Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant epoxidation of vitamin K hydroquinone to vitamin K epoxide (PubMed:17073445, PubMed:39880952, PubMed:39880037). Couples epoxidation and carboxylation in the same active site (PubMed:39880952, PubMed:39880037). Catalyzes gamma-carboxylation of blood coagulation factors (F2, F7, F9 and F10) and anticoagulants such as PROC, which are essential for thrombosis(PubMed:17073445, PubMed:39880037).

Catalyzes gamma-carboxylation of osteocalcin/BGLAP, which is essential for bone metabolism (PubMed:17073445, PubMed:39880952). Catalyzes gamma-carboxylation of matrix Gla protein (MGP) and other transmembrane gamma-Gla proteins such as PRRG2, which are essential for calcium homeostasis and haemostasis (PubMed:17073445, PubMed:39880037)

Monomer (PubMed:11570873, PubMed:39880952, PubMed:39880037). May interact with CALU (By similarity)

• Combined deficiency of vitamin K-dependent clotting factors 1 (VKCFD1)

  VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K.

• Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD)

  Characterized by hyperlaxity of the skin involving the entire body. Important phenotypic differences with classical PXE include much more severe skin laxity with spreading toward the trunk and limbs with thick, leathery skin folds rather than confinement to flexural areas, and no decrease in visual acuity. Moreover, detailed electron microscopic analyses revealed that alterations of elastic fibers as well as their mineralization are slightly different from those in classic PXE.