GLA Domain | |||||||||
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Anchoring of Coagulation factor VIIa to the membrane through its GLA domain | |||||||||
Identifiers | |||||||||
Symbol | Gla | ||||||||
Pfam | PF00594 | ||||||||
InterPro | IPR000294 | ||||||||
PROSITE | PDOC00011 | ||||||||
SCOP | 1cfi | ||||||||
OPM family | 97 | ||||||||
OPM protein | 1pfx | ||||||||
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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. [1][2]
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[3] 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.[4][5] 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.[5]
BGLAP; F10; F2; F7; F9; GAS6; MGP; PROC; PROS1; PROZ; PRRG1; PRRG2; PRRG3; PRRG4;