RHCG_PANTR
ID RHCG_PANTR Reviewed; 479 AA.
AC Q3BCQ7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Ammonium transporter Rh type C;
DE AltName: Full=Rhesus blood group family type C glycoprotein;
DE Short=Rh family type C glycoprotein;
DE Short=Rh type C glycoprotein;
GN Name=RHCG;
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 [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 an electroneutral and bidirectional ammonium
CC transporter. May regulate transepithelial ammonia secretion (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Also detected at the basolateral
CC membrane and in subapical vesicles. {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; AY831675; AAX39717.1; -; mRNA.
DR RefSeq; NP_001030600.1; NM_001035523.1.
DR AlphaFoldDB; Q3BCQ7; -.
DR SMR; Q3BCQ7; -.
DR STRING; 9598.ENSPTRP00000054512; -.
DR GeneID; 453638; -.
DR KEGG; ptr:453638; -.
DR CTD; 51458; -.
DR InParanoid; Q3BCQ7; -.
DR OrthoDB; 910733at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006873; P:cellular ion homeostasis; ISS:UniProtKB.
DR GO; GO:0070634; P:transepithelial ammonium 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; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="Ammonium transporter Rh type C"
FT /id="PRO_0000283580"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 53089 MW; C33F47E1D4056A38 CRC64;
MAWNTNLRWR LPLTCLLLQV VMVILFGVFV RYDFEADAHW WSERTHKNLS DVENEFYYRY
PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI QWALLMQGWF HFLQGRYIVV
GVENLINADF CVASVCVAFG AVLGKVSPIQ LLIMTFFQVT LFAVNEFILL NLLKVKDAGG
SMTIHTFGAY FGLTVTRILY RRNLEQSKER QNSVYQSDLF AMIGTLFLWM YWPSFNSAIS
YHGDSQHRAA INTYCSLAAC VLTSVAISSA LHKKGKLDMV HIQNATLAGG VAVGTAAEMM
LMPYGALIIG FVCGIISTLG FVYLTPFLES RLHIQDTCGI NNLHGIPGII GGIVGAVTAA
SASLEVYGKE GLVHSFDFQG FKGDWTARTQ GKFQIYGLLV TLAMALMGGI IVGLILRLPF
WGQPSDENCF EDAVYWEMPE GNSTVYIPED PTFKPSGPSV PSVPMVSPLP MASSVPLVP
