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Rhesus is commonly defined as a ‘factor’ that determines, in part, blood type, and whether neonates suffer from haemolytic disease of the newborn. These glycoprotein antigens derive from two genes, RHCE (ENSG00000188672) and RHD (ENSG00000187010) expressed on the surface of erythrocytes. On erythrocytes, RhAG associates with these antigens and functions as an ammonium transporter. RhBG and RhBG are non-erythroid related sequences associated with epithelia. Topological modelling suggests the presence of 12TM with cytoplasmic N- and C- termini. The majority of information on these transporters derives from orthologues in yeast, plants and bacteria. More recent evidence points to family members being permeable to carbon dioxide, leading to the term gas channels.
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
RhAG (SLC42A1) Show »
RhBG (SLC42A2) Show »
RhCG (SLC42A3) Show »
Further Reading Show »
Huang, CH; Ye, M. (2010) The Rh protein family: gene evolution, membrane biology, and disease association. Cell. Mol. Life Sci., 67 (8): 1203-18. [PMID:19953292]
Nakhoul, NL; Hamm, LL. (2004) Non-erythroid Rh glycoproteins: a putative new family of mammalian ammonium transporters. Pflugers Arch., 447 (5): 807-12. [PMID:12920597]
Weiner, ID; Verlander, JW. (2011) Role of NH3 and NH4+ transporters in renal acid-base transport. Am. J. Physiol. Renal Physiol., 300 (1): F11-23. [PMID:21048022]
References Show »
1. Endeward, V; Cartron, JP; Ripoche, P; Gros, G. (2008) RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane. FASEB J., 22 (1): 64-73. [PMID:17712059]
2. Ripoche, P; Bertrand, O; Gane, P; Birkenmeier, C; Colin, Y; Cartron, JP. (2004) Human Rhesus-associated glycoprotein mediates facilitated transport of NH(3) into red blood cells. Proc. Natl. Acad. Sci. U.S.A., 101 (49): 17222-7. [PMID:15572441]
3. Westhoff, CM; Ferreri-Jacobia, M; Mak, DO; Foskett, JK. (2002) Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter. J. Biol. Chem., 277 (15): 12499-502. [PMID:11861637]
4. Zidi-Yahiaoui, N; Callebaut, I; Genetet, S; Le Van Kim, C; Cartron, JP; Colin, Y; Ripoche, P; Mouro-Chanteloup, I. (2009) Functional analysis of human RhCG: comparison with E. coli ammonium transporter reveals similarities in the pore and differences in the vestibule. Am. J. Physiol., Cell Physiol., 297 (3): C537-47. [PMID:19553567]