RHCG_HUMAN
ID RHCG_HUMAN Reviewed; 479 AA.
AC Q9UBD6; A8K4D4; Q6X3Y4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ammonium transporter Rh type C;
DE AltName: Full=Rh glycoprotein kidney;
DE AltName: Full=Rhesus blood group family type C glycoprotein;
DE Short=Rh family type C glycoprotein;
DE Short=Rh type C glycoprotein;
DE AltName: Full=Tumor-related protein DRC2;
GN Name=RHCG; Synonyms=C15orf6, CDRC2, PDRC2, RHGK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Kidney;
RX PubMed=10852913; DOI=10.1074/jbc.m003353200;
RA Liu Z., Chen Y., Mo R., Hui C.-C., Cheng J.-F., Mohandas N., Huang C.-H.;
RT "Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh
RT glycoprotein homologues predominantly expressed in kidney and testis.";
RL J. Biol. Chem. 275:25641-25651(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=12204676; DOI=10.1016/s0959-8049(02)00190-9;
RA Chen B.-S., Xu Z.-X., Xu X., Cai Y., Han Y.-L., Wang J., Xia S.-H., Hu H.,
RA Wei F., Wu M., Wang M.-R.;
RT "RhCG is downregulated in oesophageal squamous cell carcinomas, but
RT expressed in multiple squamous epithelia.";
RL Eur. J. Cancer 38:1927-1936(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Esophagus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney epithelium;
RA Nakhoul N.L., Hamm L.L., Abdulnour-Nakhoul S.M., De Jong H.;
RT "Functional characterization of RhCG glycoprotein from human renal proximal
RT cells.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11062476; DOI=10.1038/81656;
RA Marini A.-M., Matassi G., Raynal V., Andre B., Cartron J.-P.,
RA Cherif-Zahar B.;
RT "The human Rhesus-associated RhAG protein and a kidney homologue promote
RT ammonium transport in yeast.";
RL Nat. Genet. 26:341-344(2000).
RN [9]
RP FUNCTION.
RX PubMed=14761968; DOI=10.1074/jbc.m308528200;
RA Bakouh N., Benjelloun F., Hulin P., Brouillard F., Edelman A.,
RA Cherif-Zahar B., Planelles G.;
RT "NH3 is involved in the NH4+ transport induced by the functional expression
RT of the human Rh C glycoprotein.";
RL J. Biol. Chem. 279:15975-15983(2004).
RN [10]
RP FUNCTION.
RX PubMed=15929723; DOI=10.1042/bj20050657;
RA Zidi-Yahiaoui N., Mouro-Chanteloup I., D'Ambrosio A.-M., Lopez C., Gane P.,
RA Le van Kim C., Cartron J.-P., Colin Y., Ripoche P.;
RT "Human Rhesus B and Rhesus C glycoproteins: properties of facilitated
RT ammonium transport in recombinant kidney cells.";
RL Biochem. J. 391:33-40(2005).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASP-177.
RX PubMed=16477434; DOI=10.1007/s00294-006-0062-5;
RA Marini A.-M., Boeckstaens M., Benjelloun F., Cherif-Zahar B., Andre B.;
RT "Structural involvement in substrate recognition of an essential aspartate
RT residue conserved in Mep/Amt and Rh-type ammonium transporters.";
RL Curr. Genet. 49:364-374(2006).
RN [12]
RP MUTAGENESIS OF PHE-74; VAL-137 AND PHE-235.
RX PubMed=16580862; DOI=10.1016/j.tracli.2006.02.025;
RA Zidi-Yahiaoui N., Ripoche P., Le Van Kim C., Gane P., D'Ambrosio A.-M.,
RA Cartron J.-P., Colin Y., Mouro-Chanteloup I.;
RT "Ammonium transport properties of HEK293 cells expressing RhCG mutants:
RT preliminary analysis of structure/function by site-directed mutagenesis.";
RL Transfus. Clin. Biol. 13:128-131(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-479, SUBUNIT, AND GLYCOSYLATION
RP AT ASN-48.
RX PubMed=20457942; DOI=10.1073/pnas.1003587107;
RA Gruswitz F., Chaudhary S., Ho J.D., Schlessinger A., Pezeshki B., Ho C.M.,
RA Sali A., Westhoff C.M., Stroud R.M.;
RT "Function of human Rh based on structure of RhCG at 2.1 A.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9638-9643(2010).
