Beta-1,4-galactosyltransferases (beta-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a beta-1,4 linkage to an acceptor sugar. There are seven members of the beta-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. Beta-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. Beta-1,4-Gal-T7 uses manganese to catalyze the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding beta-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterized by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits. Beta-1,4-galactosyltransferases (Beta-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a beta-1,4 linkage to an acceptor sugar.