Aliases for F13A1 Gene
External Ids for F13A1 Gene
Previous HGNC Symbols for F13A1 Gene
Previous GeneCards Identifiers for F13A1 Gene
This gene encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion. [provided by RefSeq, Jul 2008]
GeneCards Summary for F13A1 Gene
F13A1 (Coagulation Factor XIII A Chain) is a Protein Coding gene. Diseases associated with F13A1 include Factor Xiiia Deficiency and Factor Xiii Deficiency. Among its related pathways are Platelet activation, signaling and aggregation and Collagen biosynthesis and modifying enzymes. GO annotations related to this gene include protein-glutamine gamma-glutamyltransferase activity. An important paralog of this gene is TGM5.
UniProtKB/Swiss-Prot for F13A1 Gene
Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.