CC -!- FUNCTION: Functions as an electroneutral and bidirectional ammonium
CC transporter. May regulate transepithelial ammonia secretion.
CC {ECO:0000269|PubMed:11062476, ECO:0000269|PubMed:14761968,
CC ECO:0000269|PubMed:15929723, ECO:0000269|PubMed:16477434}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:20457942}.
CC -!- INTERACTION:
CC Q9UBD6; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-15853497, EBI-12062109;
CC Q9UBD6; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-15853497, EBI-12003442;
CC Q9UBD6; Q07325: CXCL9; NbExp=3; IntAct=EBI-15853497, EBI-3911467;
CC Q9UBD6; P52803: EFNA5; NbExp=3; IntAct=EBI-15853497, EBI-1753674;
CC Q9UBD6; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-15853497, EBI-10976398;
CC Q9UBD6; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-15853497, EBI-713304;
CC Q9UBD6; O00155: GPR25; NbExp=3; IntAct=EBI-15853497, EBI-10178951;
CC Q9UBD6; P24593: IGFBP5; NbExp=3; IntAct=EBI-15853497, EBI-720480;
CC Q9UBD6; O15243: LEPROT; NbExp=3; IntAct=EBI-15853497, EBI-15672507;
CC Q9UBD6; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-15853497, EBI-12070086;
CC Q9UBD6; Q9UBD6: RHCG; NbExp=2; IntAct=EBI-15853497, EBI-15853497;
CC Q9UBD6; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-15853497, EBI-2852148;
CC Q9UBD6; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-15853497, EBI-12111910;
CC Q9UBD6; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-15853497, EBI-11988865;
CC Q9UBD6; O75841: UPK1B; NbExp=3; IntAct=EBI-15853497, EBI-12237619;
CC Q9UBD6; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-15853497, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:12204676}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10852913,
CC ECO:0000269|PubMed:12204676}. Note=Also detected at the basolateral
CC membrane and in subapical vesicles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, placenta, pancreas,
CC esophagus and prostate. Expressed in squamous epithelial tissues (at
CC protein level). According to PubMed:11062476, specifically expressed in
CC kidney. {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:11062476,
CC ECO:0000269|PubMed:12204676}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in fetal kidney.
CC {ECO:0000269|PubMed:10852913}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10852913,
CC ECO:0000269|PubMed:20457942}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AF193809; AAF19372.1; -; mRNA.
DR EMBL; AF219986; AAG02171.1; -; Genomic_DNA.
DR EMBL; AF219981; AAG02171.1; JOINED; Genomic_DNA.
DR EMBL; AF219982; AAG02171.1; JOINED; Genomic_DNA.
DR EMBL; AF219983; AAG02171.1; JOINED; Genomic_DNA.
DR EMBL; AF219984; AAG02171.1; JOINED; Genomic_DNA.
DR EMBL; AF219985; AAG02171.1; JOINED; Genomic_DNA.
DR EMBL; AF081497; AAD55748.1; -; mRNA.
DR EMBL; AF284446; AAG02414.1; -; Genomic_DNA.
DR EMBL; AY257182; AAP81044.1; -; mRNA.
DR EMBL; AK290899; BAF83588.1; -; mRNA.
DR EMBL; AK313238; BAG36049.1; -; mRNA.
DR EMBL; AC013391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02051.1; -; Genomic_DNA.
DR EMBL; BC030965; AAH30965.1; -; mRNA.
DR CCDS; CCDS10351.1; -.
DR RefSeq; NP_001307970.1; NM_001321041.1.
DR RefSeq; NP_057405.1; NM_016321.2.
DR PDB; 3HD6; X-ray; 2.10 A; A=2-479.
DR PDBsum; 3HD6; -.
DR AlphaFoldDB; Q9UBD6; -.
DR SMR; Q9UBD6; -.
DR BioGRID; 119552; 28.
DR DIP; DIP-59334N; -.
DR IntAct; Q9UBD6; 16.
DR STRING; 9606.ENSP00000268122; -.
DR DrugBank; DB09326; Ammonia N-13.
DR TCDB; 1.A.11.4.1; the ammonium transporter channel (amt) family.
DR GlyGen; Q9UBD6; 1 site.
DR iPTMnet; Q9UBD6; -.
DR PhosphoSitePlus; Q9UBD6; -.
DR BioMuta; RHCG; -.
DR DMDM; 74734928; -.
