Sandbox Reserved 596
From Proteopedia
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'''Background''' | '''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 factors VII, IX, X, and protein C. | + | 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. |
Revision as of 00:45, 7 April 2013
| This Sandbox is Reserved from Feb 1, 2013, through May 10, 2013 for use in the course "Biochemistry" taught by Irma Santoro at the Reinhardt University. This reservation includes Sandbox Reserved 591 through Sandbox Reserved 599. |
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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
