User:Nadia Dorochko
From Proteopedia
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| + | '''Factor IX''' (plasma thromboplastin component, Christmas factor, or hemophilia B factor) is a single-chain vitamin K-dependent procoagulant glycoprotein. It is synthesized by the liver hepatocyte as a [[pre-prozymogen]] that requires extensive posttranslational modification. The pre-prozymogen contains a pre-pro sequence that is followed by a polypeptide region. The pre-peptide is a hydrophobic signal peptide at its amino terminal that transports the growing polypeptide into the lumen of the Endoplasmic Reticulum. Once inside the ER, this signal peptide is cleaved by signal peptidase. The pro-peptide contained in the protein induces the docking of the polypeptide to the vitamin K-dependent carboxylase (γ-glutamyl carboxylase), where is modified by γ-carboxylation. The posttranslational modification creates a fully gamma-carboxylated mature zymogen which can now associate with anionic phospholipid surface. | ||
Revision as of 22:49, 16 April 2009
UVM, Biochemistry Ph.D student
Factor IX
Factor IX (plasma thromboplastin component, Christmas factor, or hemophilia B factor) is a single-chain vitamin K-dependent procoagulant glycoprotein. It is synthesized by the liver hepatocyte as a pre-prozymogen that requires extensive posttranslational modification. The pre-prozymogen contains a pre-pro sequence that is followed by a polypeptide region. The pre-peptide is a hydrophobic signal peptide at its amino terminal that transports the growing polypeptide into the lumen of the Endoplasmic Reticulum. Once inside the ER, this signal peptide is cleaved by signal peptidase. The pro-peptide contained in the protein induces the docking of the polypeptide to the vitamin K-dependent carboxylase (γ-glutamyl carboxylase), where is modified by γ-carboxylation. The posttranslational modification creates a fully gamma-carboxylated mature zymogen which can now associate with anionic phospholipid surface.
