| IED ID | IndEnz0002006676 |
| Enzyme Type ID | protease006676 |
| Protein Name |
Neuroendocrine convertase 2 NEC 2 EC 3.4.21.94 Egg-laying defective protein 3 Kex2-like prohormone convertase 2 CELPC2 Prohormone convertase 2 PC2 Proprotein convertase 2 |
| Gene Name | egl-3 kpc-2 C51E3.7 |
| 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 | MKNTHVDLICVFLSIFIGIGEAVDVYTNHFHVHLKEGGGLEDAHRIAKRHGFINRGQVAASDNEYHFVQPALVHARTRRSAGHHAKLHNDDEVLHVEQLKGYTRTKRGYRPLEQRLESQFDFSAVMSPSDPLYGYQWYLKNTGQAGGKARLDLNVERAWAMGFTGKNITTAIMDDGVDYMHPDIKNNFNAEASYDFSSNDPFPYPRYTDDWFNSHGTRCAGEIVAARDNGVCGVGVAYDGKVAGIRMLDQPYMTDLIEANSMGHEPSKIHIYSASWGPTDDGKTVDGPRNATMRAIVRGVNEGRNGLGSIFVWASGDGGEDDDCNCDGYAASMWTISINSAINNGENAHYDESCSSTLASTFSNGGRNPETGVATTDLYGRCTRSHSGTSAAAPEAAGVFALALEANPSLTWRDLQHLTVLTSSRNSLFDGRCRDFPSLGINDNHRDSHGNCSHFEWQMNGVGLEYNHLFGFGVLDAAEMVMLAMAWKTSPPRYHCTAGLIDTPHEIPADGNLILEINTDGCAGSQFEVRYLEHVQAVVSFNSTRRGDTTLYLISPMGTRTMILSRRPKDDDSKDGFTNWPFMTTHTWGENPTGKWRLVARFQGPGAHAGTLKKFELMLHGTREAPYNLIEPIVGQTNKKLDTVQKAHKRSH |
| Enzyme Length | 652 |
| Uniprot Accession Number | G5ECN9 |
| Absorption | |
| Active Site | ACT_SITE 174; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 390; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.; EC=3.4.21.94; Evidence={ECO:0000303|PubMed:12657671, ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111, ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950}; |
| DNA Binding | |
| EC Number | 3.4.21.94 |
| Enzyme Function | FUNCTION: Serine endoprotease which cleaves preproteins at paired basic amino acids (PubMed:12657671, PubMed:15180830, PubMed:16945111, PubMed:23665919, PubMed:24671950). Processes FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides (PubMed:12657671, PubMed:16945111). Probably by processing flp-1 and flp-18, modulates the neuronal excitation-inhibition balance and thus the level of activity of the locomotor circuit (PubMed:23658528). Regulates sensitivity to mechanosensory stimuli (PubMed:11717360). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671). Probably by processing flp neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Cleaves pro-insulin-like proteins ins-3, ins-4 and ins-6 into their mature active forms (PubMed:23665919, PubMed:24671950). Together with convertase kpc-1, cleaves pro-insulin-like protein ins-18 (PubMed:24671950). By controlling ins-4 and ins-6 processing and thus the activation of the daf-2/InsR pathway, negatively modulates synapse development and synaptic transmission at neuromuscular junctions (PubMed:23665919). Similarly, by controlling ins-4 and ins-6 processing, negatively regulates dauer formation under optimal environmental conditions (PubMed:24671950). Under adverse environmental conditions, may promote dauer formation by processing ins-18, a daf-2/InsR antagonist (PubMed:24671950). May cleave dense-core vesicle membrane protein ida-1 (PubMed:15180830). Involved in egg-laying, fat storage and locomotion (PubMed:11813735, PubMed:11717360, PubMed:17564681). {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:15180830, ECO:0000269|PubMed:16945111, ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:23658528, ECO:0000269|PubMed:23665919, ECO:0000269|PubMed:24671950}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Mutagenesis (5); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Alternative splicing;Cell projection;Cleavage on pair of basic residues;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Ubl conjugation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:11717360}. Secreted {ECO:0000303|PubMed:24671950}. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated. {ECO:0000269|PubMed:23665919}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15338614; 15998808; 16049479; 17191499; 17251413; 17486083; 17850180; 18316030; 18524955; 18818084; 19535903; 19783783; 20454655; 20537990; 21177967; 21367940; 21980350; 22275875; 22560298; 23800452; 24698274; 25487147; 26584677; 27191843; 30454862; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,046 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |