| IED ID | IndEnz0002013522 |
| Enzyme Type ID | protease013522 |
| Protein Name |
Astacin-like metalloprotease toxin 3 EC 3.4.24.- Loxosceles astacin-like protease 3 LALP3 |
| Gene Name | |
| Organism | Loxosceles intermedia (Brown spider) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Araneae (spiders) Araneomorphae Haplogynae Scytodoidea Sicariidae Loxosceles Loxosceles intermedia (Brown spider) |
| Enzyme Sequence | MTTMSFFTVLSVAVCLCIEAGVEGSRLNGRDMLMQEESPLMERNALKYDSRLWPDGVVIYEFTSLRFYRKLIKRVMQHIADNTCITFKERTNEKGYVNIYNGKLFTCFADMGYYPFKQRLSLGLGCRSFGAILHELGHVLGLYHEQQRPDRDDYVIVYKDNIQTGALRDYEKRFENNTRVIGPFDYDSIMIYGETDARKSGSVTMKVKKPGATLVNASLKHELTALDIKKINTLYNCPGKDKF |
| Enzyme Length | 243 |
| Uniprot Accession Number | C9D7R3 |
| Absorption | |
| Active Site | ACT_SITE 135; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloprotease. Provoques deadhesion of endothelial cells from cell cultures, and also degradation of fibronectin, fibrinogen and gelatin in vitro. Its role in the venom is not fully understood but it might act as a spreading factor that facilitates diffusion of other venom toxins. Alternatively, it might be involved in the proteolytic processing of other venom toxins or it might play a role in extra-oral digestion of prey (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,942 |
| Kinetics | |
| Metal Binding | METAL 134; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 138; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 144; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.21; |