IED ID | IndEnz0002009950 |
Enzyme Type ID | protease009950 |
Protein Name |
Serine protease harobin EC 3.4.21.- Fibrin ogen olytic enzyme Snake venom serine protease SVSP |
Gene Name | |
Organism | Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis hardwickii) |
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 Hydrophiidae Hydrophis Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis hardwickii) |
Enzyme Sequence | MPLIRVLASLLILQLSYGKSLDNGAKAITSLDRIIGGFECNPSEHRSLVYLYNSAGFFCSGTLLNHEWVLTAAHCNREDIQIRLGVHNVHVHYEDEQIRVPKEKLCCLSTNNCTQFSQDIMLIRLNSPVNYSEHIAPLSLPSNPPSMGSVCCVMGWGTITSPEVTYPEVPHCVDINILHIPVCQAAYPTMSGKNILCAGILEGGKDSCKGDSGGPLICNGQIQGIVSWGRFPCAQFLEPGIYTKVFDYKDWIEGIIAGNSNVICP |
Enzyme Length | 265 |
Uniprot Accession Number | Q5MCS0 |
Absorption | |
Active Site | ACT_SITE 74; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 119; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 212; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:17544404}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Serine protein with fibrinolytic and fibrinogenolytic activities. Degrades Bbeta-chain (FGB) of fibrinogen first and then the Aalpha-chain (FGA). Gamma-chain (FGG) are also digested on prolonged incubation. In vitro, it cleaves high molecular weight (HMW) kininogen (KNG) releasing bradykinin that promotes vasodilation. In vitro and in vivo, it cleaves angiotensin-2 (AGT). This explains the reduction of blood pressure in hypertensive rats. Has also antithrombotic effects on thrombosis animal models. {ECO:0000269|PubMed:17544404}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:17544404}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:17544404}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (2); Mutagenesis (2); Propeptide (1); Signal peptide (1) |
Keywords | Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Hypotensive agent;Protease;Secreted;Serine protease;Signal;Toxin;Vasoactive;Vasodilator;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Harobin contains three additional Cys residues than other snake venom serine proteases, suggesting an additional disulfide bond. In addition, it is more stable than other snake 6-disulfide-bond serine proteases, since it is less sensitive to DTT. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 28,996 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for n-p-tosyl-gly-pro-arg p-nitroanilide {ECO:0000269|PubMed:17544404}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |