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A glycophorin is a sialoglycoprotein of the membrane of a red blood cell. It is a membrane-spanning protein and carries sugar molecules. It is heavily glycosylated (60%). Glycophorins are rich in sialic acid, which gives the red blood cells a very hydrophilic-charged coat. This enables them to circulate without adhering to other cells or vessel walls.
| Glycophorin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Dimeric transmembrane domain of human glycophorin A (20 NMR-determined structures) | |||||||||
| Identifiers | |||||||||
| Symbol | GYPA | ||||||||
| Pfam | PF01102 | ||||||||
| InterPro | IPR001195 | ||||||||
| PROSITE | PDOC00281 | ||||||||
| SCOP2 | 1afo / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 25 | ||||||||
| OPM protein | 5eh4 | ||||||||
| Membranome | 156 | ||||||||
| |||||||||
A particular mutation in Glycophorins is thought to produce a 40% reduction in risk of severe malaria. [1]
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After separation of red cell membranes by SDS-polyacrylamide gel electrophoresis and staining with periodic acid-Schiff staining (PAS), four glycophorins have been identified. These have been named glycophorin A, B, C, and D in order of the quantity present in the membrane, glycophorin A being the most and glycophorin D the least common. A fifth (glycophorin E) has been identified within the human genome but cannot easily be detected on routine gel staining. In total, the glycophorins constitute ~2% of the total erythrocyte membrane protein mass. These proteins are also known under different nomenclatures but they are probably best known as the glycophorins.
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The following four human genes encode glycophorin proteins:
Glycophorin D is now known to be a variant of Glycophorin C.
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