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1.A.11.4.3
Rhesus (Rh) complex (tetramer: RhAG2, RhCE1, RhD1) of 409 aas and 12 TMSs. Exports ammonia from human red blood cells (Conroy et al., 2005). RhAG is also called RH50.  RhAG variants (I61R, F65S), associated with overhydrated hereditary stomatocytosis (OHSt), a disease affecting erythrocytes, are alterred for bidirectional ammonium transport (Deschuyteneer et al. 2013).  The system transports ammonia, methylammonia, ethylammonia, fluoroethylamine and CO2 Michenkova et al. 202119F-fluoroethylamine has been used to study rapid transport as its NMR spectra are different inside and outside of human red blook cells (Szekely et al. 2006).

Accession Number:Q02094
Protein Name:Rhesus blood group-associated glycoprotein aka RhAG
Length:409
Molecular Weight:44198.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate ammonium, methylamine, ethylamine, carbon dioxide

Cross database links:

RefSeq: NP_000315.2   
Entrez Gene ID: 6005   
Pfam: PF00909   
OMIM: 180297  gene
268150  phenotype
KEGG: hsa:6005   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0051739 F:ammonia transmembrane transporter activity
GO:0008519 F:ammonium transmembrane transporter activity
GO:0030506 F:ankyrin binding
GO:0015696 P:ammonium transport
GO:0015670 P:carbon dioxide transport
GO:0006873 P:cellular ion homeostasis
GO:0055085 P:transmembrane transport

References (13)

[1] “Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression.”  Ridgwell K.et.al.   1417776
[2] “The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease.”  Huang C.-H.et.al.   9442063
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[5] “Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression.”  Iwamoto S.et.al.   9473510
[6] “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.”  Avent N.D.et.al.   3146980
[7] “The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast.”  Marini A.-M.et.al.   11062476
[8] “Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter.”  Westhoff C.M.et.al.   11861637
[9] “Mechanism of genetic complementation of ammonium transport in yeast by human erythrocyte Rh-associated glycoprotein.”  Westhoff C.M.et.al.   14966114
[10] “Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency.”  Cherif-Zahar B.et.al.   8563755
[11] “A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type.”  Hyland C.A.et.al.   9454778
[12] “Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment.”  Huang C.-H.et.al.   9716608
[13] “Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene.”  Huang C.-H.et.al.   10467273

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL YPLFQDVHVM 
61:	IFVGFGFLMT FLKKYGFSSV GINLLVAALG LQWGTIVQGI LQSQGQKFNI GIKNMINADF 
121:	SAATVLISFG AVLGKTSPTQ MLIMTILEIV FFAHNEYLVS EIFKASDIGA SMTIHAFGAY 
181:	FGLAVAGILY RSGLRKGHEN EESAYYSDLF AMIGTLFLWM FWPSFNSAIA EPGDKQCRAI 
241:	VNTYFSLAAC VLTAFAFSSL VEHRGKLNMV HIQNATLAGG VAVGTCADMA IHPFGSMIIG 
301:	SIAGMVSVLG YKFLTPLFTT KLRIHDTCGV HNLHGLPGVV GGLAGIVAVA MGASNTSMAM 
361:	QAAALGSSIG TAVVGGLMTG LILKLPLWGQ PSDQNCYDDS VYWKVPKTR