MGP has a high affinity binding to calcium ions, similar to other Gla-containing proteins.

The protein acts as an inhibitor of vascular mineralization and plays a role in bone organization.

In bone, its production is increased by vitamin D. The MGP was linked to the short arm of chromosome 12 in 1990.

Both have glutamate residues that are post-translationally carboxylated by the enzyme gamma-glutamyl carboxylase in a reaction that requires Vitamin K hydroquinone.

[10] Mice that lack MGP develop to term but die within two months as a result of arterial calcification which leads to blood-vessel rupture.