Coagulation factor XIII A chain (F13A1)

The protein contains 732 amino acids for an estimated molecular weight of 83267 Da.

 

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. (updated: Oct. 10, 2018)

Protein identification was indicated in the following studies:

  1. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

(right-click above to access to more options from the contextual menu)

VariantDescription
Higher specific activity
FA13AD
dbSNP:rs3024472
FA13AD
FA13AD
FA13AD
dbSNP:rs3024477
FA13AD
FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin
FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin t
FA13AD; unknown pathological significance
FA13AD; unknown pathological significance
FA13AD
FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-an
FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin t
FA13AD
dbSNP:rs5984
allele F13A*1A, allele F13A*2A and allele F13*(2)A
dbSNP:rs5983
FA13AD
FA13AD
FA13AD
dbSNP:rs17852475
allele F13A*2A and allele F13A*2B
allele F13A*1A and allele F13A*1B
FA13AD
FA13AD
FA13AD
FA13AD

The reference OMIM entry for this protein is 134570

Factor xiii, a1 subunit; f13a1
F13a
Fibrin stabilizing factor, a subunit
Fsf, a subunit
Fibrinoligase
Transglutaminase, plasma

DESCRIPTION

The F13A1 gene encodes the A subunit of factor XIII (EC 2.3.2.13), the last enzyme generated in the blood coagulation cascade. It is the zymogen for fibrinoligase, a transglutaminase that forms intramolecular gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules and thus stabilizes blood clots. Plasma factor XIII is composed of 2 A subunits, which have catalytic function, and 2 noncatalyic B subunits (F13B; 134580), which likely act as carriers proteins. However, both platelet and placental factor XIII are composed only of 2 A subunits. All forms of factor XIII are proteolytically activated by thrombin (F2; 176930) (Takahashi et al., 1986).

CLONING

Takahashi et al. (1986) and Grundmann et al. (1986) characterized the amino acid sequence and the cDNA, respectively, of the alpha subunit of placental factor XIII. Takahashi et al. (1986) determined that subunit A of factor XIII is an unglycosylated 730-residue peptide with a molecular mass of 83 kD. They identified putative thrombin and calcium-binding sites. Grundmann et al. (1986) isolated cDNAs corresponding to placental F13A, which predicted a 732-residue protein. A 4-kb mRNA species was identified, but no leader sequence was found. Electrophoretic studies showed that the A subunits expressed in placenta and in the circulation are products of the same gene locus.

GENE STRUCTURE

Ichinose and Davie (1988) determined that the F13A1 gene contains 15 exons and spans over 160 kb. Five distinct functional domains were encoded by separate exons.

MAPPING

Olaisen et al. (1984) found linkage between the A component of factor XIII and the MHC complex (see, e.g., 142800) on chromosome 6p. The maximum lod score for males was 6.89 at theta = 0.08; for females it was 0.14 at theta = 0.44. No indication of linkage to PGM3 (172100) on chromosome 6q was found. Using polymorphism of F13A in family studies, Eiberg et al. (1984) confirmed linkage with HLA (maximum lod = 5.18 at theta = 0.17 in males and 0.14 at theta = 0.37 in females). In a family segregating for all 3 loci, the gene order F13A, HLA, and GLO (138750) on 6p21 was established. Board et al. (1984) concluded that the F13A locus is distal to HLA, probably in the 6p22 region. In a later publication, Olaisen et al. (1985) reported a maximum lod score, in males, of 7.60 at theta of 0.18 for the F13A versus HLA linkage. Since the Hageman factor gene (F12; 610619) is located in the same region of 6p, there may be a cluster of coagulation genes there. HGM8 (Helsinki, 1985) placed the F13A locus in the segment of chromosome 6pter-p23. Nishigaki et al. (1986) commented on the conflicting evidence on linkage of HLA and F13A. In their own studies, the maximum lod score was only 0.33 for males at theta = 0.30; in females the lod score was negative at all values of theta. Zoghbi et al. (1988) found 3 RFLPs at the F13A locus. Together they showed heterozygosity of 91%. Using these markers, they found linkage to HLA with a maximum lod score of 11.44 at a recombination fraction of 0.25 for males and 0.35 for females. Wong et al. (1988) reported information on the linkage relationship of F13A to HLA, GLO1, and PLG (173350), based on the analysis of 44 kindreds. In their study, paternal F13A-HLA lod scores peaked at theta = 0.09; maternal F13A-HLA lod scores peaked at theta = 0.20. Paternal F13A-GLO1 lod scores peaked at theta = 0.22; maternal F13A-GLO1 lod scores were negative at all theta va ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 134570 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).