GYPC encodes glycophorins C and D, minor sialoglycoproteins on human erythrocyte membranes that carry Gerbich blood group antigens 1. The gene, located on chromosome 2-q21, produces two protein products through alternative translation initiation 1, with glycophorin D representing a truncated N-terminal form of glycophorin C 2. Functionally, GYPC plays a critical role in red blood cell membrane stability through interactions with protein 4.1R and p55 3. The extracellular domain serves dual roles: expressing Gerbich blood group determinants and acting as a receptor for Plasmodium falciparum merozoites during malarial infection 4. GYPC exhibits evidence of recent positive selection in humans, likely driven by malaria evasion pressure, representing a unique evolutionary mechanism involving co-option of untranslated region sequences 5. Clinically, GYPC variants cause rare blood phenotypes (Yus, Gerbich, and Leach types) through exon deletions 3, and anti-Gerbich antibodies have triggered hemolytic transfusion reactions and hemolytic disease of the fetus and newborn 4. Additionally, high GYPC expression correlates with unfavorable prognosis in childhood acute lymphoblastic leukemia and low expression predicts poor outcomes in FLT3-ITD-negative acute myeloid leukemia 67.