DR jPOST; Q9UBD6; -.
DR MassIVE; Q9UBD6; -.
DR PaxDb; Q9UBD6; -.
DR PeptideAtlas; Q9UBD6; -.
DR PRIDE; Q9UBD6; -.
DR ProteomicsDB; 83949; -.
DR Antibodypedia; 28582; 288 antibodies from 32 providers.
DR DNASU; 51458; -.
DR Ensembl; ENST00000268122.9; ENSP00000268122.4; ENSG00000140519.14.
DR GeneID; 51458; -.
DR KEGG; hsa:51458; -.
DR MANE-Select; ENST00000268122.9; ENSP00000268122.4; NM_016321.3; NP_057405.1.
DR UCSC; uc002bnz.4; human.
DR CTD; 51458; -.
DR DisGeNET; 51458; -.
DR GeneCards; RHCG; -.
DR HGNC; HGNC:18140; RHCG.
DR HPA; ENSG00000140519; Group enriched (esophagus, vagina).
DR MIM; 605381; gene.
DR neXtProt; NX_Q9UBD6; -.
DR OpenTargets; ENSG00000140519; -.
DR PharmGKB; PA134876043; -.
DR VEuPathDB; HostDB:ENSG00000140519; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_0_0_1; -.
DR InParanoid; Q9UBD6; -.
DR OMA; ENCFEDE; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9UBD6; -.
DR TreeFam; TF314450; -.
DR PathwayCommons; Q9UBD6; -.
DR Reactome; R-HSA-444411; Rhesus glycoproteins mediate ammonium transport.
DR SignaLink; Q9UBD6; -.
DR BioGRID-ORCS; 51458; 6 hits in 1057 CRISPR screens.
DR ChiTaRS; RHCG; human.
DR EvolutionaryTrace; Q9UBD6; -.
DR GeneWiki; RHCG; -.
DR GenomeRNAi; 51458; -.
DR Pharos; Q9UBD6; Tbio.
DR PRO; PR:Q9UBD6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UBD6; protein.
DR Bgee; ENSG00000140519; Expressed in lower esophagus mucosa and 111 other tissues.
DR ExpressionAtlas; Q9UBD6; baseline and differential.
DR Genevisible; Q9UBD6; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015837; P:amine transport; NAS:UniProtKB.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006873; P:cellular ion homeostasis; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; NAS:UniProtKB.
DR GO; GO:0042592; P:homeostatic process; NAS:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
DR GO; GO:0070634; P:transepithelial ammonium transport; IDA: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 1: Evidence at protein level;
KW 3D-structure; 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_0000283577"
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:0000269|PubMed:20457942"
FT VARIANT 202
FT /note="R -> C (in dbSNP:rs17807723)"
FT /id="VAR_031496"
FT MUTAGEN 74
FT /note="F->L: Reduction of ammonia transport."
FT /evidence="ECO:0000269|PubMed:16580862"
FT MUTAGEN 137
FT /note="V->I: Reduction of ammonia transport."
FT /evidence="ECO:0000269|PubMed:16580862"
FT MUTAGEN 177
FT /note="D->N: Loss of function."
FT /evidence="ECO:0000269|PubMed:16477434"
FT MUTAGEN 235
FT /note="F->V: Reduction of ammonia transport."
FT /evidence="ECO:0000269|PubMed:16580862"
FT CONFLICT 242
FT /note="H -> R (in Ref. 6; AAP81044)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="N -> D (in Ref. 6; AAP81044)"
FT /evidence="ECO:0000305"
FT HELIX 10..29
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3HD6"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 122..142
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 148..170
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 215..235
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 243..270
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 293..299
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 303..332
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 385..416
FT /evidence="ECO:0007829|PDB:3HD6"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3HD6"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3HD6"
SQ SEQUENCE 479 AA; 53179 MW; E5D8024D720D4589 CRC64;
MAWNTNLRWR LPLTCLLLQV IMVILFGVFV RYDFEADAHW WSERTHKNLS DMENEFYYRY
PSFQDVHVMV FVGFGFLMTF LQRYGFSAVG FNFLLAAFGI QWALLMQGWF HFLQDRYIVV
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 FNGDWTARTQ GKFQIYGLLV TLAMALMGGI IVGLILRLPF
WGQPSDENCF EDAVYWEMPE GNSTVYIPED PTFKPSGPSV PSVPMVSPLP MASSVPLVP
