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Q9UBD6 (RHCG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ammonium transporter Rh type C
Alternative name(s):
Rh glycoprotein kidney
Rhesus blood group family type C glycoprotein
Short name=Rh family type C glycoprotein
Short name=Rh type C glycoprotein
Tumor-related protein DRC2
Gene names
Name:RHCG
Synonyms:C15orf6, CDRC2, PDRC2, RHGK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion. Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Homotrimer. Ref.13

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Also detected at the basolateral membrane and in subapical vesicles By similarity. Ref.1 Ref.2

Tissue specificity

Expressed in brain, testis, placenta, pancreas, esophagus and prostate. Expressed in squamous epithelial tissues (at protein level). According to Ref.8, specifically expressed in kidney. Ref.1 Ref.2 Ref.8

Developmental stage

Specifically expressed in fetal kidney. Ref.1

Post-translational modification

N-glycosylated. Ref.1 Ref.13

Sequence similarities

Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily. [View classification]

Ontologies

Keywords
   Biological processAmmonia transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Uncategorized?

Inferred from direct assay. Source: UniProtKB

   Biological_processamine transport

Non-traceable author statement Ref.1. Source: UniProtKB

ammonium transmembrane transport

Inferred from direct assay Ref.9Ref.10Ref.12PubMed 18032481. Source: GOC

ammonium transport

Inferred from direct assay Ref.9Ref.10Ref.12PubMed 18032481. Source: UniProtKB

cellular ion homeostasis

Inferred from direct assay Ref.9. Source: UniProtKB

epithelial cell differentiation

Non-traceable author statement Ref.2. Source: UniProtKB

homeostatic process

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of pH

Inferred from electronic annotation. Source: Ensembl

transepithelial ammonium transport

Inferred from direct assay PubMed 18032481. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 16928804PubMed 18032481. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 16928804. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.2Ref.10. Source: UniProtKB

   Molecular_functionammonium transmembrane transporter activity

Inferred from direct assay Ref.9Ref.10Ref.12PubMed 18032481. Source: UniProtKB

ankyrin binding

Inferred from direct assay PubMed 12719424. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Ammonium transporter Rh type C
PRO_0000283577

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Potential
Topological domain31 – 6030Extracellular Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 854Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12317Extracellular Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 1484Cytoplasmic Potential
Transmembrane149 – 16921Helical; Potential
Topological domain170 – 1778Extracellular Potential
Transmembrane178 – 20023Helical; Potential
Topological domain201 – 21818Cytoplasmic Potential
Transmembrane219 – 23921Helical; Potential
Topological domain240 – 25011Extracellular Potential
Transmembrane251 – 27121Helical; Potential
Topological domain272 – 28110Cytoplasmic Potential
Transmembrane282 – 30221Helical; Potential
Topological domain3031Extracellular Potential
Transmembrane304 – 32421Helical; Potential
Topological domain325 – 34521Cytoplasmic Potential
Transmembrane346 – 36621Helical; Potential
Topological domain367 – 39428Extracellular Potential
Transmembrane395 – 41521Helical; Potential
Topological domain416 – 47964Cytoplasmic Potential

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Ref.13

Natural variations

Natural variant2021R → C.
Corresponds to variant rs17807723 [ dbSNP | Ensembl ].
VAR_031496

Experimental info

Mutagenesis741F → L: Reduction of ammonia transport. Ref.12
Mutagenesis1371V → I: Reduction of ammonia transport. Ref.12
Mutagenesis1771D → N: Loss of function. Ref.11
Mutagenesis2351F → V: Reduction of ammonia transport. Ref.12
Sequence conflict2421H → R in AAP81044. Ref.6
Sequence conflict4421N → D in AAP81044. Ref.6

Secondary structure

............................................. 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UBD6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E5D8024D720D4589

FASTA47953,179
        10         20         30         40         50         60 
MAWNTNLRWR LPLTCLLLQV IMVILFGVFV RYDFEADAHW WSERTHKNLS DMENEFYYRY 

        70         80         90        100        110        120 
PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI QWALLMQGWF HFLQDRYIVV 

       130        140        150        160        170        180 
GVENLINADF CVASVCVAFG AVLGKVSPIQ LLIMTFFQVT LFAVNEFILL NLLKVKDAGG 

       190        200        210        220        230        240 
SMTIHTFGAY FGLTVTRILY RRNLEQSKER QNSVYQSDLF AMIGTLFLWM YWPSFNSAIS 

       250        260        270        280        290        300 
YHGDSQHRAA INTYCSLAAC VLTSVAISSA LHKKGKLDMV HIQNATLAGG VAVGTAAEMM 

       310        320        330        340        350        360 
LMPYGALIIG FVCGIISTLG FVYLTPFLES RLHIQDTCGI NNLHGIPGII GGIVGAVTAA 

       370        380        390        400        410        420 
SASLEVYGKE GLVHSFDFQG FNGDWTARTQ GKFQIYGLLV TLAMALMGGI IVGLILRLPF 

