RHAG
| Rh-associated glycoprotein | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | RHAG ; CD241; RH2; RH50A; Rh50; Rh50GP; SLC42A1 | ||||||||||||
| External IDs | OMIM: 180297 MGI: 1202713 HomoloGene: 68045 IUPHAR: 1198 GeneCards: RHAG Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 6005 | 19743 | |||||||||||
| Ensembl | ENSG00000112077 | ENSMUSG00000023926 | |||||||||||
| UniProt | Q02094 | Q9QUT0 | |||||||||||
| RefSeq (mRNA) | NM_000324 | NM_011269 | |||||||||||
| RefSeq (protein) | NP_000315 | NP_035399 | |||||||||||
| Location (UCSC) | Chr 6: 49.57 – 49.6 Mb | Chr 17: 40.81 – 40.84 Mb | |||||||||||
| PubMed search | |||||||||||||
Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene.[1][2] RHAG has also recently been designated CD241 (cluster of differentiation 241). Mutations in the RHAG gene can cause stomatocytosis.[3]
The Rh blood group antigens (MIM 111700) are associated with human erythrocyte membrane proteins of approximately 30 kD, the so-called Rh30 polypeptides. Heterogeneously glycosylated membrane proteins of 50 and 45 kD, the Rh50 glycoproteins, are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and polyclonal antibodies. The Rh antigens appear to exist as a multisubunit complex of CD47 (MIM 601028), LW (MIM 111250), glycophorin B (MIM 111740), and play a critical role in the Rh50 glycoprotein [supplied by OMIM].[2]
Interactions
RHAG has been shown to interact with ANK1.[4]
See also
References
- ↑ Matassi G, Cherif-Zahar B, Raynal V, Rouger P, Cartron JP (Apr 1998). "Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family". Genomics 47 (2): 286–93. doi:10.1006/geno.1997.5112. PMID 9479501.
- ↑ 2.0 2.1 "Entrez Gene: RHAG Rh-associated glycoprotein".
- ↑ Stewart, A. K.; Shmukler, B. E.; Vandorpe, D. H.; Rivera, A.; Heneghan, J. F.; Li, X.; Hsu, A.; Karpatkin, M.; O'Neill, A. F.; Bauer, D. E.; Heeney, M. M.; John, K.; Kuypers, F. A.; Gallagher, P. G.; Lux, S. E.; Brugnara, C.; Westhoff, C. M.; Alper, S. L. (2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". AJP: Cell Physiology 301 (6): C1325–C1343. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667.
- ↑ Nicolas, Virginie; Le Van Kim Caroline, Gane Pierre, Birkenmeier Connie, Cartron Jean-Pierre, Colin Yves, Mouro-Chanteloup Isabelle (Jul 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". J. Biol. Chem. (United States) 278 (28): 25526–33. doi:10.1074/jbc.M302816200. ISSN 0021-9258. PMID 12719424.
Further reading
- Bakouh N, Benjelloun F, Cherif-Zahar B, Planelles G (2006). "The challenge of understanding ammonium homeostasis and the role of the Rh glycoproteins". Transfusion clinique et biologique : journal de la Société française de transfusion sanguine 13 (1-2): 139–46. doi:10.1016/j.tracli.2006.02.008. PMID 16564724.
- Ripoche P, Goossens D, Devuyst O et al. (2006). "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis". Transfusion clinique et biologique : journal de la Société française de transfusion sanguine 13 (1-2): 117–22. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.
- Ridgwell K, Spurr NK, Laguda B et al. (1992). "Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression". Biochem. J. 287. ( Pt 1): 223–8. PMC 1133147. PMID 1417776.
- Avent ND, Ridgwell K, Mawby WJ et al. (1989). "Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane". Biochem. J. 256 (3): 1043–6. PMC 1135522. PMID 3146980.
- Cherif-Zahar B, Raynal V, Gane P et al. (1996). "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency". Nat. Genet. 12 (2): 168–73. doi:10.1038/ng0296-168. PMID 8563755.
- Huang CH (1998). "The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease". J. Biol. Chem. 273 (4): 2207–13. doi:10.1074/jbc.273.4.2207. PMID 9442063.
- Hyland CA, Chérif-Zahar B, Cowley N et al. (1998). "A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type". Blood 91 (4): 1458–63. PMID 9454778.
- Iwamoto S, Omi T, Yamasaki M et al. (1998). "Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression". Biochem. Biophys. Res. Commun. 243 (1): 233–40. doi:10.1006/bbrc.1997.8023. PMID 9473510.
- Huang CH, Liu Z, Cheng G, Chen Y (1998). "Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment". Blood 92 (5): 1776–84. PMID 9716608.
- Chérif-Zahar B, Matassi G, Raynal V et al. (1998). "Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene". Blood 92 (7): 2535–40. PMID 9746795.
- Huang C, Cheng GJ, Reid ME, Chen Y (1999). "Rhmod syndrome: a family study of the translation-initiator mutation in the Rh50 glycoprotein gene". Am. J. Hum. Genet. 64 (1): 108–17. doi:10.1086/302215. PMC 1377708. PMID 9915949.
- Huang CH, Cheng G, Liu Z et al. (1999). "Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene". Am. J. Hematol. 62 (1): 25–32. doi:10.1002/(SICI)1096-8652(199909)62:1<25::AID-AJH5>3.0.CO;2-K. PMID 10467273.
- Iwamoto S, Suganuma H, Kamesaki T et al. (2000). "Cloning and characterization of erythroid-specific DNase I-hypersensitive site in human rhesus-associated glycoprotein gene". J. Biol. Chem. 275 (35): 27324–31. doi:10.1074/jbc.M003297200. PMID 10862620.
- Marini AM, Matassi G, Raynal V et al. (2000). "The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast". Nat. Genet. 26 (3): 341–4. doi:10.1038/81656. PMID 11062476.
- 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. doi:10.1074/jbc.C200060200. PMID 11861637.
- Mouro-Chanteloup I, D'Ambrosio AM, Gane P et al. (2002). "Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein". Blood 100 (3): 1038–47. PMID 12130520.
- Chen BS, Xu ZX, Xu X et al. (2002). "RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia". Eur. J. Cancer 38 (14): 1927–36. doi:10.1016/S0959-8049(02)00190-9. PMID 12204676.
- Dahl KN, Westhoff CM, Discher DE (2003). "Fractional attachment of CD47 (IAP) to the erythrocyte cytoskeleton and visual colocalization with Rh protein complexes". Blood 101 (3): 1194–9. doi:10.1182/blood-2002-04-1187. PMID 12393442.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
External links
- RHCE protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- RhAG blood group system in the BGMUT blood group antigen gene mutation database
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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