GLA domain

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain  is a protein domain that contains post-translational modifications of many glutamate residues by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla). The Gla residues are responsible for the high-affinity binding of calcium ions.

The GLA domain is responsible for the high-affinity binding of calcium ions. It starts at the N-terminal extremity of the mature form of proteins and ends with a conserved aromatic residue; a conserved Gla-x(3)-Gla-x-Cys motif is found in the middle of the domain which seems to be important for substrate recognition by the carboxylase.

The 3D structures of several Gla domains have been solved. Calcium ions induce conformational changes in the Gla domain and are necessary for the Gla domain to fold properly. A common structural feature of functional Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane.

Subfamilies

 * Coagulation factor, Gla region

Human proteins containing this domain
BGLAP;    F10;       F2;        F7;        F9;        GAS6;      MGP;       PROC; PROS1;    PROZ;      PRRG1;     PRRG2;     PRRG3;     PRRG4;