| IED ID | IndEnz0002011805 |
| Enzyme Type ID | protease011805 |
| Protein Name |
Zinc metalloproteinase partitagin EC 3.4.24.- Fragment |
| Gene Name | |
| Organism | Hippasa partita (Funnel-web spider) (Hippasa deserticola) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Araneae (spiders) Araneomorphae Entelegynae RTA clade Lycosoidea Lycosidae (wolf spiders) Hippasa Hippasa partita (Funnel-web spider) (Hippasa deserticola) |
| Enzyme Sequence | AYDPDPYKRYSAEHTFFLL |
| Enzyme Length | 19 |
| Uniprot Accession Number | P85975 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, 1,10-phenanthroline, cyanide, and serum alpha2-microglobulin. Not inhibited by EGTA, PMSF, leupeptin, pepstatin and aprotinin. {ECO:0000269|PubMed:17555860, ECO:0000269|PubMed:21150580}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloproteinase that causes hemorrhage in mice following intradermal injection and impairs hemostasis in its prey. In skin tissues, it degrades components of the basement membrane surrounding blood vessels and capillaries. In muscle tissue, it degrades the extracellular matrix, thus causing muscle necrosis. However, it lacks direct toxicity on myocytes. Hydrolyzes alpha-2 chain (COL4A2) of type IV collagen more slowly than the alpha-1 chain (COL4A1). Hydrolyzes fibronectin (FN1). It also impairs hemostasis by acting on fibrin(ogen) and platelets. Shows fibrinolytic activity, with a selective degradation of gamma-dimer (FGG). Shows fibrinogenolytic activity by preferentially cleaving the Bbeta chain, and later gamma-chain. Aalpha-chain remains resistant to proteolytic digestion. Weakly inhibits collagen-triggered platelet aggregation of human plasma rich platelet. {ECO:0000269|PubMed:17555860, ECO:0000269|PubMed:21150580}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:17555860}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. {ECO:0000269|PubMed:17555860}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17555860}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,334 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |