Coagulation Factor XIII A1 Polypeptide (F13A1)

F13-A1; FXIIIA1; Protein-glutamine gamma-glutamyltransferase A chain; Transglutaminase A chain; Coagulation factor XIII A chain

SPN	V719
HGNC	3531
MGI	1921395
PubMed	22565190
RGD	621495
UniProt	P00488
Wiki	F13A1

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.

Reference

"Amino acid sequence of the a subunit of human factor XIII."
Biochemistry 25:6900-6906(1986) [PubMed] [Europe PMC] [Abstract]

"Characterization of cDNA coding for human factor XIIIa."
Proc. Natl. Acad. Sci. U.S.A. 83:8024-8028(1986) [PubMed] [Europe PMC] [Abstract]

"Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor."
Proc. Natl. Acad. Sci. U.S.A. 85:5829-5833(1988) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta."
Proc. Natl. Acad. Sci. U.S.A. 83:8019-8023(1986) [PubMed] [Europe PMC] [Abstract]

"Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin."
Biochemistry 13:750-756(1974) [PubMed] [Europe PMC] [Abstract]

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]

"Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII."
Proc. Natl. Acad. Sci. U.S.A. 91:7296-7300(1994) [PubMed] [Europe PMC] [Abstract]

"Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII."
Thromb. Res. 78:389-397(1995) [PubMed] [Europe PMC] [Abstract]

"Two non-proline cis peptide bonds may be important for factor XIII function."
FEBS Lett. 423:291-296(1998) [PubMed] [Europe PMC] [Abstract]

"Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography."
J. Biol. Chem. 274:4917-4923(1999) [PubMed] [Europe PMC] [Abstract]

"Molecular basis for subtypic differences of the 'a' subunit of coagulation factor XIII with description of the genesis of the subtypes."
Hum. Genet. 94:129-135(1994) [PubMed] [Europe PMC] [Abstract]

"Identification of a point mutation in factor XIII A subunit deficiency."
Blood 80:937-941(1992) [PubMed] [Europe PMC] [Abstract]

"The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity."
Blood 92:2766-2770(1998) [PubMed] [Europe PMC] [Abstract]

"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]

Erratum
Nat. Genet. 23:373-373(1999)