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Ammonium transporter Rh type A (Erythrocyte membrane glycoprotein Rh50) (Rhesus blood group family type A glycoprotein) (Rh family type A glycoprotein) (Rh type A glycoprotein) (CD antigen CD241)

 RHAG_MOUSE              Reviewed;         438 AA.
Q9QUT0; Q3UP27; Q794G1;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 121.
RecName: Full=Ammonium transporter Rh type A;
AltName: Full=Erythrocyte membrane glycoprotein Rh50;
AltName: Full=Rhesus blood group family type A glycoprotein;
Short=Rh family type A glycoprotein;
Short=Rh type A glycoprotein;
AltName: CD_antigen=CD241;
Name=Rhag; Synonyms=Rh50;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL-10SnJ; TISSUE=Bone marrow;
PubMed=9705835; DOI=10.1006/bbrc.1998.9074;
Kitano T., Sumiyama K., Shiroishi T., Saitou N.;
"Conserved evolution of the Rh50 gene compared to its homologous Rh
blood group gene.";
Biochem. Biophys. Res. Commun. 249:78-85(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9929383; DOI=10.1007/PL00006453;
Matassi G., Cherif-Zahar B., Pesole G., Raynal V., Cartron J.-P.;
"The members of the RH gene family (RH50 and RH30) followed different
evolutionary pathways.";
J. Mol. Evol. 48:151-159(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10495887; DOI=10.1023/A:1018726303397;
Liu Z., Huang C.-H.;
"The mouse Rhl1 and Rhag genes: sequence, organization, expression,
and chromosomal mapping.";
Biochem. Genet. 37:119-138(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May be part of an oligomeric complex which is likely to
have a transport or channel function in the erythrocyte membrane.
Involved in ammonia transport across the erythrocyte membrane.
Seems to act in monovalent cation transport.
{ECO:0000250|UniProtKB:Q02094}.
-!- SUBUNIT: Heterotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q02094};
Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49)
family. Rh subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB015192; BAA32441.1; -; mRNA.
EMBL; AF065395; AAD13387.1; -; mRNA.
EMBL; AF057526; AAC25155.1; -; mRNA.
EMBL; AK143851; BAE25570.1; -; mRNA.
EMBL; AK157847; BAE34227.1; -; mRNA.
EMBL; CH466559; EDL23386.1; -; Genomic_DNA.
EMBL; BC101941; AAI01942.1; -; mRNA.
EMBL; BC101942; AAI01943.1; -; mRNA.
EMBL; BC103512; AAI03513.1; -; mRNA.
EMBL; BC103662; AAI03663.1; -; mRNA.
CCDS; CCDS28787.1; -.
RefSeq; NP_035399.1; NM_011269.2.
UniGene; Mm.12961; -.
ProteinModelPortal; Q9QUT0; -.
SMR; Q9QUT0; -.
IntAct; Q9QUT0; 1.
MINT; Q9QUT0; -.
STRING; 10090.ENSMUSP00000024721; -.
PhosphoSitePlus; Q9QUT0; -.
PaxDb; Q9QUT0; -.
PRIDE; Q9QUT0; -.
Ensembl; ENSMUST00000024721; ENSMUSP00000024721; ENSMUSG00000023926.
GeneID; 19743; -.
KEGG; mmu:19743; -.
UCSC; uc008col.1; mouse.
CTD; 6005; -.
MGI; MGI:1202713; Rhag.
eggNOG; KOG3796; Eukaryota.
eggNOG; ENOG410XTF8; LUCA.
GeneTree; ENSGT00390000005787; -.
HOGENOM; HOG000007656; -.
InParanoid; Q9QUT0; -.
KO; K06580; -.
OMA; GTCADMA; -.
OrthoDB; EOG091G06KX; -.
PhylomeDB; Q9QUT0; -.
TreeFam; TF314450; -.
Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-MMU-444411; Rhesus glycoproteins mediate ammonium transport.
PRO; PR:Q9QUT0; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023926; -.
Genevisible; Q9QUT0; MM.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
GO; GO:0015696; P:ammonium transport; IMP:MGI.
GO; GO:0015670; P:carbon dioxide transport; ISO:MGI.
GO; GO:0006873; P:cellular ion homeostasis; ISS:UniProtKB.
GO; GO:0048821; P:erythrocyte development; IMP:MGI.
GO; GO:0015672; P:monovalent inorganic cation transport; ISS:UniProtKB.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:MGI.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
InterPro; IPR002229; RhesusRHD.
Pfam; PF00909; Ammonium_transp; 1.
PRINTS; PR00342; RHESUSRHD.
1: Evidence at protein level;
Ammonia transport; Complete proteome; Glycoprotein; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 438 Ammonium transporter Rh type A.
/FTId=PRO_0000380190.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TOPO_DOM 26 61 Extracellular. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TOPO_DOM 83 86 Cytoplasmic. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TOPO_DOM 108 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 149 169 Helical. {ECO:0000255}.
TOPO_DOM 170 178 Extracellular. {ECO:0000255}.
TRANSMEM 179 199 Helical. {ECO:0000255}.
TOPO_DOM 200 218 Cytoplasmic. {ECO:0000255}.
TRANSMEM 219 239 Helical. {ECO:0000255}.
TOPO_DOM 240 249 Extracellular. {ECO:0000255}.
TRANSMEM 250 270 Helical. {ECO:0000255}.
TOPO_DOM 271 278 Cytoplasmic. {ECO:0000255}.
TRANSMEM 279 296 Helical. {ECO:0000255}.
TOPO_DOM 297 300 Extracellular. {ECO:0000255}.
TRANSMEM 301 321 Helical. {ECO:0000255}.
TOPO_DOM 322 342 Cytoplasmic. {ECO:0000255}.
TRANSMEM 343 363 Helical. {ECO:0000255}.
TOPO_DOM 364 372 Extracellular. {ECO:0000255}.
TRANSMEM 373 393 Helical. {ECO:0000255}.
TOPO_DOM 394 438 Cytoplasmic. {ECO:0000255}.
CARBOHYD 31 31 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 180 180 A -> P (in Ref. 4; BAE25570).
{ECO:0000305}.
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


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