| IED ID | IndEnz0002012272 |
| Enzyme Type ID | protease012272 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like agkihagin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| 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) Deinagkistrodon Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| Enzyme Sequence | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPEGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADLTASISACNGLKGHFMLQGEMYLIEPLKLSDSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQSNLTPEQQRYLNAPKFVKLFLVADNIMYLKYGRSLTNVRTRMYDMANILNLIFRRMNIHVAVTDLEIWSDKDKIIVQPSADDTLKSFATWRESVLLKHKSHDNAQLLTGINFNGPTAGLAYLGGICDPMYSTAIVQDHNKIHHLVAIAMAHEMGHNLGIDHDKDTCTCAAKSCVMAGTLSCEASYLFSDCSRKEHRAFLIKNMPQCILKKPSKTDVVSPPVCGNYFVEMGEDCDCGSPATCRDPCCDAATCKLKQGAQCAEGLCCDQCRFKGAGTQCRAAMDECDMADLCTGQSADCTDRFQKNGQPCQNNNGYCYNGTCPTMIKQCTVFFGSNAAVSQDACFQFNLQGNNYGYCRKEQNTKIACEPQNVKCGRLYCTSPEKQNPCNIYYSPSNEDKGMVLPGTKCADGKACSNGQCVDVTTPY |
| Enzyme Length | 608 |
| Uniprot Accession Number | Q1PS45 |
| Absorption | |
| Active Site | ACT_SITE 336; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA. Not inhibited by PMSF, antipain, pepstatin, and iodoacetamide (By similarity). {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Strongly inhibits the collagen-induced human platelet aggregation. Hydrolyzes the Aalpha-chain of fibrinogen (FGA), without cleavage of Bbeta- and gamma-chains. Induces apoptosis and strongly inhibits proliferation of endothelial cells as well as adhesion of the cells to extracellular matrix proteins (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (1); Metal binding (14); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Apoptosis;Calcium;Cell adhesion impairing toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 467..469; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 67,573 |
| Kinetics | |
| Metal Binding | METAL 335; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 345; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 405; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 408; /note=Calcium 1; /evidence=ECO:0000250; METAL 410; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 412; /note=Calcium 1; /evidence=ECO:0000250; METAL 415; /note=Calcium 1; /evidence=ECO:0000250; METAL 418; /note=Calcium 1; /evidence=ECO:0000250; METAL 469; /note=Calcium 2; /evidence=ECO:0000250; METAL 470; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 472; /note=Calcium 2; /evidence=ECO:0000250; METAL 483; /note=Calcium 2; /evidence=ECO:0000250; METAL 484; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |