C O N T E N T SSee AlsoDescriptionThe major sialoglycoprotein of the human erythrocyte membrane. It consists of at least two sialoglycopeptides and is composed of 60% carbohydrate including sialic acid and 40% protein. It is involved in a number of different biological activities including the binding of MN Blood Group, influenza viruses, kidney bean phytohemagglutinin, and wheat germ agglutinin. Glycophorin AGlycophorin A is a [Glycoprotiens? glycoprotein] that spans the plasma membrane (lipid bilayer) of human red blood cells. Each RBC has some 500,000 copies of the molecule embedded in its plasma membrane.
Two polymorphic versions of glycophorin A, which differ only at residues 1 and 5, occur in humans. These give rise to the MN blood groups:
Glycophorin A is the most important attachment site by which the parasite Plasmodium falciparum invades human red blood cells. Glycophorins C and DGlycophorin C and D encode the Gerbich (Ge) antigens which were described in 1960 and are named after one of the three original patients. There are four allelles, Ge-1 to Ge-4. Three types of Ge antigen negativity are known: Ge-1,-2,-3 (Leach phenotype), Ge-2,-3 and Ge-2,+3. A 3.4 kilobase pair deletion within the gene, which probably arose because of unequal crossing over between the two repeated domains, is responsible for the formation of the Ge-2,-3 genotype. The breakpoints of the deletion are located within introns 2 and 3 and results in the deletion of exon 3. Glycophorin C (GYPC; CD236/CD236R; glycoprotein beta; glycoconnectin; PAS-2') is an integral membrane protein of the erythrocyte and acts as the receptor for the Plasmodium falciparum protein PfEBP-2 (erythrocyte binding protein 2; baebl; EBA-140).[1] Other database IDs and linksNCBI genes Uniprot ID Genbank proteins Gene nomenclature database ID Genbank nucleic acids NCBI homologenes for homologs and orthologs NCBI dbSNP for single nucleotide polymorphisms HGMD ID - at the Human Gene Mutation Database
OMIM ID - at Online Mendelian Inheritance in Man Attribution
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