Q9UBD6 (RHCG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ammonia transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amine transport Non-traceable author statement Ref.1. Source: UniProtKB cellular ion homeostasis Inferred from direct assay Ref.9. Source: UniProtKB epithelial cell differentiation Non-traceable author statement Ref.2. Source: UniProtKB regulation of pH Inferred from electronic annotation. Source: Compara transepithelial ammonium transport Inferred from direct assay PubMed 18032481. Source: UniProtKB
Cellular_component	apical 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 integral to plasma membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ammonia transmembrane transporter activity Inferred from direct assay Ref.12PubMed 18032481. Source: UniProtKB ammonium transmembrane transporter activity Inferred from direct assay Ref.9Ref.10. Source: UniProtKB ankyrin binding Inferred from direct assay PubMed 12719424. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 479

479

Ammonium transporter Rh type C

PRO_0000283577

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 30

21

Helical; Potential

Topological domain

31 – 60

30

Extracellular Potential

Transmembrane

61 – 81

21

Helical; Potential

Topological domain

82 – 85

4

Cytoplasmic Potential

Transmembrane

86 – 106

21

Helical; Potential

Topological domain

107 – 123

17

Extracellular Potential

Transmembrane

124 – 144

21

Helical; Potential

Topological domain

145 – 148

4

Cytoplasmic Potential

Transmembrane

149 – 169

21

Helical; Potential

Topological domain

170 – 177

8

Extracellular Potential

Transmembrane

178 – 200

23

Helical; Potential

Topological domain

201 – 218

18

Cytoplasmic Potential

Transmembrane

219 – 239

21

Helical; Potential

Topological domain

240 – 250

11

Extracellular Potential

Transmembrane

251 – 271

21

Helical; Potential

Topological domain

272 – 281

10

Cytoplasmic Potential

Transmembrane

282 – 302

21

Helical; Potential

Topological domain

303

1

Extracellular Potential

Transmembrane

304 – 324

21

Helical; Potential

Topological domain

325 – 345

21

Cytoplasmic Potential

Transmembrane

346 – 366

21

Helical; Potential

Topological domain

367 – 394

28

Extracellular Potential

Transmembrane

395 – 415

21

Helical; Potential

Topological domain

416 – 479

64

Cytoplasmic Potential

Amino acid modifications

Glycosylation

48

1

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

Natural variations

Natural variant

202

1

R → C.
Corresponds to variant rs17807723 [ dbSNP | Ensembl ].

VAR_031496

Experimental info

Mutagenesis

74

1

F → L: Reduction of ammonia transport. Ref.12

Mutagenesis

137

1

V → I: Reduction of ammonia transport. Ref.12

Mutagenesis

177

1

D → N: Loss of function. Ref.11

Mutagenesis

235

1

F → V: Reduction of ammonia transport. Ref.12

Sequence conflict

242

1

H → R in AAP81044. Ref.6

Sequence conflict

442

1

N → D in AAP81044. Ref.6

Secondary structure

1

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479

Helix Strand Turn

Details...

Helix

10 – 29

20

Helix

55 – 71

17

Helix

73 – 77

5

Helix

78 – 80

3

Helix

85 – 109

25

Turn

114 – 116

3

Beta strand

117 – 119

3

Helix

122 – 142

21

Helix

148 – 170

23

Turn

181 – 184

4

Helix

185 – 198

14

Helix

204 – 207

4

Turn

208 – 210

3

Helix

215 – 235

21

Turn

236 – 239

4

Helix

243 – 270

28

Helix

279 – 284

6

Helix

285 – 287

3

Helix

288 – 292

5

Turn

293 – 299

7

Helix

303 – 332

30

Helix

340 – 343

4

Helix

345 – 360

16

Helix

385 – 416

32

Helix

432 – 434

3

Turn

440 – 442

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UBD6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E5D8024D720D4589	FASTA	479	53,179
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF193809 mRNA. Translation: AAF19372.1.
AF219986 , 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.

IPI

IPI00008820.

RefSeq

NP_057405.1. NM_016321.1.

UniGene

Hs.459284.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HD6	X-ray	2.10	A	2-479	[»]

ProteinModelPortal

Q9UBD6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59334N.

STRING

9606.ENSP00000268122.

Protein family/group databases

TCDB

1.A.11.4.1. ammonia transporter channel (Amt) family.

PTM databases

PhosphoSite

Q9UBD6.

Polymorphism databases

DMDM

74734928.

Proteomic databases

PaxDb

Q9UBD6.

PRIDE

Q9UBD6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268122; ENSP00000268122; ENSG00000140519.

GeneID

51458.

KEGG

hsa:51458.

UCSC

uc002bnz.2. human.

Organism-specific databases

CTD

51458.

GeneCards

GC15M090014.

HGNC

HGNC:18140. RHCG.

HPA

HPA041874.
HPA043317.

MIM

605381. gene.

neXtProt

NX_Q9UBD6.

PharmGKB

PA134876043.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG276393.

HOGENOM

HOG000007656.

HOVERGEN

HBG004374.

InParanoid

Q9UBD6.

KO

K06580.

OMA

WILYRPN.

OrthoDB

EOG4WSW9N.

PhylomeDB

Q9UBD6.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.
REACT_20679. Amine compound SLC transporters.

Gene expression databases

ArrayExpress

Q9UBD6.

Bgee

Q9UBD6.

CleanEx

HS_RHCG.

Genevestigator

Q9UBD6.

Family and domain databases

InterPro

IPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]

Pfam

PF00909. Ammonium_transp. 1 hit.
[Graphical view]

PRINTS

PR00342. RHESUSRHD.

SUPFAM

SSF111352. RH_like_transpt. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RHCG. human.

EvolutionaryTrace

Q9UBD6.

GenomeRNAi

51458.

NextBio

55075.

SOURCE

Search...

Entry information

Entry name

RHCG_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.