RHCG_MOUSE
ID RHCG_MOUSE Reviewed; 498 AA.
AC Q9QXP0; Q8BVS0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ammonium transporter Rh type C;
DE AltName: Full=Rhesus blood group family type C glycoprotein;
DE Short=Rh family type C glycoprotein;
DE Short=Rh type C glycoprotein;
DE AltName: Full=Rhesus blood group-associated C glycoprotein;
DE Short=Rhesus-associated C glycoprotein;
GN Name=Rhcg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10852913; DOI=10.1074/jbc.m003353200;
RA Liu Z., Chen Y., Mo R., Hui C.-C., Cheng J.-F., Mohandas N., Huang C.-H.;
RT "Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh
RT glycoprotein homologues predominantly expressed in kidney and testis.";
RL J. Biol. Chem. 275:25641-25651(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ; TISSUE=Kidney cortex;
RA Nakhoul N.L., Hamm L.L., Abdulnour-Nakhoul S.M., De Jong H., Palmer S.;
RT "Functional characterization of Rhcg glycoprotein.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12388412; DOI=10.1152/ajprenal.00050.2002;
RA Verlander J.W., Miller R.T., Frank A.E., Royaux I.E., Kim Y.-H.,
RA Weiner I.D.;
RT "Localization of the ammonium transporter proteins RhBG and RhCG in mouse
RT kidney.";
RL Am. J. Physiol. 284:F323-F337(2003).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15576624; DOI=10.1152/ajpgi.00418.2004;
RA Handlogten M.E., Hong S.-P., Zhang L., Vander A.W., Steinbaum M.L.,
RA Campbell-Thompson M., Weiner I.D.;
RT "Expression of the ammonia transporter proteins Rh B glycoprotein and Rh C
RT glycoprotein in the intestinal tract.";
RL Am. J. Physiol. 288:G1036-G1047(2005).
RN [7]
RP FUNCTION.
RX PubMed=16131648; DOI=10.1152/ajprenal.00147.2005;
RA Mak D.-O., Dang B., Weiner I.D., Foskett J.K., Westhoff C.M.;
RT "Characterization of ammonia transport by the kidney Rh glycoproteins RhBG
RT and RhCG.";
RL Am. J. Physiol. 290:F297-F305(2006).
CC -!- FUNCTION: Functions as an electroneutral and bidirectional ammonium
CC transporter. May regulate transepithelial ammonia secretion.
CC {ECO:0000269|PubMed:16131648}.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:15576624}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12388412,
CC ECO:0000269|PubMed:15576624}. Note=Also detected at the basolateral
CC membrane and in subapical vesicles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the forestomach and the fundus of the
CC stomach. Expressed at the level of villous in duodenum, jejunum, ileum
CC and colon. Expressed in kidney by connecting segments and collecting
CC tubules (at protein level). Expressed in testis by seminiferous
CC tubules. {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:12388412,
CC ECO:0000269|PubMed:15576624}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AF193810; AAF19373.1; -; mRNA.
DR EMBL; AY254686; AAP81168.1; -; mRNA.
DR EMBL; AK076757; BAC36469.1; -; mRNA.
DR EMBL; BC119045; AAI19046.1; -; mRNA.
DR CCDS; CCDS21383.1; -.
DR RefSeq; NP_062773.2; NM_019799.3.
DR AlphaFoldDB; Q9QXP0; -.
DR SMR; Q9QXP0; -.
DR STRING; 10090.ENSMUSP00000032766; -.
DR GlyGen; Q9QXP0; 1 site.
DR PhosphoSitePlus; Q9QXP0; -.
DR jPOST; Q9QXP0; -.
DR PaxDb; Q9QXP0; -.
DR PRIDE; Q9QXP0; -.
DR Antibodypedia; 28582; 288 antibodies from 32 providers.
DR DNASU; 56315; -.
DR Ensembl; ENSMUST00000032766; ENSMUSP00000032766; ENSMUSG00000030549.
DR GeneID; 56315; -.
DR KEGG; mmu:56315; -.
DR UCSC; uc009hyo.2; mouse.
DR CTD; 51458; -.
DR MGI; MGI:1888517; Rhcg.
DR VEuPathDB; HostDB:ENSMUSG00000030549; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_0_0_1; -.
DR InParanoid; Q9QXP0; -.
DR OMA; ENCFEDE; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9QXP0; -.
DR TreeFam; TF314450; -.
DR Reactome; R-MMU-444411; Rhesus glycoproteins mediate ammonium transport.
DR BioGRID-ORCS; 56315; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rhcg; mouse.
DR PRO; PR:Q9QXP0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QXP0; protein.
DR Bgee; ENSMUSG00000030549; Expressed in right kidney and 52 other tissues.
DR ExpressionAtlas; Q9QXP0; baseline and differential.
DR Genevisible; Q9QXP0; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006873; P:cellular ion homeostasis; ISO:MGI.
DR GO; GO:0006885; P:regulation of pH; IMP:UniProtKB.
DR GO; GO:0070634; P:transepithelial ammonium transport; ISO:MGI.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR002229; RhesusRHD.
DR Pfam; PF00909; Ammonium_transp; 1.
DR PRINTS; PR00342; RHESUSRHD.
PE 1: Evidence at protein level;
KW Ammonia transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="Ammonium transporter Rh type C"
FT /id="PRO_0000283579"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 333
FT /note="H -> L (in Ref. 1; AAF19373, 2; AAP81168 and 4;
FT AAI19046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 54972 MW; B10F6A09C16DB464 CRC64;
MAWNTNLRGR LPITCLILQV TMVVLFGVFV RYDIQADAHW WLEKKRKNIS SDVENEFYYR
YPSFQDVHAM VFVGFGFLMT FLQRYGFSAV GFNFLLAAFG IQWALLMQGW FHYFEEGHIV
LSVENIIQAD FCVASSCVAF GAVLGKVSPM QLLIMTFFQV TLFTVNEFIL LNLIEAKDAG
GSMTIHTFGA YFGLTVTWIL YRKNLDQSKQ RQSSVYHSDL FAMIGTLFLW IYWPSFNSAS
SFHGDAQHRA ALNTYLSLAA SVLTTVTVSS IVHKKGKLDM VHIQNATLAG GVGVGTAAEM
MLTPYGALIV GFFCGIFSTL GFAYLTPFLE SRHRIQDTCG IHNLHGIPGI IGGIVGAVTA
AYSSPDVYGE PGIVHSFGFG SYKMDWNKRM QGRSQIFGLL LSLAMALVGG IIVGFILKLP
FWGQAADENC FEDSIYWEVH EEVNTVYIPE DLAHKHSTSL VPAMPLVLPT TSASIVPPVP
PTPPVSLATS APSAALVH
