Detail Information for IndEnz0002011982
IED ID IndEnz0002011982
Enzyme Type ID protease011982
Protein Name Snake venom serine protease Afaacytin alpha/beta/beta' chains
SVSP
EC 3.4.21.-
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 VIGGAECNINEHRSLVLLYXSSSXFGE
Enzyme Length 27
Uniprot Accession Number Q9PRM8
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP), benzamidine, heparin and hirudin, but not by plasmatic thrombin inhibitors, antithrombin-III and ecotin. {ECO:0000269|PubMed:8521839}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Snake venom serine protease that exhibits alpha-fibrinase and beta-fibrinogenase activities. It replaces missing factors VIII (F8) and IX (F9) in deficient plasmas by activating purified human factor X (F10) into factor Xa. It releases serotonin from platelets and induces platelet aggregation in human (but not in rabbit). Has caseinolytic, arginine-esterase and amidase activities. {ECO:0000269|PubMed:8521839}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1)
Keywords Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;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 PTM: Both chains alpha and beta are N-glycosylated.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 2,918
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda