RHAG_RAT
ID RHAG_RAT Reviewed; 450 AA.
AC Q7TNK7; O88300;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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].
RC TISSUE=Blood;
RX PubMed=16227429; DOI=10.1073/pnas.0507886102;
RA Huang C.-H., Peng J.;
RT "Evolutionary conservation and diversification of Rh family genes and
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15512-15517(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 {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; AB015194; BAA32443.1; -; mRNA.
DR EMBL; AF531097; AAQ10014.1; -; mRNA.
DR RefSeq; NP_075411.2; NM_023022.2.
DR AlphaFoldDB; Q7TNK7; -.
DR SMR; Q7TNK7; -.
DR STRING; 10116.ENSRNOP00000065437; -.
DR GlyGen; Q7TNK7; 4 sites.
DR iPTMnet; Q7TNK7; -.
DR PhosphoSitePlus; Q7TNK7; -.
DR PaxDb; Q7TNK7; -.
DR GeneID; 65207; -.
DR KEGG; rno:65207; -.
DR UCSC; RGD:61871; rat.
DR CTD; 6005; -.
DR RGD; 61871; Rhag.
DR eggNOG; KOG3796; Eukaryota.
DR InParanoid; Q7TNK7; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q7TNK7; -.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-RNO-444411; Rhesus glycoproteins mediate ammonium transport.
DR PRO; PR:Q7TNK7; -.
DR Proteomes; UP000002494; Unplaced.
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:RGD.
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; ISS:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; ISO:RGD.
DR GO; GO:0006873; P:cellular ion homeostasis; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; ISO:RGD.
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..450
FT /note="Ammonium transporter Rh type A"
FT /id="PRO_0000380191"
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..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 34..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
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 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="S -> P (in Ref. 1; BAA32443)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="G -> S (in Ref. 1; BAA32443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49062 MW; D5F1BBCE45D6335D CRC64;
MRFKFSLIAL SLEVVMIVSF ALFVEYETSQ NGSQKSASQQ NASQQNAAAQ QNASQQGNAS
SPAKEDQFFQ LYPLFQHVHV MIFVGFGFLM TFLKKYGFSG VGFNLFLAAL GLQWGTIVQG
LLHSHGLKFP FRIKNMINAD FSTATVLISF GAVLGKTSPI QMIIMTILEI AVFAGNEHLV
TEIFKASDTG ASMTIHAFGA YFGLAVAGVL YRSGLKHGHP NEESVYHSDL FAMIGTLFLW
MFWPSFNSAI AQPENNQYRA IVNTYMSLAA CVITAYALSS LVERRGRLDM VHIQNATLAG
GVAVGTCADM EIPLYFAMTI GSIAGIISVL GYKFLSPLLA HKLMIHDTCG VHNLHGLPGV
FGGLASIVAI SWGKSTVSTM AMQATALGSS IGSAIVGGLV TGLILKLPVW NQPPDEYCFD
DSVSWKVPKY RELDNYFFQH VTHNHVEHEV
