Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1988 Aug;85(16):5829-33.
doi: 10.1073/pnas.85.16.5829.

Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor

A Ichinose  1 , E W Davie
Affiliations

Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor

A Ichinose et al. Proc Natl Acad Sci U S A. 1988 Aug.

Abstract

Factor XIII (plasma transglutaminase, fibrin stabilizing factor) is a glycoprotein that circulates in blood as a tetramer (a2b2) consisting of two a and two b subunits. The primary structures of the a and b subunits of human factor XIII have been reported by a combination of cDNA cloning and amino acid sequence analysis. To establish the gene structure of the a subunit for factor XIII, several human genomic libraries were screened by using the cDNA encoding the a subunit as a probe. Among approximately equal to 5 x 10(7) recombinant phage, 121 have been shown to contain an insert encoding a portion of the a subunit. Twenty-five unique clones were then characterized by restriction mapping, Southern blotting, and DNA sequencing. Overlapping clones encoding the a subunit of factor XIII span greater than 160 kilobases. The gene was found to contain 15 exons separated by 14 introns. All the sequences of the introns at the intron-exon boundaries were GT-AG, which are the same as those found in other eukaryotic genes. DNA sequence analysis revealed that the activation peptide released by thrombin, the active site cysteine region, the two putative calcium-binding regions, and the thrombin cleavage site leading to inactivation are encoded by separate exons. This suggests that the introns may separate the a subunit into functional and structural domains. A comparison of the amino acid sequence deduced from the genomic DNA sequence with those deduced from cDNA or determined by amino acid sequence analysis of the plasma and placental proteins revealed apparent amino acid polymorphisms in six positions of the polypeptide chain of the a subunit.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Mol Cell Biol. 1985 Oct;5(10):2713-9 - PubMed
    1. Biochemistry. 1988 Apr 19;27(8):2898-905 - PubMed
    1. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8019-23 - PubMed
    1. Proc Natl Acad Sci U S A. 1970 Jun;66(2):472-9 - PubMed
    1. Ann N Y Acad Sci. 1972 Dec 8;202:190-9 - PubMed

Publication types

LinkOut - more resources