ID RHAG_HUMAN Reviewed; 409 AA.
AC Q02094; B2R8T8; O43514; O43515; Q7L8L3; Q9H454;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-NOV-2024, entry version 197.
DE RecName: Full=Ammonium transporter Rh type A {ECO:0000305};
DE AltName: Full=Erythrocyte membrane glycoprotein Rh50;
DE AltName: Full=Erythrocyte plasma membrane 50 kDa glycoprotein;
DE Short=Rh50A;
DE AltName: Full=Rhesus blood group family type A glycoprotein;
DE Short=Rh family type A glycoprotein;
DE Short=Rh type A glycoprotein;
DE AltName: Full=Rhesus blood group-associated ammonia channel;
DE AltName: Full=Rhesus blood group-associated glycoprotein;
DE AltName: CD_antigen=CD241;
GN Name=RHAG {ECO:0000312|HGNC:HGNC:10006}; Synonyms=RH50;
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 [MRNA] (ISOFORM 1), AND VARIANT ASP-242.
RC TISSUE=Bone marrow, and Liver;
RX PubMed=1417776; DOI=10.1042/bj2870223;
RA Ridgwell K., Spurr N.K., Laguda B., Macgeoch C., Avent N.D., Tanner M.J.A.;
RT "Isolation of cDNA clones for a 50 kDa glycoprotein of the human
RT erythrocyte membrane associated with Rh (rhesus) blood-group antigen
RT expression.";
RL Biochem. J. 287:223-228(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=9442063; DOI=10.1074/jbc.273.4.2207;
RA Huang C.-H.;
RT "The human Rh50 glycoprotein gene. Structural organization and associated
RT splicing defect resulting in Rh(null) disease.";
RL J. Biol. Chem. 273:2207-2213(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-270.
RC TISSUE=Heart;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] OF 1-52, AND TISSUE SPECIFICITY.
RX PubMed=9473510; DOI=10.1006/bbrc.1997.8023;
RA Iwamoto S., Omi T., Yamasaki M., Okuda H., Kawano M., Kajii E.;
RT "Identification of 5' flanking sequence of RH50 gene and the core region
RT for erythroid-specific expression.";
RL Biochem. Biophys. Res. Commun. 243:233-240(1998).
RN [7]
RP PROTEIN SEQUENCE OF 1-39.
RX PubMed=3146980; DOI=10.1042/bj2561043;
RA Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J., Kumpel B.;
RT "Protein-sequence studies on Rh-related polypeptides suggest the presence
RT of at least two groups of proteins which associate in the human red-cell
RT membrane.";
RL Biochem. J. 256:1043-1046(1988).
RN [8]
RP FUNCTION.
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, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11861637; DOI=10.1074/jbc.c200060200;
RA Westhoff C.M., Ferreri-Jacobia M., Mak D.-O.D., Foskett J.K.;
RT "Identification of the erythrocyte Rh blood group glycoprotein as a
RT mammalian ammonium transporter.";
RL J. Biol. Chem. 277:12499-12502(2002).
RN [10]
RP FUNCTION.
RX PubMed=12130520;
RA Mouro-Chanteloup I., D'Ambrosio A.M., Gane P., Le Van Kim C., Raynal V.,
RA Dhermy D., Cartron J.P., Colin Y.;
RT "Cell-surface expression of RhD blood group polypeptide is
RT posttranscriptionally regulated by the RhAG glycoprotein.";
RL Blood 100:1038-1047(2002).
RN [11]
RP CHARACTERIZATION.
RX PubMed=14966114; DOI=10.1074/jbc.m311853200;
RA Westhoff C.M., Siegel D.L., Burd C.G., Foskett J.K.;
RT "Mechanism of genetic complementation of ammonium transport in yeast by
RT human erythrocyte Rh-associated glycoprotein.";
RL J. Biol. Chem. 279:17443-17448(2004).
RN [12]
RP FUNCTION.
RX PubMed=15572441; DOI=10.1073/pnas.0403704101;
RA Ripoche P., Bertrand O., Gane P., Birkenmeier C., Colin Y., Cartron J.P.;
RT "Human Rhesus-associated glycoprotein mediates facilitated transport of
RT NH(3) into red blood cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17222-17227(2004).
RN [13]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15856280; DOI=10.1007/s00424-005-1381-y;
RA Benjelloun F., Bakouh N., Fritsch J., Hulin P., Lipecka J., Edelman A.,
RA Planelles G., Thomas S.R., Cherif-Zahar B.;
RT "Expression of the human erythroid Rh glycoprotein (RhAG) enhances both NH3
RT and NH4+ transport in HeLa cells.";
RL Pflugers Arch. 450:155-167(2005).
RN [14]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=17712059; DOI=10.1096/fj.07-9097com;
RA Endeward V., Cartron J.P., Ripoche P., Gros G.;
RT "RhAG protein of the Rhesus complex is a CO2 channel in the human red cell
RT membrane.";
RL FASEB J. 22:64-73(2008).
RN [15]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=19273840; DOI=10.1073/pnas.0813231106;
RA Musa-Aziz R., Chen L.M., Pelletier M.F., Boron W.F.;
RT "Relative CO2/NH3 selectivities of AQP1, AQP4, AQP5, AmtB, and RhAG.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5406-5411(2009).
