RHCG1_TAKRU
ID RHCG1_TAKRU Reviewed; 485 AA.
AC Q18PF5; Q7T3R5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Ammonium transporter Rh type C 1;
DE AltName: Full=FRhcg1;
DE AltName: Full=Rhesus blood group family type C glycoprotein 1;
DE Short=RHCG-1;
DE Short=Rh family type C glycoprotein 1;
DE Short=Rh type C glycoprotein 1;
GN Name=rhcg1;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17218543; DOI=10.1096/fj.06-6834com;
RA Nakada T., Westhoff C.M., Kato A., Hirose S.;
RT "Ammonia secretion from fish gill depends on a set of Rh glycoproteins.";
RL FASEB J. 21:1067-1074(2007).
CC -!- FUNCTION: Functions as an ammonia transporter. May play a role in the
CC elimination of ammonia in the gill. {ECO:0000269|PubMed:17218543}.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17218543}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17218543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q18PF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q18PF5-2; Sequence=VSP_024338;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the gill by mitochondria-
CC rich cells. {ECO:0000269|PubMed:17218543}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AY116075; AAM48578.1; -; mRNA.
DR EMBL; AB218981; BAE96343.1; -; mRNA.
DR RefSeq; NP_001027819.1; NM_001032647.1. [Q18PF5-2]
DR RefSeq; XP_011605548.1; XM_011607246.1.
DR AlphaFoldDB; Q18PF5; -.
DR SMR; Q18PF5; -.
DR STRING; 31033.ENSTRUP00000001063; -.
DR GeneID; 445990; -.
DR KEGG; tru:445990; -.
DR CTD; 792274; -.
DR eggNOG; KOG3796; Eukaryota.
DR InParanoid; Q18PF5; -.
DR OrthoDB; 910733at2759; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
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 Alternative splicing; Ammonia transport; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..485
FT /note="Ammonium transporter Rh type C 1"
FT /id="PRO_0000283587"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 453..485
FT /note="LPEDEESAPPILHYNNHMANKDVVDTNFGMEQN -> GIFHSKATRAAPQCD
FT LVAAETHVCFPNRSNSAWVCFQVQLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16227429"
FT /id="VSP_024338"
SQ SEQUENCE 485 AA; 53460 MW; CC4FA065797F2778 CRC64;
MGCVQSFRTL CDRPKNTNVR ISLPAVCFVW QIAMIILFGV FIRYDEESDT HWIEHRKKEN
ISSDIENDFY FRYPSFQDVH VMIFVGFGFL MTFLKRYSFG AVGFNFLIAA FGLQWALLMQ
GWFHSLDYTD GKIKIGVESL INADFCVAGC LIAYGAVLGK VSPVQLMVLT LFGITLFAVE
EYIILSLIHA RDAGGSMVIH TFGGYYGLSI SWMLYRPNLD QSSNLQGSVY HSDVFAMIGT
LFLWMFWPSF NSAITDHGDG QHRAAINTYL ALASTVLTTV AISSLFQKHG KLDMVHIQNS
TLAGGVAVGT AAEFMLMPYG SLIVGFCCGI ISTLGYIYLT PFMEKHLKIQ DTCGIHNLHA
MPGVIGGIVG AITAAAASES VYGKEGLINT FDFEGAFKNM VPTKQGGHQA AGLCVAICFG
IGGGIIVGCI LRLPIWGDPA DDNCFNDEPY WELPEDEESA PPILHYNNHM ANKDVVDTNF
GMEQN
