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Ammonium transporter Rh type A (Erythrocyte membrane glycoprotein Rh50) (Erythrocyte plasma membrane 50 kDa glycoprotein) (Rh50A) (Rhesus blood group family type A glycoprotein) (Rh family type A glycoprotein) (Rh type A glycoprotein) (Rhesus blood group-associated ammonia channel) (Rhesus blood group-associated glycoprotein) (CD antigen CD241)

 RHAG_HUMAN              Reviewed;         409 AA.
Q02094; B2R8T8; O43514; O43515; Q7L8L3; Q9H454;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
22-NOV-2017, entry version 154.
RecName: Full=Ammonium transporter Rh type A;
AltName: Full=Erythrocyte membrane glycoprotein Rh50;
AltName: Full=Erythrocyte plasma membrane 50 kDa glycoprotein;
Short=Rh50A;
AltName: Full=Rhesus blood group family type A glycoprotein;
Short=Rh family type A glycoprotein;
Short=Rh type A glycoprotein;
AltName: Full=Rhesus blood group-associated ammonia channel;
AltName: Full=Rhesus blood group-associated glycoprotein;
AltName: CD_antigen=CD241;
Name=RHAG; Synonyms=RH50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-242.
TISSUE=Bone marrow, and Liver;
PubMed=1417776; DOI=10.1042/bj2870223;
Ridgwell K., Spurr N.K., Laguda B., Macgeoch C., Avent N.D.,
Tanner M.J.A.;
"Isolation of cDNA clones for a 50 kDa glycoprotein of the human
erythrocyte membrane associated with Rh (rhesus) blood-group antigen
expression.";
Biochem. J. 287:223-228(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
PubMed=9442063; DOI=10.1074/jbc.273.4.2207;
Huang C.-H.;
"The human Rh50 glycoprotein gene. Structural organization and
associated splicing defect resulting in Rh(null) disease.";
J. Biol. Chem. 273:2207-2213(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-270.
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-52, AND TISSUE SPECIFICITY.
PubMed=9473510; DOI=10.1006/bbrc.1997.8023;
Iwamoto S., Omi T., Yamasaki M., Okuda H., Kawano M., Kajii E.;
"Identification of 5' flanking sequence of RH50 gene and the core
region for erythroid-specific expression.";
Biochem. Biophys. Res. Commun. 243:233-240(1998).
[7]
PROTEIN SEQUENCE OF 1-39.
PubMed=3146980; DOI=10.1042/bj2561043;
Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J.,
Kumpel B.;
"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. 256:1043-1046(1988).
[8]
FUNCTION.
PubMed=11062476; DOI=10.1038/81656;
Marini A.-M., Matassi G., Raynal V., Andre B., Cartron J.-P.,
Cherif-Zahar B.;
"The human Rhesus-associated RhAG protein and a kidney homologue
promote ammonium transport in yeast.";
Nat. Genet. 26:341-344(2000).
[9]
FUNCTION.
PubMed=11861637; DOI=10.1074/jbc.C200060200;
Westhoff C.M., Ferreri-Jacobia M., Mak D.-O.D., Foskett J.K.;
"Identification of the erythrocyte Rh blood group glycoprotein as a
mammalian ammonium transporter.";
J. Biol. Chem. 277:12499-12502(2002).
[10]
CHARACTERIZATION.
PubMed=14966114; DOI=10.1074/jbc.M311853200;
Westhoff C.M., Siegel D.L., Burd C.G., Foskett J.K.;
"Mechanism of genetic complementation of ammonium transport in yeast
by human erythrocyte Rh-associated glycoprotein.";
J. Biol. Chem. 279:17443-17448(2004).
[11]
VARIANT RHN ASN-79.
PubMed=8563755; DOI=10.1038/ng0296-168;
Cherif-Zahar B., Raynal V., Gane P., Mattei M.-G., Bailly P.,
Gibbs B., Colin Y., Cartron J.-P.;
"Candidate gene acting as a suppressor of the RH locus in most cases
of Rh-deficiency.";
Nat. Genet. 12:168-173(1996).
[12]
VARIANT RHN GLU-279.
PubMed=9454778;
Hyland C.A., Cherif-Zahar B., Cowley N., Raynal V., Parkes J.,
Saul A., Cartron J.-P.;
"A novel single missense mutation identified along the RH50 gene in a
composite heterozygous Rhnull blood donor of the regulator type.";
Blood 91:1458-1463(1998).
[13]
VARIANT RHN GLU-279.
PubMed=9716608;
Huang C.-H., Liu Z., Cheng G., Chen Y.;
"Rh50 glycoprotein gene and rhnull disease: a silent splice donor is
trans to a Gly279-->Glu missense mutation in the conserved
transmembrane segment.";
Blood 92:1776-1784(1998).
