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RHBG_PANTR
ID   RHBG_PANTR              Reviewed;         458 AA.
AC   Q95M74;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11358367; DOI=10.1006/bcmd.2000.0355;
RA   Huang C.-H., Liu P.Z.;
RT   "New insights into the Rh superfamily of genes and proteins in erythroid
RT   cells and nonerythroid tissues.";
RL   Blood Cells Mol. Dis. 27:90-101(2001).
RN   [2]
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; AY013268; AAK15395.1; -; Genomic_DNA.
DR   EMBL; AY013264; AAK15395.1; JOINED; Genomic_DNA.
DR   EMBL; AY013265; AAK15395.1; JOINED; Genomic_DNA.
DR   EMBL; AY013266; AAK15395.1; JOINED; Genomic_DNA.
DR   EMBL; AY013267; AAK15395.1; JOINED; Genomic_DNA.
DR   EMBL; AY831674; AAX39716.1; -; mRNA.
DR   RefSeq; NP_001009091.1; NM_001009091.2.
DR   AlphaFoldDB; Q95M74; -.
DR   SMR; Q95M74; -.
DR   STRING; 9598.ENSPTRP00000054083; -.
DR   PaxDb; Q95M74; -.
DR   Ensembl; ENSPTRT00000061546; ENSPTRP00000054083; ENSPTRG00000001458.
DR   GeneID; 457394; -.
DR   KEGG; ptr:457394; -.
DR   CTD; 57127; -.
DR   VGNC; VGNC:10035; RHBG.
DR   eggNOG; KOG3796; Eukaryota.
DR   GeneTree; ENSGT00950000182844; -.
DR   InParanoid; Q95M74; -.
DR   OMA; IFVRYNH; -.
DR   OrthoDB; 910733at2759; -.
DR   Proteomes; UP000002277; Chromosome 1.
DR   Bgee; ENSPTRG00000001458; Expressed in cerebellar cortex and 6 other tissues.
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; IBA:GO_Central.
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: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; 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_0000283600"
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   REGION          439..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  49502 MW;  D40B8EC84FA5C16B CRC64;
     MAGSPSRAAG RRLQLPLLCL FLQGATAVLF AVFVRYNHKT DAALWHRSNH SNADNEFYFR
     YPSFQDVHAM VFVGFGFLMV FLQRYGFSSV GFTFLLAAFA LQWSTLVQGF LHSFHGGHIH
     VGVESMINAD FCAGAVLISF GAVLGKTGPA QLLLMALLEV VLFGINEFVL LHLLGVRDAG
     GSMTIHTFGA YFGLVLSRVL YRPQLEKSKH RQGSVYHSDL FAMIGTIFLW IFWPSFNAAL
     TALGAGQHRT ALNTYYSLAA STLGTFALSA LVGEDGRLDM VHIQNAALAG GVVVGTSSEM
     MLTPFGALTA GFLAGTVSTL GYKFFRPILE SKFKVQDTCG VHNLHGMPGV LGALLGVLVA
     GLATHEAYGD GLESVFPLIA EGQRSATSQA MHQLFGLFVT LMFASVGGGL GGLLLKLPFL
     DSPPDSQCYE DQVHWQVPGE HEDKAQRPLR VEEADTQA
 
 
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