RHBG_RAT
ID RHBG_RAT Reviewed; 455 AA.
AC Q68FT6; Q7TNP0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=12595489; DOI=10.1097/01.asn.0000050413.43662.55;
RA Quentin F., Eladari D., Cheval L., Lopez C., Goossens D., Colin Y.,
RA Cartron J.-P., Paillard M., Chambrey R.;
RT "RhBG and RhCG, the putative ammonia transporters, are expressed in the
RT same cells in the distal nephron.";
RL J. Am. Soc. Nephrol. 14:545-554(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15611082; DOI=10.1074/jbc.m413351200;
RA Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R.,
RA Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.;
RT "The ammonium transporter RhBG: requirement of a tyrosine-based signal and
RT ankyrin-G for basolateral targeting and membrane anchorage in polarized
RT kidney epithelial cells.";
RL J. Biol. Chem. 280:8221-8228(2005).
CC -!- FUNCTION: Functions as a specific ammonium transporter. {ECO:0000250}.
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 (at protein level). {ECO:0000269|PubMed:12595489}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12595489}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AY129072; AAN07790.1; -; mRNA.
DR EMBL; BC079365; AAH79365.1; -; mRNA.
DR RefSeq; NP_898877.1; NM_183054.1.
DR AlphaFoldDB; Q68FT6; -.
DR SMR; Q68FT6; -.
DR STRING; 10116.ENSRNOP00000026396; -.
DR GlyGen; Q68FT6; 1 site.
DR PaxDb; Q68FT6; -.
DR Ensembl; ENSRNOT00000026396; ENSRNOP00000026396; ENSRNOG00000019412.
DR GeneID; 310625; -.
DR KEGG; rno:310625; -.
DR UCSC; RGD:727813; rat.
DR CTD; 57127; -.
DR RGD; 727813; Rhbg.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_0_0_1; -.
DR InParanoid; Q68FT6; -.
DR OMA; IFVRYNH; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q68FT6; -.
DR TreeFam; TF314450; -.
DR Reactome; R-RNO-444411; Rhesus glycoproteins mediate ammonium transport.
DR PRO; PR:Q68FT6; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019412; Expressed in ovary and 16 other tissues.
DR ExpressionAtlas; Q68FT6; baseline and differential.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; 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:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
DR GO; GO:0070634; P:transepithelial ammonium transport; 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; 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_0000283605"
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..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..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 CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 347
FT /note="L -> V (in Ref. 1; AAN07790)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="L -> V (in Ref. 1; AAN07790)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="K -> R (in Ref. 1; AAN07790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 49731 MW; 725815539CC2F19A CRC64;
MARIPRHRRL VLPLLCLLFQ GATSLLFAIF VRYNHETDAA LWHWGNHSNV DNEFYFRYPS
FQDVHVMVFV GFGFLMVFLQ RYGFSSVGFT FLVATFTLQW ATLLQGFLHS FHGGHIHIGV
ESLINADFCA GAVLISFGAV LGKTGPAQLL LMALLEAVLF SVNEFILLSL LGVRDAGGSM
TIHTFGAYFG LFLSRVLYRS QLEKSRHRQT SVYNSDLFAM IGTIFLWVFW PSFNSAPTAL
GDGQHRTVVN TYYSLTASTL STFALSALVS GDGRLDMVHI QNAALAGGVV VGTASEMMLT
PFGALAAGFL AGTVSTLGYK FFTPILESRF KLQDTCGVHN LHGMPGLLGA ILGVLVAALA
THEAYGDGLQ TVFPLIAKGQ RSATSQAMYQ LFGMFVTLVF ASVGGSLGGL LLKLPFLDSP
PDSQCFEDQV YWEVPGEQEA ETQRPLRTEE PDTQA
