RHCG

RHCG plays a critical role in ammonium handling and pH homeostasis in the kidney.{{cite journal | vauthors = Biver S, Belge H, Bourgeois S, Van Vooren P, Nowik M, Scohy S, Houillier P, Szpirer J, Szpirer C, Wagner CA, Devuyst O, Marini AM | title = A role for Rhesus factor Rhcg in renal ammonium excretion and male fertility | journal = Nature | volume = 456 | issue = 7220 | pages = 339–43 |date=November 2008 | pmid = 19020613 | doi = 10.1038/nature07518 | bibcode = 2008Natur.456..339B | s2cid = 205215412 }} The structure of the RHCG protein{{PDB|3hd6}}; {{cite journal | vauthors = Gruswitz F, Chaudhary S, Ho JD, Schlessinger A, Pezeshki B, Ho CM, Sali A, Westhoff CM, Stroud RM | title = Function of human Rh based on structure of RhCG at 2.1 A | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 107 | issue = 21 | pages = 9638–43 |date=May 2010 | pmid = 20457942 | pmc = 2906887 | doi = 10.1073/pnas.1003587107 | doi-access = free | bibcode = 2010PNAS..107.9638G }} indicates that it has a hydrophobic ammonia-conducting channel and shows that it shares a common fold with the ammonia transporters, thus making it an ammonia transporter.

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• {{cite journal | vauthors=Bakouh N, Benjelloun F, Cherif-Zahar B, Planelles G |title=The challenge of understanding ammonium homeostasis and the role of the Rh glycoproteins. |journal=Transfusion Clinique et Biologique |volume=13 |issue= 1–2 |pages= 139–46 |year= 2006 |pmid= 16564724 |doi= 10.1016/j.tracli.2006.02.008 }}
• {{cite journal |vauthors=Zidi-Yahiaoui N, Ripoche P, Le Van Kim C, etal |title=Ammonium transport properties of HEK293 cells expressing RhCG mutants: preliminary analysis of structure/function by site-directed mutagenesis. |journal=Transfusion Clinique et Biologique |volume=13 |issue= 1–2 |pages= 128–31 |year= 2006 |pmid= 16580862 |doi= 10.1016/j.tracli.2006.02.025 }}
• {{cite journal |vauthors=Ridgwell K, Spurr NK, Laguda B, etal |title=Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression. |journal=Biochem. J. |volume=287 |issue= 1|pages= 223–8 |year= 1992 |doi=10.1042/bj2870223 |pmid= 1417776 | pmc=1133147 }}
• {{cite journal |vauthors=Liu Z, Chen Y, Mo R, etal |title=Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25641–51 |year= 2000 |pmid= 10852913 |doi= 10.1074/jbc.M003353200 |doi-access= free }}
• {{cite journal |vauthors=Marini AM, Matassi G, Raynal V, etal |title=The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. |journal=Nat. Genet. |volume=26 |issue= 3 |pages= 341–4 |year= 2000 |pmid= 11062476 |doi= 10.1038/81656 |s2cid=21313219 }}
• {{cite journal |vauthors=Chen BS, Xu ZX, Xu X, etal |title=RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia. |journal=Eur. J. Cancer |volume=38 |issue= 14 |pages= 1927–36 |year= 2002 |pmid= 12204676 |doi=10.1016/S0959-8049(02)00190-9 }}
• {{cite journal |vauthors=Verlander JW, Miller RT, Frank AE, etal |title=Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=284 |issue= 2 |pages= F323–37 |year= 2003 |pmid= 12388412 |doi= 10.1152/ajprenal.00050.2002 }}
• {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
• {{cite journal |vauthors=Nicolas V, Le Van Kim C, Gane P, etal |title=Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation. |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 25526–33 |year= 2003 |pmid= 12719424 |doi= 10.1074/jbc.M302816200 |doi-access= free }}
• {{cite journal |vauthors=Hemker MB, Cheroutre G, van Zwieten R, etal |title=The Rh complex exports ammonium from human red blood cells. |journal=Br. J. Haematol. |volume=122 |issue= 2 |pages= 333–40 |year= 2003 |pmid= 12846905 |doi=10.1046/j.1365-2141.2003.04425.x |s2cid=3094213 |doi-access=free }}
• {{cite journal |vauthors=Bakouh N, Benjelloun F, Hulin P, etal |title=NH₃ is involved in the NH₄⁺ transport induced by the functional expression of the human Rh C glycoprotein. |journal=J. Biol. Chem. |volume=279 |issue= 16 |pages= 15975–83 |year= 2004 |pmid= 14761968 |doi= 10.1074/jbc.M308528200 |doi-access= free }}
• {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
• {{cite journal |vauthors=Zidi-Yahiaoui N, Mouro-Chanteloup I, D'Ambrosio AM, etal |title=Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells. |journal=Biochem. J. |volume=391 |issue= Pt 1 |pages= 33–40 |year= 2006 |pmid= 15929723 |doi= 10.1042/BJ20050657 | pmc=1237136 }}
• {{cite journal | vauthors=Huang CH, Peng J |title=Evolutionary conservation and diversification of Rh family genes and proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 43 |pages= 15512–7 |year= 2005 |pmid= 16227429 |doi= 10.1073/pnas.0507886102 | pmc=1266151 |bibcode=2005PNAS..10215512H |doi-access=free }}
• {{cite journal |vauthors=Marini AM, Boeckstaens M, Benjelloun F, etal |title=Structural involvement in substrate recognition of an essential aspartate residue conserved in Mep/Amt and Rh-type ammonium transporters. |journal=Curr. Genet. |volume=49 |issue= 6 |pages= 364–74 |year= 2006 |pmid= 16477434 |doi= 10.1007/s00294-006-0062-5 |s2cid=28636156 }}

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{{Membrane transport proteins}}

Category:Solute carrier family

{{membrane-protein-stub}}