[14]
VARIANTS RHN ARG-280 AND VAL-380, AND VARIANT ILE-270.
PubMed=10467273;
DOI=10.1002/(SICI)1096-8652(199909)62:1<25::AID-AJH5>3.0.CO;2-K;
Huang C.-H., Cheng G., Liu Z., Chen Y., Reid M.E., Halverson G.,
Okubo Y.;
"Molecular basis for Rh(null) syndrome: identification of three new
missense mutations in the Rh50 glycoprotein gene.";
Am. J. Hematol. 62:25-32(1999).
[15]
INVOLVEMENT IN OHST, VARIANTS OHST ARG-61 AND SER-65, CHARACTERIZATION
OF VARIANTS OHST ARG-61 AND SER-65, FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=18931342; DOI=10.1182/blood-2008-07-171140;
Bruce L.J., Guizouarn H., Burton N.M., Gabillat N., Poole J.,
Flatt J.F., Brady R.L., Borgese F., Delaunay J., Stewart G.W.;
"The monovalent cation leak in overhydrated stomatocytic red blood
cells results from amino acid substitutions in the Rh-associated
glycoprotein.";
Blood 113:1350-1357(2009).
[16]
VARIANTS GLU-106; GLN-164 AND LEU-227, AND FUNCTION.
PubMed=19744193; DOI=10.1111/j.1423-0410.2009.01243.x;
Tilley L., Green C., Poole J., Gaskell A., Ridgwell K., Burton N.M.,
Uchikawa M., Tsuneyama H., Ogasawara K., Akkoek C.A., Daniels G.;
"A new blood group system, RHAG: three antigens resulting from amino
acid substitutions in the Rh-associated glycoprotein.";
Vox Sang. 98:151-159(2010).
[17]
VARIANT OHST SER-65, CHARACTERIZATION OF VARIANT OHST SER-65, AND
FUNCTION.
PubMed=21849667; DOI=10.1152/ajpcell.00054.2011;
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.;
"Loss-of-function and gain-of-function phenotypes of stomatocytosis
mutant RhAG F65S.";
Am. J. Physiol. 301:C1325-C1343(2011).
[18]
CHARACTERIZATION OF VARIANT OHST SER-65, FUNCTION, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=22012326; DOI=10.1152/ajpcell.00092.2011;
Genetet S., Ripoche P., Picot J., Bigot S., Delaunay J.,
Armari-Alla C., Colin Y., Mouro-Chanteloup I.;
"Human RhAG ammonia channel is impaired by the Phe65Ser mutation in
overhydrated stomatocytic red cells.";
Am. J. Physiol. 302:C419-C428(2012).
[19]
VARIANT ILE-270.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Associated with rhesus blood group antigen expression
(PubMed:19744193). May be part of an oligomeric complex which is
likely to have a transport or channel function in the erythrocyte
membrane (PubMed:11062476, PubMed:11861637). Involved in ammonia
transport across the erythrocyte membrane (PubMed:21849667,
PubMed:22012326). Seems to act in monovalent cation transport
(PubMed:18931342, PubMed:21849667). {ECO:0000269|PubMed:11062476,
ECO:0000269|PubMed:11861637, ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:19744193, ECO:0000269|PubMed:21849667,
ECO:0000269|PubMed:22012326}.
-!- SUBUNIT: Heterotetramer.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:22012326}; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q02094-1; Sequence=Displayed;
Name=2;
IsoId=Q02094-2; Sequence=VSP_047629, VSP_047630;
-!- TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:22012326, ECO:0000269|PubMed:9473510}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:22012326}.
-!- DISEASE: Regulator type Rh-null hemolytic anemia (RHN)
[MIM:268150]: Form of chronic hemolytic anemia in which the red
blood cells have a stomatocytosis and spherocytosis morphology, an
increased osmotic fragility, an altered ion transport system, and
abnormal membrane phospholipid organization.
{ECO:0000269|PubMed:10467273, ECO:0000269|PubMed:8563755,
ECO:0000269|PubMed:9454778, ECO:0000269|PubMed:9716608}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Overhydrated hereditary stomatocytosis (OHST)
[MIM:185000]: An autosomal dominant disorder of red cell membrane
permeability to monovalent cations, characterized by macrocytic
hemolytic anemia of fluctuating severity, circulating erythrocytes
with slit-like lucencies (stomata) evident on fixed, stained
peripheral blood smears. OHST red cells exhibit cation leak,
resulting in elevated cell sodium content with reduced potassium
content. The disease is marked by splenomegaly or
hepatosplenomegaly, cholelithiasis and a strong tendency for iron
overload. {ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:21849667, ECO:0000269|PubMed:22012326}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49)
family. Rh subfamily. {ECO:0000305}.
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EMBL; X64594; CAA45883.1; -; mRNA.
