRNGTETVPVKHPVTTWSEGDFYRVLPAGKYEIIVAAEGYDIAAKNVTVENKVRDSALVVNFALSPAADEPSENEQEQIAELVNEIARRR | 
| Enzyme Length | 472 | 
| Uniprot Accession Number | O17754 | 
| Absorption | |
| Active Site | ACT_SITE 329; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 | 
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; Evidence={ECO:0000303|PubMed:12657671, ECO:0000303|PubMed:17564681}; | 
| DNA Binding | |
| EC Number | 3.4.17.10 | 
| Enzyme Function | FUNCTION: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage (PubMed:17564681, PubMed:12657671). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671, PubMed:22275875). Involved in egg-laying, defecation and locomotion (PubMed:11813735, PubMed:17564681, PubMed:22275875). By processing FLP neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Involved in reducing pharyngeal pumping in response to high CO(2) levels (PubMed:25101962). {ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:22275875, ECO:0000269|PubMed:25101962}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (3); Metal binding (3); Signal peptide (1) | 
| Keywords | Carboxypeptidase;Cell projection;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc | 
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:12657671}. Perikaryon {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to axons in the nerve ring. {ECO:0000269|PubMed:12657671}. | 
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | 14704431; 16049479; 17164286; 17251413; 18316030; 18524955; 18818084; 19343510; 20439776; 21177967; 22286215; 22347378; 22560298; 23658528; 23665919; 23800452; 23852451; 25487147; 30454862; | 
| Motif | |
| Gene Encoded By | |
| Mass | 52,279 | 
| Kinetics | |
| Metal Binding | METAL 101; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 104; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 232; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 | 
| Rhea ID | |
| Cross Reference Brenda |