| IED ID | IndEnz0002015509 |
| Enzyme Type ID | protease015509 |
| Protein Name |
Zinc metalloproteinase nas-37 EC 3.4.24.- Nematode astacin 37 |
| Gene Name | nas-37 C17G1.6 |
| 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 | MKSQACLKVCLALIGLVSIVSTAYIANDVVSDYAEVKELLAAFYRKHAKKYGHDYDPAAIQAIAENMDKSVKNDKTEATVNRKLWNEVFENDIILTLPQAESLLSESNSPRSRRQAHPDPRNFWPNLTISYEFYGGEETWRQLIRSAIRHVEQNVCFKFKENGGDRDGLRYYRGNGCWSNVGRVGGRQLVSIGYGCDSLGIVSHETLHALGLWHEQSRDDRDNFISIVADKITRGTEGNFAKRTAANSDNLGQPYDLGSVMHYGAKSFAYDWSSDTIKTRDWRYQNTIGQRDGLSFKDAKMINTRYCSNVCQRSLPCLNEGYTDPNNCGRCRCPSGYGGTYCETVEYTSCGGSLTASSSYKKIESGIVQPDANCVWRIRNPGGNVEVMFDQVNFQCADPCQSYVEVKYLSQKTSTGARLCCSLPSVIRSEGDDVIIILRGTPNTAVGWRGFTLKYRAIGGTPITPATVRPTYATTTRPYWTRTASGWIHIKNPPLYKPDGQIYTSDEQSAETKYSSEELYDPSTFLSPSSSSASPALLLPSDASPQRPSAQEHDLSQLSQNALTRPTPTTTVAPDTASWSAWGEWSACSQPCGGCGTKTRVRACYGGNQVCPGSNLDRESCNAHACAKPKKGMICNGRLLLPCDLLAKLNFGSNNYLNPKLKQSGFARSSTLPLPRISQRKPVFVNELEVHPPTERFLSSSTRRVKRQTANRFCEKRFIYQCPTALLTIQMEYKPDTQGTNDAYFQQYPECCSGYTPRRGVCYKN |
| Enzyme Length | 765 |
| Uniprot Accession Number | Q93243 |
| Absorption | |
| Active Site | ACT_SITE 205; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:15255192). Required during ecdysis, the opening of the cuticle to allow the worm to escape (PubMed:15539494). {ECO:0000250|UniProtKB:A8Q2D1, ECO:0000269|PubMed:15255192, ECO:0000269|PubMed:15539494}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (1); Metal binding (3); Mutagenesis (1); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Alternative splicing;Cleavage on pair of basic residues;Developmental protein;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15539494}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11231151; 12529635; 14551910; 15338614; 16122351; 17850180; 20109220; 22560298; 23800452; 25487147; 27129311; 27506200; |
| Motif | |
| Gene Encoded By | |
| Mass | 85,180 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 208; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 214; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda |