User:Nadia Dorochko
From Proteopedia
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== '''Factor IX ''' == | == '''Factor IX ''' == | ||
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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. | '''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. | ||
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The structure consists of 415 amino acides that are separated into an amino terminal Gla domain (12 Gla residues), which is a characteristic feature of all vitamin K–dependent factors. The Gla region is followed bt two tandem EGF domains (residues 85-127), activation peptide region which is cleaved off upon activation of FIX to FIXa , and a serine protease domain, which contains enzymatic activity. | The structure consists of 415 amino acides that are separated into an amino terminal Gla domain (12 Gla residues), which is a characteristic feature of all vitamin K–dependent factors. The Gla region is followed bt two tandem EGF domains (residues 85-127), activation peptide region which is cleaved off upon activation of FIX to FIXa , and a serine protease domain, which contains enzymatic activity. | ||
Revision as of 19:18, 18 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.
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