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1.A.11.4.1
Rhesus (Rh) type C glycoprotein NH3/NH4+ transporter, RhCG (also called tumor-related protein DRC2) (Bakouh et al., 2004; Worrell et al., 2007). Zidi-Yahiaoui et al. (2009) have described characteristics of the pore/vestibule. The structure is known to 2.1 Å resolution (Gruswitz et al., 2010). Each monomer contains 12 transmembrane helices, one more than in the bacterial homologs. Reconstituted into proteoliposomes, RhCG conducts NH3 to raise the internal pH. Models of the erythrocyte Rh complex based on the RhCG structure suggest that the erythrocytic Rh complex is composed of stochastically assembled heterotrimers of RhAG, RhD, and RhCE (Gruswitz et al., 2010).

Accession Number:Q9UBD6
Protein Name:Ammonium transporter Rh type C aka RhCG
Length:479
Molecular Weight:53179.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:11
Location1 / Topology2 / Orientation3: Apical cell membrane1 / Multi-pass membrane protein2
Substrate ammonia, NH4+

Cross database links:

Genevestigator: Q9UBD6
eggNOG: prNOG18998
HEGENOM: HBG713085
RefSeq: NP_057405.1   
Entrez Gene ID: 51458   
Pfam: PF00909   
OMIM: 605381  gene
KEGG: hsa:51458   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0016323 C:basolateral plasma membrane
GO:0031410 C:cytoplasmic vesicle
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:0015837 P:amine transport
GO:0006873 P:cellular ion homeostasis
GO:0030855 P:epithelial cell differentiation
GO:0070634 P:transepithelial ammonium transport
GO:0055085 P:transmembrane transport

References (8)

[1] “Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis.”  Liu Z.et.al.   10852913
[2] “RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia.”  Chen B.-S.et.al.   12204676
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast.”  Marini A.-M.et.al.   11062476
[5] “NH3 is involved in the NH4+ transport induced by the functional expression of the human Rh C glycoprotein.”  Bakouh N.et.al.   14761968
[6] “Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells.”  Zidi-Yahiaoui N.et.al.   15929723
[7] “Structural involvement in substrate recognition of an essential aspartate residue conserved in Mep/Amt and Rh-type ammonium transporters.”  Marini A.-M.et.al.   16477434
[8] “Ammonium transport properties of HEK293 cells expressing RhCG mutants: preliminary analysis of structure/function by site-directed mutagenesis.”  Zidi-Yahiaoui N.et.al.   16580862
Structure:
3HD6     

External Searches:

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  • 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:	MAWNTNLRWR LPLTCLLLQV IMVILFGVFV RYDFEADAHW WSERTHKNLS DMENEFYYRY 
61:	PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI QWALLMQGWF HFLQDRYIVV 
121:	GVENLINADF CVASVCVAFG AVLGKVSPIQ LLIMTFFQVT LFAVNEFILL NLLKVKDAGG 
181:	SMTIHTFGAY FGLTVTRILY RRNLEQSKER QNSVYQSDLF AMIGTLFLWM YWPSFNSAIS 
241:	YHGDSQHRAA INTYCSLAAC VLTSVAISSA LHKKGKLDMV HIQNATLAGG VAVGTAAEMM 
301:	LMPYGALIIG FVCGIISTLG FVYLTPFLES RLHIQDTCGI NNLHGIPGII GGIVGAVTAA 
361:	SASLEVYGKE GLVHSFDFQG FNGDWTARTQ GKFQIYGLLV TLAMALMGGI IVGLILRLPF 
421:	WGQPSDENCF EDAVYWEMPE GNSTVYIPED PTFKPSGPSV PSVPMVSPLP MASSVPLVP