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Q9QXP0 (RHCG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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):
Rhesus blood group family type C glycoprotein
Short name=Rh family type C glycoprotein
Short name=Rh type C glycoprotein
Rhesus blood group-associated C glycoprotein
Short name=Rhesus-associated C glycoprotein
Gene names
Name:Rhcg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length498 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.7

Subunit structure

Homotrimer.

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Also detected at the basolateral membrane and in subapical vesicles By similarity. Ref.5 Ref.6

Tissue specificity

Expressed in the forestomach and the fundus of the stomach. Expressed at the level of villous in duodenum, jejunum, ileum and colon. Expressed in kidney by connecting segments and collecting tubules (at protein level). Expressed in testis by seminiferous tubules. Ref.1 Ref.5 Ref.6

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Ammonium transporter Rh type C
PRO_0000283579

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Potential
Topological domain31 – 6131Extracellular Potential
Transmembrane62 – 8221Helical; Potential
Topological domain83 – 864Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 12417Extracellular Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 1538Cytoplasmic Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 1795Extracellular Potential
Transmembrane180 – 20021Helical; Potential
Topological domain201 – 21919Cytoplasmic Potential
Transmembrane220 – 24021Helical; Potential
Topological domain241 – 25111Extracellular Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 2797Cytoplasmic Potential
Transmembrane280 – 30223Helical; Potential
Topological domain303 – 3042Extracellular Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 34015Cytoplasmic Potential
Transmembrane341 – 36121Helical; Potential
Topological domain362 – 39534Extracellular Potential
Transmembrane396 – 41621Helical; Potential
Topological domain417 – 49882Cytoplasmic Potential

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3331H → L in AAF19373. Ref.1
Sequence conflict3331H → L in AAP81168. Ref.2
Sequence conflict3331H → L in AAI19046. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9QXP0 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: B10F6A09C16DB464

FASTA49854,972
        10         20         30         40         50         60 
MAWNTNLRGR LPITCLILQV TMVVLFGVFV RYDIQADAHW WLEKKRKNIS SDVENEFYYR 

        70         80         90        100        110        120 
YPSFQDVHAM VFVGFGFLMT FLQRYGFSAV GFNFLLAAFG IQWALLMQGW FHYFEEGHIV 

       130        140        150        160        170        180 
LSVENIIQAD FCVASSCVAF GAVLGKVSPM QLLIMTFFQV TLFTVNEFIL LNLIEAKDAG 

       190        200        210        220        230        240 
GSMTIHTFGA YFGLTVTWIL YRKNLDQSKQ RQSSVYHSDL FAMIGTLFLW IYWPSFNSAS 

       250        260        270        280        290        300 
SFHGDAQHRA ALNTYLSLAA SVLTTVTVSS IVHKKGKLDM VHIQNATLAG GVGVGTAAEM 

       310        320        330        340        350        360 
MLTPYGALIV GFFCGIFSTL GFAYLTPFLE SRHRIQDTCG IHNLHGIPGI IGGIVGAVTA 

       370        380        390        400        410        420 
AYSSPDVYGE PGIVHSFGFG SYKMDWNKRM QGRSQIFGLL LSLAMALVGG IIVGFILKLP 

       430        440        450        460        470        480 
FWGQAADENC FEDSIYWEVH EEVNTVYIPE DLAHKHSTSL VPAMPLVLPT TSASIVPPVP 

       490 
PTPPVSLATS APSAALVH

« 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 [MRNA], TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Functional characterization of Rhcg glycoprotein."
Nakhoul N.L., Hamm L.L., Abdulnour-Nakhoul S.M., De Jong H., Palmer S.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
Tissue: Kidney cortex.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[4]"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].
[5]"Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney."
Verlander J.W., Miller R.T., Frank A.E., Royaux I.E., Kim Y.-H., Weiner I.D.
Am. J. Physiol. 284:F323-F337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Expression of the ammonia transporter proteins Rh B glycoprotein and Rh C glycoprotein in the intestinal tract."
Handlogten M.E., Hong S.-P., Zhang L., Vander A.W., Steinbaum M.L., Campbell-Thompson M., Weiner I.D.
Am. J. Physiol. 288:G1036-G1047(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]"Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG."
Mak D.-O., Dang B., Weiner I.D., Foskett J.K., Westhoff C.M.
Am. J. Physiol. 290:F297-F305(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF193810 mRNA. Translation: AAF19373.1.
AY254686 mRNA. Translation: AAP81168.1.
AK076757 mRNA. Translation: BAC36469.1.
BC119045 mRNA. Translation: AAI19046.1.
IPIIPI00311731.
RefSeqNP_062773.2. NM_019799.3.
UniGeneMm.10909.

3D structure databases

ProteinModelPortalQ9QXP0.
SMRQ9QXP0. Positions 2-441.
ModBaseSearch...

PTM databases

PhosphoSiteQ9QXP0.

Proteomic databases

PRIDEQ9QXP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032766; ENSMUSP00000032766; ENSMUSG00000030549.
GeneID56315.
KEGGmmu:56315.
UCSCuc009hyo.2. mouse.

Organism-specific databases

CTD51458.
MGIMGI:1888517. Rhcg.

Phylogenomic databases

eggNOGNOG276393.
GeneTreeENSGT00390000005787.
HOGENOMHOG000007656.
HOVERGENHBG004374.
InParanoidQ9QXP0.
KOK06580.
OMAWILYRPN.
OrthoDBEOG4WSW9N.

Gene expression databases

ArrayExpressQ9QXP0.
BgeeQ9QXP0.
CleanExMM_RHCG.
GenevestigatorQ9QXP0.

Family and domain databases

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

Other

NextBio312264.
SOURCESearch...

Entry information

Entry nameRHCG_MOUSE
AccessionPrimary (citable) accession number: Q9QXP0
Secondary accession number(s): Q8BVS0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: April 3, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents