RHAG

RHAG
Identifiers
Aliases	RHAG, CD241, RH2, RH50A, Rh50, Rh50GP, SLC42A1, OHS, OHST, Rh-associated glycoprotein, Rh associated glycoprotein, RHNR
External IDs	OMIM: 180297; MGI: 1202713; HomoloGene: 68045; GeneCards: RHAG; OMA:RHAG - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	49,636,839 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	41,151,645 bp
RNA expression pattern
	Top expressed in
	trabecular bone; ; bone marrow; ; bone marrow cells; ; testicle; ; blood; ; right auricle; ; monocyte; ; amniotic fluid; ; ventricle; ; cervix;
	Top expressed in
	fetal liver hematopoietic progenitor cell; ; tibiofemoral joint; ; human fetus; ; body of femur; ; spleen; ; bone marrow; ; blood; ; tail of embryo; ; yolk sac; ; genital tubercle;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	ankyrin binding; carbon dioxide transmembrane transporter activity; ammonium transmembrane transporter activity; leak channel activity;
Cellular component	integral component of membrane; plasma membrane; integral component of plasma membrane; membrane;
Biological process	multicellular organismal iron ion homeostasis; bicarbonate transport; organic cation transport; carbon dioxide transport; erythrocyte development; cellular ion homeostasis; carbon dioxide transmembrane transport; ammonium transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	6005
	19743
	ENSG00000112077
	ENSMUSG00000023926
	Q02094
	Q9QUT0
	NM_000324
	NM_011269
	NP_000315
	NP_035399
	Wikidata
View/Edit Human	View/Edit Mouse

Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene.^[5]^[6] RHAG has also recently been designated CD241 (cluster of differentiation 241). Mutations in the RHAG gene can cause stomatocytosis.^[7]

Function

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].^[6]

Interactions

RHAG has been shown to interact with ANK1.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000112077 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000023926 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Matassi G, Chérif-Zahar B, Raynal V, Rouger P, Cartron JP (Jan 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.
^ ^a ^b "Entrez Gene: RHAG Rh-associated glycoprotein".
^ Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL (Dec 2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". American Journal of Physiology. Cell Physiology. 301 (6): C1325-43. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667.
^ Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I (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". The Journal of Biological Chemistry. 278 (28): 25526–33. doi:10.1074/jbc.M302816200. PMID 12719424.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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. 13 (1–2): 139–46. doi:10.1016/j.tracli.2006.02.008. PMID 16564724.
Ripoche P, Goossens D, Devuyst O, Gane P, Colin Y, Verkman AS, Cartron JP (2006). "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis". Transfusion Clinique et Biologique. 13 (1–2): 117–22. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.
Ridgwell K, Spurr NK, Laguda B, MacGeoch C, Avent ND, Tanner MJ (Oct 1992). "Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression". The Biochemical Journal. 287. 287 (1): 223–8. doi:10.1042/bj2870223. PMC 1133147. PMID 1417776.
Avent ND, Ridgwell K, Mawby WJ, Tanner MJ, Anstee DJ, Kumpel B (Dec 1988). "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". The Biochemical Journal. 256 (3): 1043–6. doi:10.1042/bj2561043. PMC 1135522. PMID 3146980.
Cherif-Zahar B, Raynal V, Gane P, Mattei MG, Bailly P, Gibbs B, Colin Y, Cartron JP (Feb 1996). "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency". Nature Genetics. 12 (2): 168–73. doi:10.1038/ng0296-168. PMID 8563755. S2CID 1999844.
Huang CH (Jan 1998). "The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease". The Journal of Biological Chemistry. 273 (4): 2207–13. doi:10.1074/jbc.273.4.2207. PMID 9442063.
Hyland CA, Chérif-Zahar B, Cowley N, Raynal V, Parkes J, Saul A, Cartron JP (Feb 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. doi:10.1182/blood.V91.4.1458. PMID 9454778.
Iwamoto S, Omi T, Yamasaki M, Okuda H, Kawano M, Kajii E (Feb 1998). "Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression". Biochemical and Biophysical Research Communications. 243 (1): 233–40. doi:10.1006/bbrc.1997.8023. PMID 9473510.
Huang CH, Liu Z, Cheng G, Chen Y (Sep 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. doi:10.1182/blood.V92.5.1776. PMID 9716608.
Chérif-Zahar B, Matassi G, Raynal V, Gane P, Delaunay J, Arrizabalaga B, Cartron JP (Oct 1998). "Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene". Blood. 92 (7): 2535–40. doi:10.1182/blood.V92.7.2535. PMID 9746795.
Huang C, Cheng GJ, Reid ME, Chen Y (Jan 1999). "Rhmod syndrome: a family study of the translation-initiator mutation in the Rh50 glycoprotein gene". American Journal of Human Genetics. 64 (1): 108–17. doi:10.1086/302215. PMC 1377708. PMID 9915949.
Huang CH, Cheng G, Liu Z, Chen Y, Reid ME, Halverson G, Okubo Y (Sep 1999). "Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene". American Journal of Hematology. 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, Omi T, Okuda H, Kajii E (Sep 2000). "Cloning and characterization of erythroid-specific DNase I-hypersensitive site in human rhesus-associated glycoprotein gene". The Journal of Biological Chemistry. 275 (35): 27324–31. doi:10.1074/jbc.M003297200. PMID 10862620.
Marini AM, Matassi G, Raynal V, André B, Cartron JP, Chérif-Zahar B (Nov 2000). "The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast". Nature Genetics. 26 (3): 341–4. doi:10.1038/81656. PMID 11062476. S2CID 21313219.
Westhoff CM, Ferreri-Jacobia M, Mak DO, Foskett JK (Apr 2002). "Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter". The Journal of Biological Chemistry. 277 (15): 12499–502. doi:10.1074/jbc.C200060200. PMID 11861637.
Mouro-Chanteloup I, D'Ambrosio AM, Gane P, Le Van Kim C, Raynal V, Dhermy D, Cartron JP, Colin Y (Aug 2002). "Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein". Blood. 100 (3): 1038–47. doi:10.1182/blood.V100.3.1038. PMID 12130520.
Chen BS, Xu ZX, Xu X, Cai Y, Han YL, Wang J, Xia SH, Hu H, Wei F, Wu M, Wang MR (Sep 2002). "RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia". European Journal of Cancer. 38 (14): 1927–36. doi:10.1016/S0959-8049(02)00190-9. PMID 12204676.
Dahl KN, Westhoff CM, Discher DE (Feb 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.