EMBL; AF031548; AAC04247.1; -; mRNA.
EMBL; AF031549; AAC04248.1; -; mRNA.
EMBL; AF237387; AAF78209.1; -; Genomic_DNA.
EMBL; AF237382; AAF78209.1; JOINED; Genomic_DNA.
EMBL; AF237383; AAF78209.1; JOINED; Genomic_DNA.
EMBL; AF237384; AAF78209.1; JOINED; Genomic_DNA.
EMBL; AF237385; AAF78209.1; JOINED; Genomic_DNA.
EMBL; AF237386; AAF78209.1; JOINED; Genomic_DNA.
EMBL; AK313505; BAG36285.1; -; mRNA.
EMBL; AL121950; CAC10519.2; -; Genomic_DNA.
EMBL; AL590244; CAC10519.2; JOINED; Genomic_DNA.
EMBL; AL590244; CAI13085.1; -; Genomic_DNA.
EMBL; AL121950; CAI13085.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX04337.1; -; Genomic_DNA.
EMBL; CH471081; EAX04338.1; -; Genomic_DNA.
CCDS; CCDS4927.1; -. [Q02094-1]
PIR; S29124; S29124.
RefSeq; NP_000315.2; NM_000324.2. [Q02094-1]
UniGene; Hs.120950; -.
ProteinModelPortal; Q02094; -.
BioGrid; 111937; 1.
IntAct; Q02094; 1.
STRING; 9606.ENSP00000360217; -.
TCDB; 1.A.11.4.3; the ammonium transporter channel (amt) family.
iPTMnet; Q02094; -.
PhosphoSitePlus; Q02094; -.
BioMuta; RHAG; -.
DMDM; 218511807; -.
PaxDb; Q02094; -.
PeptideAtlas; Q02094; -.
PRIDE; Q02094; -.
DNASU; 6005; -.
Ensembl; ENST00000371175; ENSP00000360217; ENSG00000112077. [Q02094-1]
GeneID; 6005; -.
KEGG; hsa:6005; -.
UCSC; uc003ozk.5; human. [Q02094-1]
CTD; 6005; -.
DisGeNET; 6005; -.
EuPathDB; HostDB:ENSG00000112077.15; -.
GeneCards; RHAG; -.
H-InvDB; HIX0005947; -.
HGNC; HGNC:10006; RHAG.
HPA; HPA055331; -.
MalaCards; RHAG; -.
MIM; 180297; gene.
MIM; 185000; phenotype.
MIM; 268150; phenotype.
neXtProt; NX_Q02094; -.
OpenTargets; ENSG00000112077; -.
Orphanet; 3203; Overhydrated hereditary stomatocytosis.
Orphanet; 71275; Rh deficiency syndrome.
PharmGKB; PA34381; -.
eggNOG; KOG3796; Eukaryota.
eggNOG; ENOG410XTF8; LUCA.
GeneTree; ENSGT00390000005787; -.
HOGENOM; HOG000007656; -.
HOVERGEN; HBG004374; -.
InParanoid; Q02094; -.
KO; K06580; -.
OMA; GTCADMA; -.
PhylomeDB; Q02094; -.
TreeFam; TF314450; -.
Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-HSA-444411; Rhesus glycoproteins mediate ammonium transport.
Reactome; R-HSA-5619042; Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN).
ChiTaRS; RHAG; human.
GeneWiki; RHAG; -.
GenomeRNAi; 6005; -.
PRO; PR:Q02094; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112077; -.
CleanEx; HS_RHAG; -.
ExpressionAtlas; Q02094; baseline and differential.
Genevisible; Q02094; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0030506; F:ankyrin binding; IPI:UniProtKB.
GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; TAS:Reactome.
GO; GO:0022840; F:leak channel activity; IDA:UniProtKB.
GO; GO:0072488; P:ammonium transmembrane transport; IMP:UniProtKB.
GO; GO:0015696; P:ammonium transport; IDA:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
GO; GO:0006873; P:cellular ion homeostasis; IDA:UniProtKB.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0015672; P:monovalent inorganic cation transport; IDA:UniProtKB.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
InterPro; IPR002229; RhesusRHD.
Pfam; PF00909; Ammonium_transp; 1.
PRINTS; PR00342; RHESUSRHD.
SUPFAM; SSF111352; SSF111352; 1.
1: Evidence at protein level;
Alternative splicing; Ammonia transport; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Hereditary hemolytic anemia; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 409 Ammonium transporter Rh type A.
/FTId=PRO_0000168199.
TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.
TRANSMEM 3 23 Helical. {ECO:0000255}.
TOPO_DOM 24 51 Extracellular. {ECO:0000255}.
TRANSMEM 52 72 Helical. {ECO:0000255}.
