F10 Gene - Coagulation Factor X
Essential serine protease in the blood coagulation cascade
Gene Information Card
| Symbol | F10 |
|---|---|
| Full Name | Coagulation factor X |
| Gene Type | protein-coding |
| Chromosomal Location | 13q34 |
| NCBI Gene ID | 2159 ncbi.nlm.nih.gov/gene/2159 |
| Ensembl ID | ENSG00000126218 |
| UniProt ID | P00742 |
| OMIM ID | 613872 |
| HGNC ID | 3530 |
| Aliases | FX, FXA, Stuart factor, Stuart-Prower factor |
Description
The F10 gene encodes coagulation factor X, a vitamin K-dependent serine protease that plays a central role in blood coagulation. Factor X is synthesized in the liver and secreted as a zymogen. Upon activation by factor IXa (in the intrinsic pathway) or factor VIIa (in the extrinsic pathway), factor Xa converts prothrombin to thrombin, initiating the common coagulation pathway. Mutations in F10 cause factor X deficiency, a rare bleeding disorder, and polymorphisms influence warfarin sensitivity.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Factor X deficiency | Loss-of-function mutations in F10 reduce factor X activity, impairing thrombin generation and leading to bleeding tendency. | ClinVar, OMIM |
| Thrombophilia | Gain-of-function variants (e.g., p.Gly380Arg) increase factor Xa activity, predisposing to venous thromboembolism. | ClinVar, OMIM |
| Warfarin sensitivity | Polymorphisms in F10 affect warfarin dose requirements by altering factor X synthesis or activity. | NCBI Gene, ClinVar |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 38.2 | High |
| Pancreas | 0.6 | Low |
| Kidney | 0.3 | Low |
| Lung | 0.2 | Low |
| Heart | 0.1 | Not detected |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 | 45.1 | Hepatocellular carcinoma cell line; high expression |
| Huh-7 | 32.8 | Hepatoma cell line |
| HEK293 | 0.5 | Low expression |
| K562 | 0.1 | Not detected |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.488G>A (p.Gly163Asp) | Missense | Rare | Loss of function; associated with factor X deficiency |
| c.1138G>A (p.Gly380Arg) | Missense | Rare | Gain of function; associated with thrombophilia |
| c.1A>G (p.Met1Val) | Missense | Rare | Loss of function; initiation codon mutation causing factor X deficiency |
| c.1240C>T (p.Arg414Cys) | Missense | Rare | Loss of function; disrupts disulfide bond formation |
Mutation functional classification
Loss of Function (LOF)
Missense, nonsense, frameshift, and splice-site mutations that reduce factor X activity cause factor X deficiency (autosomal recessive bleeding disorder).
Gain of Function (GOF)
Missense mutations such as p.Gly380Arg increase factor Xa activity and are associated with thrombophilia.
Dominant Negative (DN)
Not reported for F10; factor X deficiency is typically recessive.
View complete mutation data：
Gene Ontology (GO)
| • serine-type endopeptidase activity | • calcium ion binding |
| • blood coagulation | • proteolysis |
| • extracellular space | • endoplasmic reticulum lumen |
Pathways
• Blood coagulation (intrinsic and extrinsic pathways)
• Common pathway of coagulation
• Vitamin K metabolism
Protein Summary
Coagulation factor X is a vitamin K-dependent glycoprotein synthesized as a single-chain zymogen (precursor) of 488 amino acids. After removal of the signal peptide and propeptide, the mature protein circulates as a two-chain molecule (light chain and heavy chain) linked by a disulfide bond. The light chain contains a Gla domain (calcium binding) and two EGF-like domains; the heavy chain contains the serine protease catalytic domain. Activation by factor IXa or VIIa cleaves the activation peptide, yielding factor Xa, which then converts prothrombin to thrombin.
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