A family of sialylated transmembrane glycoproteins of the human erythrocyte. Glycophorin A is an integral membrane protein (131 aa) that is highly O-glycosylated and is rich in terminal sialic acid. The peptide chain carries the MN blood group antigens at its N-terminus. Glycophorin B carries Ss and U antigens. Glycophorin C (CD236/CD236R, glycoprotein β, glycoconnectin, 128 aa) constitutes ~4% of the erythrocyte glycoprotein. It is the receptor for the Plasmodium falciparum protein PfEBP-2 (erythrocyte binding protein 2, baebl, EBA-140). Glycophorin C has a role in the maintenance of red cell shape, probably through an interaction with band 3. Glycophorin D is a shorter form of glycophorin C and together the two encode the Gerbich (Ge) antigens. Glycophorin E, like glycophorin B, is derived from ancestral glycophorin A by gene duplication.