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Q9QXP0

- RHCG_MOUSE

UniProt

Q9QXP0 - RHCG_MOUSE

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Protein

Ammonium transporter Rh type C

Gene

Rhcg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.1 Publication

GO - Molecular functioni

  1. ammonium transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ammonium transmembrane transport Source: GOC
  2. ammonium transport Source: UniProtKB
  3. cellular ion homeostasis Source: Ensembl
  4. regulation of pH Source: UniProtKB
  5. transepithelial ammonium transport Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Ammonia transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198711. Rhesus glycoproteins mediate ammonium transport.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Rhcg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1888517. Rhcg.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST
Topological domaini31 – 6131ExtracellularSequence AnalysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence AnalysisAdd
BLAST
Topological domaini83 – 864CytoplasmicSequence Analysis
Transmembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 12417ExtracellularSequence AnalysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence AnalysisAdd
BLAST
Topological domaini146 – 1538CytoplasmicSequence Analysis
Transmembranei154 – 17421HelicalSequence AnalysisAdd
BLAST
Topological domaini175 – 1795ExtracellularSequence Analysis
Transmembranei180 – 20021HelicalSequence AnalysisAdd
BLAST
Topological domaini201 – 21919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei220 – 24021HelicalSequence AnalysisAdd
BLAST
Topological domaini241 – 25111ExtracellularSequence AnalysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 2797CytoplasmicSequence Analysis
Transmembranei280 – 30223HelicalSequence AnalysisAdd
BLAST
Topological domaini303 – 3042ExtracellularSequence Analysis
Transmembranei305 – 32521HelicalSequence AnalysisAdd
BLAST
Topological domaini326 – 34015CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei341 – 36121HelicalSequence AnalysisAdd
BLAST
Topological domaini362 – 39534ExtracellularSequence AnalysisAdd
BLAST
Transmembranei396 – 41621HelicalSequence AnalysisAdd
BLAST
Topological domaini417 – 49882CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. integral component of plasma membrane Source: Ensembl
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Ammonium transporter Rh type CPRO_0000283579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9QXP0.

PTM databases

PhosphoSiteiQ9QXP0.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ9QXP0.
CleanExiMM_RHCG.
ExpressionAtlasiQ9QXP0. baseline and differential.
GenevestigatoriQ9QXP0.

Interactioni

Subunit structurei

Homotrimer.

Structurei

3D structure databases

ProteinModelPortaliQ9QXP0.
SMRiQ9QXP0. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276393.
GeneTreeiENSGT00390000005787.
HOGENOMiHOG000007656.
HOVERGENiHBG004374.
InParanoidiQ9QXP0.
KOiK06580.
OMAiENCFEDE.
OrthoDBiEOG73NG3C.
PhylomeDBiQ9QXP0.
TreeFamiTF314450.

Family and domain databases

Gene3Di1.10.3430.10. 1 hit.
InterProiIPR029020. Ammonium/urea_transptr.
IPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PfamiPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSiPR00342. RHESUSRHD.
SUPFAMiSSF111352. SSF111352. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9QXP0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAWNTNLRGR LPITCLILQV TMVVLFGVFV RYDIQADAHW WLEKKRKNIS
60 70 80 90 100
SDVENEFYYR YPSFQDVHAM VFVGFGFLMT FLQRYGFSAV GFNFLLAAFG
110 120 130 140 150
IQWALLMQGW FHYFEEGHIV LSVENIIQAD FCVASSCVAF GAVLGKVSPM
160 170 180 190 200
QLLIMTFFQV TLFTVNEFIL LNLIEAKDAG GSMTIHTFGA YFGLTVTWIL
210 220 230 240 250
YRKNLDQSKQ RQSSVYHSDL FAMIGTLFLW IYWPSFNSAS SFHGDAQHRA
260 270 280 290 300
ALNTYLSLAA SVLTTVTVSS IVHKKGKLDM VHIQNATLAG GVGVGTAAEM
310 320 330 340 350
MLTPYGALIV GFFCGIFSTL GFAYLTPFLE SRHRIQDTCG IHNLHGIPGI
360 370 380 390 400
IGGIVGAVTA AYSSPDVYGE PGIVHSFGFG SYKMDWNKRM QGRSQIFGLL
410 420 430 440 450
LSLAMALVGG IIVGFILKLP FWGQAADENC FEDSIYWEVH EEVNTVYIPE
460 470 480 490
DLAHKHSTSL VPAMPLVLPT TSASIVPPVP PTPPVSLATS APSAALVH
Length:498
Mass (Da):54,972
Last modified:April 3, 2007 - v2
Checksum:iB10F6A09C16DB464
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3331H → L in AAF19373. (PubMed:10852913)Curated
Sequence conflicti333 – 3331H → L in AAP81168. 1 PublicationCurated
Sequence conflicti333 – 3331H → L in AAI19046. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193810 mRNA. Translation: AAF19373.1.
AY254686 mRNA. Translation: AAP81168.1.
AK076757 mRNA. Translation: BAC36469.1.
BC119045 mRNA. Translation: AAI19046.1.
CCDSiCCDS21383.1.
RefSeqiNP_062773.2. NM_019799.3.
UniGeneiMm.10909.

Genome annotation databases

EnsembliENSMUST00000032766; ENSMUSP00000032766; ENSMUSG00000030549.
GeneIDi56315.
KEGGimmu:56315.
UCSCiuc009hyo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193810 mRNA. Translation: AAF19373.1 .
AY254686 mRNA. Translation: AAP81168.1 .
AK076757 mRNA. Translation: BAC36469.1 .
BC119045 mRNA. Translation: AAI19046.1 .
CCDSi CCDS21383.1.
RefSeqi NP_062773.2. NM_019799.3.
UniGenei Mm.10909.

3D structure databases

ProteinModelPortali Q9QXP0.
SMRi Q9QXP0. Positions 2-441.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9QXP0.

Proteomic databases

PRIDEi Q9QXP0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032766 ; ENSMUSP00000032766 ; ENSMUSG00000030549 .
GeneIDi 56315.
KEGGi mmu:56315.
UCSCi uc009hyo.2. mouse.

Organism-specific databases

CTDi 51458.
MGIi MGI:1888517. Rhcg.

Phylogenomic databases

eggNOGi NOG276393.
GeneTreei ENSGT00390000005787.
HOGENOMi HOG000007656.
HOVERGENi HBG004374.
InParanoidi Q9QXP0.
KOi K06580.
OMAi ENCFEDE.
OrthoDBi EOG73NG3C.
PhylomeDBi Q9QXP0.
TreeFami TF314450.

Enzyme and pathway databases

Reactomei REACT_198711. Rhesus glycoproteins mediate ammonium transport.

Miscellaneous databases

NextBioi 312264.
PROi Q9QXP0.
SOURCEi Search...

Gene expression databases

Bgeei Q9QXP0.
CleanExi MM_RHCG.
ExpressionAtlasi Q9QXP0. baseline and differential.
Genevestigatori Q9QXP0.

Family and domain databases

Gene3Di 1.10.3430.10. 1 hit.
InterProi IPR029020. Ammonium/urea_transptr.
IPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view ]
Pfami PF00909. Ammonium_transp. 1 hit.
[Graphical view ]
PRINTSi PR00342. RHESUSRHD.
SUPFAMi SSF111352. SSF111352. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRHCG_MOUSE
AccessioniPrimary (citable) accession number: Q9QXP0
Secondary accession number(s): Q8BVS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3