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From Proteopedia

Protein Z

Table of Contents

Background

Protein Z (PZ) is a vitamin k-dependent glycoprotein made in the liver and involved in the blood-clot-forming coagulation cascade. Bovine PZ was first identified by Prowse and Esnouf in 1977 and Human PZ was first isolated and studied by Broze Jr. and Miletich in 1984. The gene coding for PZ, called PROZ, was found in 1998 on chromosome 13 at location 13q34 and is composed of nine exons (one being an alternative exon). PZ consists of a gla-rich area, two EGF-like regions, and a trypsin-like domain and has a molecular weight of 62 kDa. PZ genetically and structurally mimics other factors of the coagulation cascade but it is not a catalyticaly active enzyme. PZ is not like the other vitamin k-dependent coagulation factors because it does not have an active center, thus it lacks the serine needed for an active site of serine proteases, like the coagulation factors VII, IX, X, and protein C. PZ's 396 amino acid sequence is N-terminally analogous to the serine protease coagulation factors, whose similarly composed genes are found clustered together along with PROZ on chromosome 13.

Structure

Function

Clinical Relevance

References