Detail Information for IndEnz0002013531
IED ID IndEnz0002013531
Enzyme Type ID protease013531
Protein Name Snake venom serine protease IVa
SVSP
EC 3.4.21.-
Basic proteinase IVa
Fragment
Gene Name
Organism Cerastes cerastes (Horned desert viper)
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 Viperinae (vipers) Cerastes Cerastes cerastes (Horned desert viper)
Enzyme Sequence VIGGAEENINEHRSL
Enzyme Length 15
Uniprot Accession Number Q7LZF4
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inactivated by p-APMSF, leupeptin, iodoacetamide, protein kinase C inhibitor, phosphatase inhibitor, ATP and PGE1. Is insensitive to acetylsalicylic acid, ADP scavenger system, protein kinase A inhibitor and hirudin. {ECO:0000269|PubMed:7612660}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Snake venom serine protease that potently induces platelet aggregation. Its aggregatory activity is partially inhibited by monoclonal antibodies against GPIb and the thrombin receptor. Its ability to induce intracellular Ca(2+) release is blocked by pretreating platelets with thrombin. Hydrolyzes thrombin chromogenic substrate CBS 34.47, but shows very weak coagulant activity. Can hydrolyze fibrinogen alpha-chains. {ECO:0000269|PubMed:7612660}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Non-terminal residue (1)
Keywords Direct protein sequencing;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 1,638
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda