RHCG_TETNG
ID RHCG_TETNG Reviewed; 475 AA.
AC Q3BBX7; Q4S7D9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
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; ORFNames=GSTENG00022829001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
CC -!- FUNCTION: Functions as an ammonia transporter. May play a role in the
CC elimination of ammonia in the gill (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG03443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY865615; AAY41907.1; -; mRNA.
DR EMBL; CAAE01014715; CAG03443.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q3BBX7; -.
DR SMR; Q3BBX7; -.
DR KEGG; tng:GSTEN00022829G001; -.
DR InParanoid; Q3BBX7; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 Ammonia transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Ammonium transporter Rh type C"
FT /id="PRO_0000283591"
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..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 52622 MW; F6E70239DB2DA426 CRC64;
MGCVQSFRNF CDRPKNTNVR ISLPAVCFVW QIAMIILFGV FIRYNEEADT HWVEYRKKEN
ISSDIENDFY FRYPSFQDVH VMIFVGFGFL MTFLKRYSFG AVGFNFLIAA FGLQWALLMQ
GWFHSLDYTD GKIKIGIENL INADFCVAGC LIAYGAVLGK VSPVQLMVLT LFGITLFAVE
EYIILNLIHA RDAGGSMVIH TFGGYYGLSI SWMLYRPNLE QSSNLQGSVY QSDVFAMIGT
LFLWMFWPSF NSAITDHGDG QHRAAINTYL ALASTVLTTV AISSLFQKHG KLDMVHIQNS
TLAGGVAVGT AAEFMLMPYG SLIVGFCCGI ISTLGYIYLT PFMEKYLKIQ DTCGIHNLHA
MPGLIGGIVG AITAAAATES VYGKEGLVNT FDFVGPFKNM VPTTQGGHQA AGLCVAICFG
IGGGIMVGCI LRLPIWCDPA DDNCFNDEPY WELPEEEEII PPILHYNNHM VNKDV
