Transglutaminase, C-terminal

AccessionIPR008958; (Transglutaminase_C) matches 1931 proteins
FullNameTransglutaminase, C-terminal
SignaturesPFAM: PF00927 Transglut_C

Synonym(s): Protein-glutamine gamma-glutamyltransferase, Fibrinoligase, TGase

Transglutaminases catalyse the post-translational modification of proteins at glutamine residues, with formation of isopeptide bonds. Members of the transglutaminase family usually have three domains: N-terminal (), middle () and C-terminal. The middle domain is usually well conserved, but family members can display major differences in their N- and C-terminal domains, although their overall structure is conserved []. This entry represents the C-terminal domain found in transglutaminases, which consists of an immunoglobulin-like beta-sandwich consisting of seven strands in two sheets with a Greek key topology.

The best known transglutaminase is blood coagulation factor XIII, a plasma tetrameric protein composed of two catalytic A subunits and two non-catalytic B subunits. Factor XIII is responsible for cross-linking fibrin chains, thus stabilising the fibrin clot. Protein-glutamine gamma-glutamyltransferases () are calcium-dependent enzymes that catalyse the cross-linking of proteins by promoting the formation of isopeptide bonds between the gamma-carboxyl group of a glutamine in one polypeptide chain and the epsilon-amino group of a lysine in a second polypeptide chain. TGases also catalyse the conjugation of polyamines to proteins [, ].

  1. Greenberg CS, Birckbichler PJ, Rice RH. (1991)
    Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues.
    FASEB J. 5: 3071-7
    [PUBMED:1683845] [PUB00001513]
  2. Ichinose A, Bottenus RE, Davie EW. (1990)
    Structure of transglutaminases.
    J. Biol. Chem. 265: 13411-4
    [PUBMED:1974250] [PUB00002570]
  3. Casadio R, Polverini E, Mariani P, Spinozzi F, Carsughi F, Fontana A, Polverino de Laureto P, Matteucci G, Bergamini CM. (1999)
    The structural basis for the regulation of tissue transglutaminase by calcium ions.
    Eur. J. Biochem. 262: 672-9
    [PUBMED:10411627] [PUB00010639]
Database linksEC:;
PDB: 1evu; PDB: 1ex0; PDB: 1f13; PDB: 1fie; PDB: 1g0d; PDB: 1ggt; PDB: 1ggu; PDB: 1ggy; PDB: 1kv3; PDB: 1l9m; PDB: 1l9n; PDB: 1nud; PDB: 1nuf; PDB: 1nug; PDB: 1qrk; PDB: 2q3z; PDB: 2xzz; PDB: 3ly6; PDB: 3s3j; PDB: 3s3p; PDB: 3s3s; PDB: 4kty; CATH:; SCOP: b.1.5.1;
Taxonomy DistributionEukaryota: 1931
Arthropoda: 619
Chordata: 1211
Eukaryota: 1931
Metazoa: 1931
Mouse: 23
Nematoda: 32
Arthropoda: 42
Chordata: 6
Metazoa: 1929
Nematoda: 29
Chordata: 1196
Nematoda: 3
Arthropoda: 577
Chordata: 9
Metazoa: 1
Metazoa: 1
FruitFly: 3
Human: 38
Metazoa: 1