RHCG_RABIT
ID RHCG_RABIT Reviewed; 467 AA.
AC Q95JD3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 73.
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 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=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).
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; AY013263; AAK14653.1; -; mRNA.
DR RefSeq; NP_001076198.1; NM_001082729.1.
DR AlphaFoldDB; Q95JD3; -.
DR SMR; Q95JD3; -.
DR STRING; 9986.ENSOCUP00000014962; -.
DR PRIDE; Q95JD3; -.
DR GeneID; 100009494; -.
DR KEGG; ocu:100009494; -.
DR CTD; 51458; -.
DR eggNOG; KOG3796; Eukaryota.
DR InParanoid; Q95JD3; -.
DR OrthoDB; 910733at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0072488; P:ammonium 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; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..467
FT /note="Ammonium transporter Rh type C"
FT /id="PRO_0000283583"
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..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..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..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..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 436..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 51731 MW; 2EE5A3D47597C46F CRC64;
MAWNTNLRWR LPLLCLVLEV AMVVLFGLFV RYSPDADSSW SNEKRKGNIT SDLENEFYYR
YPSFQDVHVM VFLGFGFLMT FLQRYGYCAL GFNFLLAALG VQWALLMQGW FQYTKDRLIL
LGIKNLIDAD SCVASVCVAF GAVLGKVSPV QMLLMTFFQV ALFSANEFLL LHVLEVKDAG
GSITIHIFGA YFGLTVTWIL YRHNLDHSRE RQSSVYHSNL FAMIGTLFLW IYWPSFNSAM
SNYGDAQHRA AINTYCSLAA SVLTSVAMSS VLHKKGKLDM VHIQNATLAG GVGVGTAAEM
MLMPYGALIV GFICGAVSTL GFVYLTPFLE SRLRIQDTCG IHNLHGIPGL IGAIVGAVTA
AYASPDGDRG FVYPFGFHNE KDEKVQGRFQ AFGLLLTLAI AMVGGTIMGL ILKLPFWGQA
MDEDCFDDSI YWEMHEEKSS SPEDHTHKPS VPTEPVEQPT SSATLAP
