PROZ (Protein Z) is a 396 amino acids long (~62 kDa) vitamin K-dependent plasma glycoprotein. It has four domains: a gla-rich region, two EGF-like domains and a trypsin-like domain. It lacks the serine residue that would make it catalytically active as a serine protease. It is a member of the coagulation cascade, the group of blood proteins that leads to the formation of blood clots. It is vitamin K-dependent, and its functionality is therefore impaired in warfarin therapy. It is a glycoprotein. Although it is not enzymatically active, it is structurally related to several serine proteases of the coagulation cascade: factors VII, I, Xenopus/Amphibian,, , Xenopus/Amphibian, and protein C. The carbo, Xenopus/Amphibian,yglutamate residues (which require vitamin K) bind protein Z to phospholipid surfaces. The main role of protein Z appears to be the degradation of factor , Xenopus/Amphibian,a. This is done by protein Z-related protease inhibitor (ZPI), but the reaction is accelerated 1000-fold by the presence of protein Z. ZPI also degrades factor , Xenopus/Amphibian,I, but this reaction does not require the presence of protein Z. ZPI deficiency states have been associated with a propensity to thrombosis.
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