Coagulation factor XIII, A1 polypeptide

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Coagulation factor XIII, A1 polypeptide
Protein F13A1 PDB 1evu.png
PDB rendering based on 1evu.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols F13A1 ; F13A
External IDs OMIM134570 MGI1921395 HomoloGene20077 ChEMBL: 4530 GeneCards: F13A1 Gene
EC number
RNA expression pattern
PBB GE F13A1 203305 at tn.png
More reference expression data
Species Human Mouse
Entrez 2162 74145
Ensembl ENSG00000124491 ENSMUSG00000039109
UniProt P00488 Q8BH61
RefSeq (mRNA) NM_000129 NM_001166391
RefSeq (protein) NP_000120 NP_001159863
Location (UCSC) Chr 6:
6.14 – 6.32 Mb
Chr 13:
36.87 – 37.05 Mb
PubMed search [1] [2]

Coagulation factor XIII A chain is a protein that in humans is encoded by the 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 composed of just 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.[1]


Coagulation factor XIII, A1 polypeptide has been shown to interact with F13B.[2][3]


  1. ^ "Entrez Gene: F13A1 coagulation factor XIII, A1 polypeptide". 
  2. ^ Carrell NA, Erickson HP, McDonagh J (Jan 1989). "Electron microscopy and hydrodynamic properties of factor XIII subunits". J. Biol. Chem. 264 (1): 551–6. PMID 2491853. 
  3. ^ Achyuthan KE, Rowland TC, Birckbichler PJ, Lee KN, Bishop PD, Achyuthan AM (Sep 1996). "Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin". Mol. Cell. Biochem. 162 (1): 43–9. doi:10.1007/bf00250994. PMID 8905624. 

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