Detail Information for IndEnz0002011435
IED ID IndEnz0002011435
Enzyme Type ID protease011435
Protein Name Coagulation factor X-activating enzyme heavy chain
EC 3.4.24.58
Coagulation factor X-activating enzyme chain alpha
RVV-X heavy chain
Snake venom metalloproteinase
SVMP
Fragment
Gene Name
Organism Daboia russelii (Russel's viper) (Vipera russelii)
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) Daboia Daboia russelii (Russel's viper) (Vipera russelii)
Enzyme Sequence VATSEQFNKTFIELVIVVD
Enzyme Length 19
Uniprot Accession Number P86536
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.; EC=3.4.24.58; Evidence={ECO:0000250|UniProtKB:Q7LZ61};
DNA Binding
EC Number 3.4.24.58
Enzyme Function FUNCTION: Catalytic subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that acts in hemostasis. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond at position 234 and is also able to activate coagulation factor IX (F9) and protein C (PROC) by specific cleavage of Arg-Ile and Arg-Val bonds (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Non-terminal residue (1)
Keywords Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7LZ61}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 2,152
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda