RHBG_MOUSE
ID RHBG_MOUSE Reviewed; 455 AA.
AC Q8BUX5; Q9QXP1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ammonium transporter Rh type B;
DE AltName: Full=Rhesus blood group family type B glycoprotein;
DE Short=Rh family type B glycoprotein;
DE Short=Rh type B glycoprotein;
GN Name=Rhbg;
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], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=11024028; DOI=10.1074/jbc.m007528200;
RA Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.;
RT "Rh type B glycoprotein is a new member of the Rh superfamily and a
RT putative ammonia transporter in mammals.";
RL J. Biol. Chem. 276:1424-1433(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C3H/HeJ; TISSUE=Kidney cortex;
RX PubMed=15353405; DOI=10.1152/ajprenal.00419.2003;
RA Nakhoul N.L., Dejong H., Abdulnour-Nakhoul S.M., Boulpaep E.L.,
RA Hering-Smith K., Hamm L.L.;
RT "Characteristics of renal Rhbg as an NH4(+) transporter.";
RL Am. J. Physiol. 288:F170-F181(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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].
RC STRAIN=FVB/N; TISSUE=Colon;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12730882; DOI=10.1016/s0016-5085(03)00277-4;
RA Weiner I.D., Miller R.T., Verlander J.W.;
RT "Localization of the ammonium transporters, Rh B glycoprotein and Rh C
RT glycoprotein, in the mouse liver.";
RL Gastroenterology 124:1432-1440(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [8]
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 a specific ammonium transporter.
CC {ECO:0000269|PubMed:15353405, ECO:0000269|PubMed:16131648}.
CC -!- SUBUNIT: Interacts (via C-terminus) with ANK2 and ANK3; required for
CC targeting to the basolateral membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney by connecting segments and
CC collecting tubules. Also expressed in liver by perivenous hepatocytes.
CC Expressed in the forestomach and the fundus of the stomach. Expressed
CC in duodenum, jejunum, ileum and colon at the level of villous (at
CC protein level). Specifically expressed in kidney where it is restricted
CC to the epithelial linings of the convoluted tubules and the loop of
CC Henle. Also detected in ovary. Expressed by hepatocytes and dermal hair
CC follicles and papillae. {ECO:0000269|PubMed:11024028,
CC ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:12730882,
CC ECO:0000269|PubMed:15576624}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos at 15 dpc and 17 dpc.
CC Expressed in kidney, skin and liver of 16.5 dpc embryos.
CC {ECO:0000269|PubMed:11024028}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11024028}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AF193808; AAF19371.1; -; mRNA.
DR EMBL; AY254685; AAP81167.1; -; mRNA.
DR EMBL; AK081882; BAC38359.1; -; mRNA.
DR EMBL; BC029236; AAH29236.1; -; mRNA.
DR CCDS; CCDS17466.1; -.
DR RefSeq; NP_067350.2; NM_021375.3.
DR AlphaFoldDB; Q8BUX5; -.
DR SMR; Q8BUX5; -.
DR STRING; 10090.ENSMUSP00000130767; -.
DR GlyGen; Q8BUX5; 1 site.
DR iPTMnet; Q8BUX5; -.
DR PhosphoSitePlus; Q8BUX5; -.
DR jPOST; Q8BUX5; -.
DR MaxQB; Q8BUX5; -.
DR PaxDb; Q8BUX5; -.
DR PRIDE; Q8BUX5; -.
DR DNASU; 58176; -.
DR Ensembl; ENSMUST00000171887; ENSMUSP00000130767; ENSMUSG00000104445.
DR GeneID; 58176; -.
DR KEGG; mmu:58176; -.
DR UCSC; uc008pui.1; mouse.
DR CTD; 57127; -.
DR MGI; MGI:1927379; Rhbg.
DR VEuPathDB; HostDB:ENSMUSG00000104445; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_0_0_1; -.
DR InParanoid; Q8BUX5; -.
DR OMA; IFVRYNH; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q8BUX5; -.
DR TreeFam; TF314450; -.
DR Reactome; R-MMU-444411; Rhesus glycoproteins mediate ammonium transport.
DR BioGRID-ORCS; 58176; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rhbg; mouse.
DR PRO; PR:Q8BUX5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BUX5; protein.
DR Bgee; ENSMUSG00000104445; Expressed in right kidney and 46 other tissues.
DR Genevisible; Q8BUX5; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin 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: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; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..455
FT /note="Ammonium transporter Rh type B"
FT /id="PRO_0000283599"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 413..421
FT /note="Interaction with ANK3"
FT /evidence="ECO:0000250"
FT REGION 434..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 195
FT /note="W -> R (in Ref. 1; AAF19371 and 4; AAH29236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 49543 MW; C8D57B88A37089D2 CRC64;
MARVPRHRRL VLPLLCLLFQ GATALLFAIF VRYNHETDAA LWHWGNHSNV DNEFYFRYPS
FQDVHVMVFV GFGFLMVFLQ RYGFSSVGFT FLVASLTLQW ATLLQGFLHS FHGGHIHVGV
ESLINADFCA GAVLISFGAV LGKTGPAQLL LMALLEAVLF SVNEFILLSL LGVRDAGGSM
TIHTFGAYFG LFLSWVLYRS QLEKSRHRQS SVYNSDLFAM IGTIFLWVFW PSFNSAPTAL
GDGQHRTVVN TYYSLTASTL STFALSALVS GDGRLDMVHV QNAALAGGVV VGTSSEMMLT
PFGALAAGFL AGTVSTLGYK FFTPILESRF KLQDTCGVHN LHGMPGVLGA ILGVVVAALA
THEAYGDGLQ SVFPLIAKGQ RSATSQAVYQ LFGMFVTLVF ASVGGSLGGL LLRLPFLDSP
PDSQCFEDQV YWEVPGEQET ETQRPLRGGE SDTRA
