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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 and fluoroethylamine.  19F-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:Q02161
Protein Name:Blood group Rh(D) polypeptide aka RhD
Length:417
Molecular Weight:45211.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate NH4+

Cross database links:

Genevestigator: Q02161
RefSeq: NP_001121163.1    NP_057208.2   
Entrez Gene ID: 6007   
Pfam: PF00909   
OMIM: 111680  gene
KEGG: hsa:6007   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0008519 F:ammonium transmembrane transporter activity
GO:0055085 P:transmembrane transport

References (14)

[1] “Molecular cloning and primary structure of the human blood group RhD polypeptide.”  le van Kim C.et.al.   1438298
[2] “Multiple Rh messenger RNA isoforms are produced by alternative splicing.”  le van Kim C.et.al.   1379850
[3] “Molecular cloning of RhD cDNA derived from a gene present in RhD-positive, but not RhD-negative individuals.”  Arce M.A.et.al.   8329718
[4] “Isolation of a new cDNA clone encoding an Rh polypeptide associated with the Rh blood group system.”  Kajii E.et.al.   7916743
[5] “Identification of a new RhD-specific mRNA from K562 cells.”  Westhoff C.M.et.al.   8180407
[6] “Identification of a partial internal deletion in the RH locus causing the human erythrocyte D-phenotype.”  Huang C.-H.et.al.   7606008
[7] “Rh(D) antigen expression and isolation of a new Rh(D) cDNA isoform in human erythroleukemic K562 cells.”  Suyama K.et.al.   8080999
[8] “The DNA sequence and biological annotation of human chromosome 1.”  Gregory S.G.et.al.   16710414
[9] “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
[10] “Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and -negative erythrocytes.”  Saboori A.M.et.al.   3131772
[11] “Determination of the N-terminal sequence of human red cell Rh(D) polypeptide and demonstration that the Rh(D), (c), and (E) antigens are carried by distinct polypeptide chains.”  Bloy C.et.al.   3135863
[12] “Regarding the size of Rh proteins.”  Suyama K.et.al.   1898705
[13] “Leu110Pro substitution in the RhD polypeptide is responsible for the DVII category blood group phenotype.”  Rouillac C.et.al.   7741145
[14] “The consensus coding sequences of human breast and colorectal cancers.”  Sjoeblom T.et.al.   16959974

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
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  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI 
61:	GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA 
121:	LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG 
181:	LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN 
241:	TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV 
301:	AGLISVGGAK YLPGCCNRVL GIPHSSIMGY NFSLLGLLGE IIYIVLLVLD TVGAGNGMIG 
361:	FQVLLSIGEL SLAIVIALMS GLLTGLLLNL KIWKAPHEAK YFDDQVFWKF PHLAVGF