Molecule functiona Molecule name Animal source (sp) Molecular mass (Da) Additional targets Functional characteristic Referenceb Factor X activators RVV-X Vipera russelli (Daboia russelli) 92,880 FIX metalloprotease, Ca2+ dependent Kisiel et al. [52]; Takeya et al. [50] VLFXA Vipera lebetina 89,400 FIX metalloprotease, Ca2+ dependent Siigur et al. [51,54] - Bungarus faciatus 70,000 S-2266 and S-2302 (kallikrein substrates) serine protease, Ca2+ dependent Zhang et al. [49] Losac Lonomia obliqua 45,000 - serine protease, Ca2+ independent Alvarez Flores et al. [33]           Prothrombin (FII) activators Ecarin Echis carinatus 56,000 or 72,000 - metalloprotease, Ca2+ independent group Ac   Yamada et al. [71]; Moore [72] Insularinase A Bothrops insularis 22,639 FX, fibrinogen, fibrin metalloprotease, group A Modesto et al. [40] Berythractivase Bothrops erythromelas 78,000 - metalloprotease, group A Silva et al. [41] Carinactivase-1 Echis carinatus 87,000 - Metalloprotease Ca2+ dependent, group B Yamada et al. [71] Pseutarin C Pseudonaja textilis ~250,000 - serine protease, dependent on Ca2+ and phospholipids, group C, structurally and functionally similar to the mammalian FXa-FVa complex Rao and Kini [39] Trocarin D Tropidechis carinatus 46,515 - serine protease, dependent on Ca2+, phospholipids and FVa group D, structurally similar to the mammalian FXa Joseph et al. [42] Textarin Pseudonaja textilis 53,000 - serine protease, dependent on Ca2+, phospholipids and FVa, group D Stocker et al. [73] Lopap Lonomia obliqua 69,000 or 20,800 - serine protease, its activity is enhanced by Ca2+ ions, structurally similar to lipocalin family members Reis et al. [4,44,45] Factor V activators RVV-V Vipera russelli (Dabioa russeli) 29,000 - serine protease Kisiel [1] LVV-V (VLFVA) Vipera lebetina (Daboia lebetina) 28,400 - serine protease Siigur et al. [54] Lonomin VI: a Lonomia achelous - - metalloprotease López et al. [59] Thrombin-like Ancrod (Arvin) Calloselasma rhodostoma (Agkistrodon rhodostoma) 48,000 (29,000d) - serine protease Burkhart et al. [94]; Yu et al. [93] Batroxobin (Reptilase or Defibrase) Bothrops atrox (Bothrops moojeni) 29,100 (25,503d) - serine protease Marsh [78]; Vu et al. [86] Thrombocytin Bothrops atrox 36,000 prothrombin, FXIII, FVIII and platelets serine protease Niewiarowski et al. [61]; Glusa et al [62] a Some molecules can display more than one function. bThe given references may not be of the first author to describe the respective molecules. cAccording to classification by Kini (2005) d Based on amino acid composition without carbohydrate content

Table 1: Biochemical properties of procoagulant proteins from snake and arthropod venoms.