The Reactome event describes intracellular accumulation and/or decreased secretion of FIX due to different HB-related genetic alterations spread throughout the F9 gene. The F9 variants are described in relation to changes in the protein sequence. Defective splicing events induced by F9 mutations are not shown here.", "cellular_location": "endoplasmic reticulum lumen", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00740-1" ], "evidence": [ { "id": "R-HSA-9670888", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670888" } ] }, { "id": "R-HSA-9673223", "name": "FIX(29-461) variant is not activated (factor XIa catalyst)", "equation": "", "summary": "In healthy individuals, conversion of factor IX (FIX) to the activated FIX is a calcium-dependent process catalyzed by factor VIIa (FVIIa) in the presence of tissue factor and phosphatidyl serine-rich phospholipid (Vadivel K & Bajaj SP 2012) or by factor XIa (FXIa) in a phospholipid-independent reaction (Wolberg AS et al. 1997; Smith SB et al. 2008; Geng Y et al. 2012). Regardless of the activating protease, FIX is cleaved first after Arg191 (R191-A192, the \u03b1-cleavage) forming the intermediate FIX product, then after the residue 226 (R226-V227, the \u03b2-cleavage) to form the activated FIXa (FIXa\u03b2) (Smith SB et al. 2008; Geng Y et al. 2012; Mohammed BM et al. 2018). Deficiency or dysfunction of FIX leads to hemophilia B (HB), an X-linked, recessive, bleeding disorder. On a molecular level, HB is due to a heterogeneous spectrum of mutations spread throughout the F9 gene (Rallapalli PM et al. 2013).
The Reactome event describes the defective proteolytic activation of FIX by factor XIa due to the presence of HB-associated point mutations R191C, R191H, R226Q and R226W in the cleavage sites of FIX (Liddell MB et al. 1989; Monroe DM et al. 1989; Suehiro K et al. 1989; Diuguid DL et al. 1989; Bertina RM et al.1990). In addition, naturally occurring point mutations in the FIX propeptide sequence such as R43Q, R43L or R46S are also annotated here. These FIX variants are secreted into the circulation with a mutant 18-amino acid propeptide still attached (Bentley AK et al. 1986; Galeffi P & Brownlee GG 1987). The unprocessed FIX variants were found to affect the function of the protein by destabilizing the calcium-induced conformation of FIX (Wojcik EG et al. 1997) and showed delayed activation by FXIa (Liddell MB et al. 1989; Ware J et al. 1989; de la Salle C et al. 1993; Wojcik EG et al. 1997; Bristol JA et al. 1993).
",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00740-1",
"P03951-1"
],
"evidence": [
{
"id": "R-HSA-9673223",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9673223"
}
]
},
{
"id": "R-HSA-9673231",
"name": "GGCX does not gamma-carboxylate 3D-F9(29-461) (pro-factor IX)",
"equation": "",
"summary": "Being a vitamin K\u2010dependent (VKD) glycoprotein, factor IX (FIX) is synthesized first as a precursor protein which then undergoes extensive posttranslational modification including \u03b3-carboxylation. The precursor FIX protein has the following parts, starting with a signal peptide at the amino-terminal end, which directs the protein to the endoplasmic reticulum (ER), and continuing with the 18 residue length propeptide. The propeptide contains the \u03b3\u2010carboxylase recognition site (\u03b3\u2010CRS) in the N\u2010terminal part of the propeptide for connecting substrate to the gamma-glutamyl carboxylase (GGCX), and a peptidase recognition site in the C\u2010terminal for cleaving by PACE/furin (Higgins\u2010Gruber SL et al. 2010). GGCX in the ER \u03b3-carboxylates twelve glutamate residues on F9(29-461) (pro-factor IX) converting the specific glutamic acids in the GLA domain to \u03b3\u2010carboxyglutamic acid residues. MK4 (vitamin K hydroquinone) is oxidized to MK4 epoxide in the process (Berkner KL 2000; Furie B et al. 1999; Stenina O et al. 2001; Morris DP et al. 1995; Ware J et al. 1989). The signal peptide and the propeptide sequence of FIX are removed before the protein is secreted into the circulation,
Naturally occurring hemophilia B (HB)-associated point mutations in the FIX propeptide sequence such as F9 N43Q/L or F9 N46S reduce affinity to GGCX resulting in reduced \u03b3-carboxylation and aberrant propeptide processing (Bentley AK et al. 1986; Rabiet MJ et al. 1987; Diuguid DL et al. 1986; Ware J et al. 1989; de la Salle C et al. 1993). FIX variants are secreted into the circulation with a mutant 18-amino acid propeptide still attached (Bentley AK et al. 1986; Galeffi P & Brownlee GG 1987). However, unprocessed FIX variants showed altered phospholipid binding properties and delayed activation by factor XIa (Liddell MB et al. 1989; Ware J et al. 1989; de la Salle C et al. 1993; Wojcik EG et al. 1997; Bristol JA et al. 1993, 1994). In addition, beta-hydroxylation of aspartic acid 110 (D110) is an independent process which does not require vitamin K and is mediated through a hydroxylation recognition site in the mature Factor IX, not in the propeptide (Rabiet MJ et al. 1987).
The Reactome event describes defective \u03b3-carboxylation of FIX variants due to HB-associated genetic defects in the propeptide sequence of the F9 gene.
",
"cellular_location": "endoplasmic reticulum lumen, endoplasmic reticulum membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00740-1",
"P38435-1"
],
"evidence": [
{
"id": "R-HSA-9673231",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9673231"
}
]
}
],
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