External links

RHCE+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
RhAG blood group system in the BGMUT blood group antigen gene mutation database

This membrane protein–related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000112077 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000023926 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9479501-5] Matassi G, Chérif-Zahar B, Raynal V, Rouger P, Cartron JP (Jan 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.

[entrez-6] "Entrez Gene: RHAG Rh-associated glycoprotein".

[7] Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL (Dec 2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". American Journal of Physiology. Cell Physiology. 301 (6): C1325-43. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667.

[pmid12719424-8] Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I (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". The Journal of Biological Chemistry. 278 (28): 25526–33. doi:10.1074/jbc.M302816200. PMID 12719424.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

v t e Blood transfusion and transfusion medicine
Blood products	Whole blood Platelets Platelet transfusion Red blood cells Plasma Fresh frozen plasma PF24 Cryoprecipitate Cryosupernatant White blood cells Granulocyte transfusion Blood substitutes
General concepts	Blood bank Blood donation Blood management International Society of Blood Transfusion ISBT 128
Methods	Apheresis (plasmapheresis, plateletpheresis, leukapheresis) Exchange transfusion Intraoperative blood salvage
Tests	Blood compatibility testing Cross-matching Coombs test Kleihauer–Betke test Antibody elution Monocyte monolayer assay
Transfusion reactions and adverse effects	Transfusion hemosiderosis Transfusion related acute lung injury Transfusion associated circulatory overload Transfusion-associated graft versus host disease Febrile non-hemolytic transfusion reaction Hemolytic reaction acute delayed Serum sickness Transfusion transmitted infection
Blood group systems	Blood types ABO Secretor status Augustine CD59 Chido-Rodgers Colton Cromer Diego Dombrock Duffy Er FORS Gerbich GIL GLOB Hh Ii Indian JR JMH KANNO Kell (Xk) Kidd Knops Lan Lewis Lutheran LW MNS OK P1PK Raph Rh and RHAG Scianna Sid T-Tn Vel Xg Yt Other

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

RHAG

Function

Interactions

See also

References

Further reading

External links