RHBG_RABIT
ID RHBG_RABIT Reviewed; 458 AA.
AC Q95JD4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
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: 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 {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {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; AY013262; AAK14652.1; -; mRNA.
DR RefSeq; NP_001075605.1; NM_001082136.1.
DR AlphaFoldDB; Q95JD4; -.
DR SMR; Q95JD4; -.
DR STRING; 9986.ENSOCUP00000023475; -.
DR Ensembl; ENSOCUT00000023604; ENSOCUP00000023475; ENSOCUG00000016130.
DR GeneID; 100008876; -.
DR KEGG; ocu:100008876; -.
DR CTD; 57127; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR InParanoid; Q95JD4; -.
DR OrthoDB; 910733at2759; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000016130; Expressed in skin of back and 7 other tissues.
DR ExpressionAtlas; Q95JD4; baseline.
DR GO; GO:0046658; C:anchored component of plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
DR GO; GO:0070634; P:transepithelial ammonium transport; IEA:Ensembl.
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; Cell membrane; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..458
FT /note="Ammonium transporter Rh type B"
FT /id="PRO_0000283604"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..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..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 416..424
FT /note="Interaction with ANK3"
FT /evidence="ECO:0000250"
FT MOTIF 429..432
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 458 AA; 49425 MW; 0FC41E08EC78B357 CRC64;
MAKSPRRVAG RRLLLPLLCL FFQGATAILF AIFVRYDQQT DAALWHGGNH SNADNEFYFR
YPSFQDVHAM VFVGFGFLMV FLQRYGYSSL GFTFLLGAFA LQWATLVQGF LHSFHGGHIH
VGMESLINAD FCAGAVLISF GAVLGKTGPA QLLLMALLEV ALFGLNEFVL LCLLGVRDAG
GSMTIHTFGA YFGLVLSRVL YRPHLEKSQH RQGSVYHSDL FAMIGTIFLW IFWPSFNSAL
TSRGDGQPRT ALNTYYSLTA STLSTFALSA LVGKDGRLDM VHVQNAALAG GVVVGTASEM
MLTPFGALAA GCLAGAISTL GYKFFTPILE SKLKIQDTCG VHNLHGMPGV LGALLGALMT
GLTTHEAYGD GLQSVFPLIA EGQRSATSQA IYQLFGLSVT LLFASAGGVL GGLLLKLPFL
DAPPDSQCYE DQMCWEVPGE HGYEAQEALR VEEPDTEA
