| IED ID | IndEnz0002015508 |
| Enzyme Type ID | protease015508 |
| Protein Name |
Zinc metalloproteinase nas-36 EC 3.4.24.- Nematode astacin 36 |
| Gene Name | nas-36 |
| Organism | Haemonchus contortus (Barber pole worm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Strongylida Trichostrongyloidea Haemonchidae Haemonchus Haemonchus contortus (Barber pole worm) |
| Enzyme Sequence | MLLLVLLFVFISATNASDVGRRELEKHFDVGDSSLDSVGDVLLKLKKLAHQRAFGNREFGHDAEEDSKKPVAISVLQPTVAKDVSPYLFEGDIFLSKKQAINILKEVSGIESKSKPNVRGRRSFDASPESKWPTTAPIKYRFHESIDFYAVSNIIKAIRYWENVTCLEFENSPDVADNEDFIEFFQGQGCYSMIGRNGGRQGVSIGENCVKAGVIEHEIGHAIGMWHEQSRPDAQSYIKVESDFILPSYVSDFLQRDKDIDTLGLPYDLGSVMHYGSTAFSVDQSSKTLITRDPLYQSTIGQRETLSFLDIETINKAYCSDRCSGSNDCKNGGYPHPKQCDTCLCPNGLSGPKCEDFEPPRKAECGGKIVVKEEWQSIESPGFPDPGYDPDQKCNWVFEVAGKRIEFEFIEEFSFLCTSTCVDYVEMKISADLRPTGFRWCCFNIPKGSFVSELNIAVIIFRSQLTNDVGFKLQARATDLPARTTPAPVVITTTPVPTTIEGTDQWAEWGSWSQCSRSCGGCGIMSRVRVCRTKQCKGRRQEFSTCNLKACPIDKHCAKLLANDKICNGRVCTKASQALSGCLEPQCCPPFINVDGTCQSDSPLLNDFELAK |
| Enzyme Length | 612 |
| Uniprot Accession Number | D5FM37 |
| Absorption | |
| Active Site | ACT_SITE 218; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000269|PubMed:20800010}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease (PubMed:20800010). Involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (By similarity). {ECO:0000250|UniProtKB:Q18206, ECO:0000269|PubMed:20800010}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (8); Domain (4); Glycosylation (2); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,068 |
| Kinetics | |
| Metal Binding | METAL 217; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 221; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 227; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda |