| IED ID | IndEnz0002011471 |
| Enzyme Type ID | protease011471 |
| Protein Name |
Snake venom metalloproteinase ACLH SVMP EC 3.4.24.- ACL hemorrhagic toxin I ACLH-I ACLHT-I Hemorrhagic metalloproteinase ACLH |
| Gene Name | |
| Organism | Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Agkistrodon Agkistrodon contortrix (Copperhead) Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| Enzyme Sequence | MIQVLLVTLCLAAFPYQGSSIILESGNVNDYEVVYPRKVTPVPKGAVQPKYEDAMQYELKVNGEPVVLHLERNKGLFSKDYSETHYSPDGRKITTYPPVEDHCYYHGRIQNDADSIASISACNGLKGHFKLQGEMYLIEPLELSDSEAHAVFKYENVEKEDEAPKICGVTQNWESYEPIKKASQLNLNYQYQRYVELVTVVDHGMYTKYNGDSDKIRQWVHQMVNTMKESYRYMYIDISLAGVEIWSNKDLIDVQPAARHTLDSFGEWRERDLLHRISHDNAQLLTSTDFDGPTIGLAYVGTMCDPKLSTGVVEDHSKINFLVAVTMAHEMGHNLGMRHDTGSCSCGGYSCIMSPVISDDSPKYFSNCSYIQCWDFIMKENPQCILNKPLRTDTVSTPVSGDELLEA |
| Enzyme Length | 407 |
| Uniprot Accession Number | Q92032 |
| Absorption | |
| Active Site | ACT_SITE 330; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This zinc hemorrhagic metalloproteinase has fibrino(geno)lytic activities. It causes hemorrhage and has myonecrotic activity on both fiber types I and II. The recombinant enzyme, without post-translational modifications, also has proteolytic activity, but does not show any hemorrhagic activity. {ECO:0000269|PubMed:11072042, ECO:0000269|PubMed:15313443, ECO:0000269|PubMed:8444323}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Metal binding (7); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Secreted;Sialic acid;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains sialic acid terminally alpha(2-6)-linked to galactose in a complex N-glycan chain. {ECO:0000269|PubMed:15313443}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,109 |
| Kinetics | |
| Metal Binding | METAL 196; /note=Calcium; /evidence=ECO:0000250; METAL 280; /note=Calcium; /evidence=ECO:0000250; METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 384; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 387; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |