RHAG_MOUSE
ID RHAG_MOUSE Reviewed; 438 AA.
AC Q9QUT0; Q3UP27; Q794G1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ammonium transporter Rh type A;
DE AltName: Full=Erythrocyte membrane glycoprotein Rh50;
DE AltName: Full=Rhesus blood group family type A glycoprotein;
DE Short=Rh family type A glycoprotein;
DE Short=Rh type A glycoprotein;
DE AltName: CD_antigen=CD241;
GN Name=Rhag; Synonyms=Rh50;
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].
RC STRAIN=C57BL-10SnJ; TISSUE=Bone marrow;
RX PubMed=9705835; DOI=10.1006/bbrc.1998.9074;
RA Kitano T., Sumiyama K., Shiroishi T., Saitou N.;
RT "Conserved evolution of the Rh50 gene compared to its homologous Rh blood
RT group gene.";
RL Biochem. Biophys. Res. Commun. 249:78-85(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9929383; DOI=10.1007/pl00006453;
RA Matassi G., Cherif-Zahar B., Pesole G., Raynal V., Cartron J.-P.;
RT "The members of the RH gene family (RH50 and RH30) followed different
RT evolutionary pathways.";
RL J. Mol. Evol. 48:151-159(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10495887; DOI=10.1023/a:1018726303397;
RA Liu Z., Huang C.-H.;
RT "The mouse Rhl1 and Rhag genes: sequence, organization, expression, and
RT chromosomal mapping.";
RL Biochem. Genet. 37:119-138(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be part of an oligomeric complex which is likely to have
CC a transport or channel function in the erythrocyte membrane. Involved
CC in ammonia transport across the erythrocyte membrane. Seems to act in
CC monovalent cation transport. {ECO:0000250|UniProtKB:Q02094}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q02094}; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AB015192; BAA32441.1; -; mRNA.
DR EMBL; AF065395; AAD13387.1; -; mRNA.
DR EMBL; AF057526; AAC25155.1; -; mRNA.
DR EMBL; AK143851; BAE25570.1; -; mRNA.
DR EMBL; AK157847; BAE34227.1; -; mRNA.
DR EMBL; CH466559; EDL23386.1; -; Genomic_DNA.
DR EMBL; BC101941; AAI01942.1; -; mRNA.
DR EMBL; BC101942; AAI01943.1; -; mRNA.
DR EMBL; BC103512; AAI03513.1; -; mRNA.
DR EMBL; BC103662; AAI03663.1; -; mRNA.
DR CCDS; CCDS28787.1; -.
DR RefSeq; NP_035399.1; NM_011269.2.
DR AlphaFoldDB; Q9QUT0; -.
DR SMR; Q9QUT0; -.
DR STRING; 10090.ENSMUSP00000024721; -.
DR GlyGen; Q9QUT0; 4 sites.
DR PhosphoSitePlus; Q9QUT0; -.
DR jPOST; Q9QUT0; -.
DR PaxDb; Q9QUT0; -.
DR PRIDE; Q9QUT0; -.
DR ProteomicsDB; 255324; -.
DR Antibodypedia; 17000; 63 antibodies from 23 providers.
DR DNASU; 19743; -.
DR Ensembl; ENSMUST00000024721; ENSMUSP00000024721; ENSMUSG00000023926.
DR GeneID; 19743; -.
DR KEGG; mmu:19743; -.
DR UCSC; uc008col.1; mouse.
DR CTD; 6005; -.
DR MGI; MGI:1202713; Rhag.
DR VEuPathDB; HostDB:ENSMUSG00000023926; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_1_0_1; -.
DR InParanoid; Q9QUT0; -.
DR OMA; EITIFAC; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9QUT0; -.
DR TreeFam; TF314450; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-MMU-444411; Rhesus glycoproteins mediate ammonium transport.
DR BioGRID-ORCS; 19743; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9QUT0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QUT0; protein.
DR Bgee; ENSMUSG00000023926; Expressed in fetal liver hematopoietic progenitor cell and 70 other tissues.
DR ExpressionAtlas; Q9QUT0; baseline and differential.
DR Genevisible; Q9QUT0; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:MGI.
DR GO; GO:0015670; P:carbon dioxide transport; ISO:MGI.
DR GO; GO:0006873; P:cellular ion homeostasis; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP: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; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..438
FT /note="Ammonium transporter Rh type A"
FT /id="PRO_0000380190"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..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..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 180
FT /note="A -> P (in Ref. 4; BAE25570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 47837 MW; 077935143287FF9B CRC64;
MRFKFPLMAI SLEVAMIVLF GLFVEYETPQ NASQKNASHQ NASQQGNTSS SAKKDQFFQL
YPLFQDVHVM IFVGFGFLMT FLKKYGFSGV GFNLFLAALG LQWGTIMQGL LHSHGKEFHF
GIYNMINADF STATVLISFG AVLGKTSPIQ MLIMTILEIA VFAGNEYLVT ELFEASDTGA
SMTIHAFGAY FGLAVAGVLY RPGLRCEHPN DESVYHSDLF AMIGTLFLWI FWPSFNSAIA
DPGDHQYRAI VNTYMSLAAC VITAYALSSL VERRGRLDMV HIQNATLAGG VAVGTCADME
IPLYAAMTIG SIAGIISVLG YKFFSPLLAN KLMIHDTCGV HNLHGLPGVF GGLASIVAIS
WGMSTASMAM QAAALGSSIG SAIVGGLLTG LILKLPIWNQ PPDEYCYDDS VSWKVPKFRE
LDNRFFQHAN HNHVEHEV