TOPO_DOM 73 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TOPO_DOM 101 113 Extracellular. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 143 163 Helical. {ECO:0000255}.
TOPO_DOM 164 167 Extracellular. {ECO:0000255}.
TRANSMEM 168 188 Helical. {ECO:0000255}.
TOPO_DOM 189 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 239 Extracellular. {ECO:0000255}.
TRANSMEM 240 260 Helical. {ECO:0000255}.
TOPO_DOM 261 268 Cytoplasmic. {ECO:0000255}.
TRANSMEM 269 291 Helical. {ECO:0000255}.
TOPO_DOM 292 295 Extracellular. {ECO:0000255}.
TRANSMEM 296 318 Helical. {ECO:0000255}.
TOPO_DOM 319 332 Cytoplasmic. {ECO:0000255}.
TRANSMEM 333 353 Helical. {ECO:0000255}.
TOPO_DOM 354 362 Extracellular. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
TOPO_DOM 384 409 Cytoplasmic. {ECO:0000255}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 316 351 PLFTTKLRIHDTCGVHNLHGLPGVVGGLAGIVAVAM -> V
YGHAGSCTGFLYRNSSCWRSDDRFNSKVASLGTAI (in
isoform 2). {ECO:0000303|PubMed:9442063}.
/FTId=VSP_047629.
VAR_SEQ 352 409 Missing (in isoform 2).
{ECO:0000303|PubMed:9442063}.
/FTId=VSP_047630.
VARIANT 61 61 I -> R (in OHST; strongly enhances
monovalent cation leak;
dbSNP:rs863225469).
{ECO:0000269|PubMed:18931342}.
/FTId=VAR_076283.
VARIANT 65 65 F -> S (in OHST; enhances monovalent
cation leak; decreases ammonium fluxes;
highly decreases STOM expression;
decreases membrane expression; no effect
on water permeability;
dbSNP:rs863225468).
{ECO:0000269|PubMed:18931342,
ECO:0000269|PubMed:21849667,
ECO:0000269|PubMed:22012326}.
/FTId=VAR_076284.
VARIANT 79 79 S -> N (in RHN; dbSNP:rs121918586).
{ECO:0000269|PubMed:8563755}.
/FTId=VAR_006921.
VARIANT 106 106 Q -> E (polymorphism; in Duclos or RHAG1
antigen (030001)).
{ECO:0000269|PubMed:19744193}.
/FTId=VAR_076285.
VARIANT 164 164 K -> Q (polymorphism; in DSLK or RHAG3
antigen (030003); dbSNP:rs144305805).
{ECO:0000269|PubMed:19744193}.
/FTId=VAR_076286.
VARIANT 227 227 S -> L (polymorphism; in Ol(a) or RHAG2
antigen (030002)).
{ECO:0000269|PubMed:19744193}.
/FTId=VAR_076287.
VARIANT 242 242 N -> D (in dbSNP:rs1058063).
{ECO:0000269|PubMed:1417776}.
/FTId=VAR_047999.
VARIANT 270 270 V -> I (in dbSNP:rs16879498).
{ECO:0000269|PubMed:10467273,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_015855.
VARIANT 279 279 G -> E (in RHN; dbSNP:rs28933991).
{ECO:0000269|PubMed:9454778,
ECO:0000269|PubMed:9716608}.
/FTId=VAR_015856.
VARIANT 280 280 G -> R (in RHN; dbSNP:rs104893987).
{ECO:0000269|PubMed:10467273}.
/FTId=VAR_015857.
VARIANT 380 380 G -> V (in RHN; dbSNP:rs121918589).
{ECO:0000269|PubMed:10467273}.
/FTId=VAR_015858.
CONFLICT 2 2 R -> C (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 37 37 N -> P (in Ref. 7; AA sequence).
{ECO:0000305}.
SEQUENCE 409 AA; 44198 MW; F6F024399CC0C88D CRC64;
MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL YPLFQDVHVM
IFVGFGFLMT FLKKYGFSSV GINLLVAALG LQWGTIVQGI LQSQGQKFNI GIKNMINADF
SAATVLISFG AVLGKTSPTQ MLIMTILEIV FFAHNEYLVS EIFKASDIGA SMTIHAFGAY
FGLAVAGILY RSGLRKGHEN EESAYYSDLF AMIGTLFLWM FWPSFNSAIA EPGDKQCRAI
VNTYFSLAAC VLTAFAFSSL VEHRGKLNMV HIQNATLAGG VAVGTCADMA IHPFGSMIIG
SIAGMVSVLG YKFLTPLFTT KLRIHDTCGV HNLHGLPGVV GGLAGIVAVA MGASNTSMAM
QAAALGSSIG TAVVGGLMTG LILKLPLWGQ PSDQNCYDDS VYWKVPKTR


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