RHAG_CANLF
ID RHAG_CANLF Reviewed; 415 AA.
AC Q3BCQ5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
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; AY831677; AAX39719.1; -; mRNA.
DR RefSeq; NP_001104238.1; NM_001110768.1.
DR AlphaFoldDB; Q3BCQ5; -.
DR SMR; Q3BCQ5; -.
DR STRING; 9615.ENSCAFP00000040637; -.
DR PaxDb; Q3BCQ5; -.
DR GeneID; 481833; -.
DR KEGG; cfa:481833; -.
DR CTD; 6005; -.
DR eggNOG; KOG3796; Eukaryota.
DR HOGENOM; CLU_021386_1_0_1; -.
DR InParanoid; Q3BCQ5; -.
DR OrthoDB; 910733at2759; -.
DR Reactome; R-CFA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-CFA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-CFA-444411; Rhesus glycoproteins mediate ammonium transport.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000002141; Expressed in bone marrow and 17 other tissues.
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: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:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Ammonia transport; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..415
FT /note="Ammonium transporter Rh type A"
FT /id="PRO_0000380189"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 44905 MW; 5FDEF008A97A9BD0 CRC64;
MRFIFPTIAV LLEASMIVLF GFFVKYETEQ NAIQQPNSTN STKVDRSLEL YPLFQDVHVM
IFVGFGFLMT FLKKYGFSSV GINLLIAALG LQWGTFVQGM VHRHGQTIYI GIKNMINADF
STATVLISFG AVLGKISPTQ MLIMTIIEIT VFAGNEYVVG EIFQASDIGA SMTIHAFGAY
FGLAVAGVLY RTGLRKGHEK EESEYHSDLF AMIGTLFLWM FWPSFNSAIA ETAEEQYLAI
INTYLSLVAC VLTAYAMSSL VGHRGKLDMV HIQNATLAGG VAVGTCADMK IHPYGSLIIG
SIAGMVSVLG FRFLTPCLTA KLRIHDTCGV HNLHGLPGVV GGLSSIVAIL LGVSTASSMT
MQAAALGSSI GSAIAGGLIT GLILRFIVRG QPSKDNFFDD SVYWEVPKEK ELDNV