       430        440        450        460        470 
WGQPSDENCF EDAVYWEMPE GNSTVYIPED PTFKPSGPSV PSVPMVSPLP MASSVPLVP 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis."
Liu Z., Chen Y., Mo R., Hui C.-C., Cheng J.-F., Mohandas N., Huang C.-H.
J. Biol. Chem. 275:25641-25651(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, GLYCOSYLATION.
Tissue: Kidney.
[2]"RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia."
Chen B.-S., Xu Z.-X., Xu X., Cai Y., Han Y.-L., Wang J., Xia S.-H., Hu H., Wei F., Wu M., Wang M.-R.
Eur. J. Cancer 38:1927-1936(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Placenta.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Esophagus and Tongue.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Functional characterization of RhCG glycoprotein from human renal proximal cells."
Nakhoul N.L., Hamm L.L., Abdulnour-Nakhoul S.M., De Jong H.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney epithelium.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[8]"The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast."
Marini A.-M., Matassi G., Raynal V., Andre B., Cartron J.-P., Cherif-Zahar B.
Nat. Genet. 26:341-344(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"NH3 is involved in the NH4+ transport induced by the functional expression of the human Rh C glycoprotein."
Bakouh N., Benjelloun F., Hulin P., Brouillard F., Edelman A., Cherif-Zahar B., Planelles G.
J. Biol. Chem. 279:15975-15983(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells."
Zidi-Yahiaoui N., Mouro-Chanteloup I., D'Ambrosio A.-M., Lopez C., Gane P., Le van Kim C., Cartron J.-P., Colin Y., Ripoche P.
Biochem. J. 391:33-40(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Structural involvement in substrate recognition of an essential aspartate residue conserved in Mep/Amt and Rh-type ammonium transporters."
Marini A.-M., Boeckstaens M., Benjelloun F., Cherif-Zahar B., Andre B.
Curr. Genet. 49:364-374(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-177.
[12]"Ammonium transport properties of HEK293 cells expressing RhCG mutants: preliminary analysis of structure/function by site-directed mutagenesis."
Zidi-Yahiaoui N., Ripoche P., Le Van Kim C., Gane P., D'Ambrosio A.-M., Cartron J.-P., Colin Y., Mouro-Chanteloup I.
Transfus. Clin. Biol. 13:128-131(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-74; VAL-137 AND PHE-235.
[13]"Function of human Rh based on structure of RhCG at 2.1 A."
Gruswitz F., Chaudhary S., Ho J.D., Schlessinger A., Pezeshki B., Ho C.M., Sali A., Westhoff C.M., Stroud R.M.
Proc. Natl. Acad. Sci. U.S.A. 107:9638-9643(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-479, SUBUNIT, GLYCOSYLATION AT ASN-48.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF193809 mRNA. Translation: AAF19372.1.
AF219986 expand/collapse EMBL AC list , AF219981, AF219982, AF219983, AF219984, AF219985 Genomic DNA. Translation: AAG02171.1.
AF081497 mRNA. Translation: AAD55748.1.
AF284446 Genomic DNA. Translation: AAG02414.1.
AY257182 mRNA. Translation: AAP81044.1.
AK290899 mRNA. Translation: BAF83588.1.
AK313238 mRNA. Translation: BAG36049.1.
AC013391 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02051.1.
BC030965 mRNA. Translation: AAH30965.1.
RefSeqNP_057405.1. NM_016321.2.
UniGeneHs.459284.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HD6X-ray2.10A2-479[»]
ProteinModelPortalQ9UBD6.
SMRQ9UBD6. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59334N.
STRING9606.ENSP00000268122.

Chemistry

GuidetoPHARMACOLOGY1200.

Protein family/group databases

TCDB1.A.11.4.1. the ammonia transporter channel (amt) family.

PTM databases

PhosphoSiteQ9UBD6.

Polymorphism databases

DMDM74734928.

Proteomic databases

PaxDbQ9UBD6.
PRIDEQ9UBD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268122; ENSP00000268122; ENSG00000140519.
GeneID51458.
KEGGhsa:51458.
UCSCuc002bnz.2. human.

Organism-specific databases

CTD51458.
GeneCardsGC15M090014.
HGNCHGNC:18140. RHCG.
HPAHPA041874.
HPA043317.
MIM605381. gene.
neXtProtNX_Q9UBD6.
PharmGKBPA134876043.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276393.
HOGENOMHOG000007656.
HOVERGENHBG004374.
InParanoidQ9UBD6.
KOK06580.
OMASQHRAAI.
PhylomeDBQ9UBD6.
TreeFamTF314450.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_20679. Amine compound SLC transporters.

Gene expression databases

ArrayExpressQ9UBD6.
BgeeQ9UBD6.
CleanExHS_RHCG.
GenevestigatorQ9UBD6.

Family and domain databases

InterProIPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PfamPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSPR00342. RHESUSRHD.
SUPFAMSSF111352. SSF111352. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRHCG. human.
EvolutionaryTraceQ9UBD6.
GeneWikiRHCG.
GenomeRNAi51458.
NextBio55075.
PROQ9UBD6.
SOURCESearch...

Entry information

Entry nameRHCG_HUMAN
AccessionPrimary (citable) accession number: Q9UBD6
Secondary accession number(s): A8K4D4, Q6X3Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM