Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (PubMed:6425296). Under physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (By similarity).
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Hemophilia B
HEMB
An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma.
None
The disease is caused by variants affecting the gene represented in this entry.
Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:25251685, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493, PubMed:6603618, PubMed:8076946).
Thrombophilia, X-linked, due to factor IX defect
THPH8
A hemostatic disorder characterized by a tendency to thrombosis.
None
The disease is caused by variants affecting the gene represented in this entry.
Warfarin sensitivity, X-linked
WARFS
A condition characterized by sensitivity to warfarin, a drugs used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. Warfarin sensitive individuals develop bleeding complications when they are given warfarin within the therapeutic ranges.
None
The disease is caused by variants affecting the gene represented in this entry.
Activated by factor XIa, which excises the activation peptide (PubMed:1730085, PubMed:9169594, PubMed:22961984). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729).
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Belongs to the peptidase S1 family.
Detected in blood plasma (at protein level) (PubMed:19846852, PubMed:2592373, PubMed:3857619, PubMed:8295821, PubMed:9169594). Synthesized primarily in the liver and secreted in plasma.
Proteins
Metabolism
51778Da
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