RN [16]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=24077989; DOI=10.1007/s00232-013-9593-0;
RA Geyer R.R., Parker M.D., Toye A.M., Boron W.F., Musa-Aziz R.;
RT "Relative CO(2)/NH(3) permeabilities of human RhAG, RhBG and RhCG.";
RL J. Membr. Biol. 246:915-926(2013).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=27247322; DOI=10.3324/haematol.2016.146209;
RA Satchwell T.J., Bell A.J., Hawley B.R., Pellegrin S., Mordue K.E.,
RA van Deursen C.T., Braak N.H., Huls G., Leers M.P., Overwater E.,
RA Tamminga R.Y., van der Zwaag B., Fermo E., Bianchi P., van Wijk R.,
RA Toye A.M.;
RT "Severe Ankyrin-R deficiency results in impaired surface retention and
RT lysosomal degradation of RhAG in human erythroblasts.";
RL Haematologica 101:1018-1027(2016).
RN [18]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=26354748; DOI=10.1152/ajpcell.00085.2015;
RA Caner T., Abdulnour-Nakhoul S., Brown K., Islam M.T., Hamm L.L.,
RA Nakhoul N.L.;
RT "Mechanisms of ammonia and ammonium transport by rhesus-associated
RT glycoproteins.";
RL Am. J. Physiol. 309:C747-C758(2015).
RN [19] {ECO:0007744|PDB:7UZQ, ECO:0007744|PDB:7V0K, ECO:0007744|PDB:7V0S, ECO:0007744|PDB:8CRT, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL, ECO:0007744|PDB:8CSX, ECO:0007744|PDB:8CTE}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.17 ANGSTROMS), FUNCTION, SUBUNIT,
RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH RHCE AND GYPB.
RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w;
RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T.,
RA Clarke O.B.;
RT "Architecture of the human erythrocyte ankyrin-1 complex.";
RL Nat. Struct. Mol. Biol. 29:706-718(2022).
RN [20]
RP VARIANT RHN ASN-79.
RX PubMed=8563755; DOI=10.1038/ng0296-168;
RA Cherif-Zahar B., Raynal V., Gane P., Mattei M.-G., Bailly P., Gibbs B.,
RA Colin Y., Cartron J.-P.;
RT "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-
RT deficiency.";
RL Nat. Genet. 12:168-173(1996).
RN [21]
RP VARIANT RHN GLU-279.
RX PubMed=9454778;
RA Hyland C.A., Cherif-Zahar B., Cowley N., Raynal V., Parkes J., Saul A.,
RA Cartron J.-P.;
RT "A novel single missense mutation identified along the RH50 gene in a
RT composite heterozygous Rhnull blood donor of the regulator type.";
RL Blood 91:1458-1463(1998).
RN [22]
RP VARIANT RHN GLU-279.
RX PubMed=9716608;
RA Huang C.-H., Liu Z., Cheng G., Chen Y.;
RT "Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans
RT to a Gly279-->Glu missense mutation in the conserved transmembrane
RT segment.";
RL Blood 92:1776-1784(1998).
RN [23]
RP VARIANTS RHN ARG-280 AND VAL-380, AND VARIANT ILE-270.
RX PubMed=10467273;
RX DOI=10.1002/(sici)1096-8652(199909)62:1<25::aid-ajh5>3.0.co;2-k;
RA Huang C.-H., Cheng G., Liu Z., Chen Y., Reid M.E., Halverson G., Okubo Y.;
RT "Molecular basis for Rh(null) syndrome: identification of three new
RT missense mutations in the Rh50 glycoprotein gene.";
RL Am. J. Hematol. 62:25-32(1999).
RN [24]
RP INVOLVEMENT IN OHST, VARIANTS OHST ARG-61 AND SER-65, CHARACTERIZATION OF
RP VARIANTS OHST ARG-61 AND SER-65, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RX PubMed=18931342; DOI=10.1182/blood-2008-07-171140;
RA Bruce L.J., Guizouarn H., Burton N.M., Gabillat N., Poole J., Flatt J.F.,
RA Brady R.L., Borgese F., Delaunay J., Stewart G.W.;
RT "The monovalent cation leak in overhydrated stomatocytic red blood cells
RT results from amino acid substitutions in the Rh-associated glycoprotein.";
RL Blood 113:1350-1357(2009).
RN [25]
RP VARIANTS GLU-106; GLN-164 AND LEU-227, AND FUNCTION.
RX PubMed=19744193; DOI=10.1111/j.1423-0410.2009.01243.x;
RA Tilley L., Green C., Poole J., Gaskell A., Ridgwell K., Burton N.M.,
RA Uchikawa M., Tsuneyama H., Ogasawara K., Akkoek C.A., Daniels G.;
RT "A new blood group system, RHAG: three antigens resulting from amino acid
RT substitutions in the Rh-associated glycoprotein.";
RL Vox Sang. 98:151-159(2010).
RN [26]
RP VARIANT OHST SER-65, CHARACTERIZATION OF VARIANT OHST SER-65, FUNCTION, AND
RP TRANSPORTER ACTIVITY.
RX PubMed=21849667; DOI=10.1152/ajpcell.00054.2011;
RA Stewart A.K., Shmukler B.E., Vandorpe D.H., Rivera A., Heneghan J.F.,
RA Li X., Hsu A., Karpatkin M., O'Neill A.F., Bauer D.E., Heeney M.M.,
RA John K., Kuypers F.A., Gallagher P.G., Lux S.E., Brugnara C.,
RA Westhoff C.M., Alper S.L.;
RT "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant
RT RhAG F65S.";
RL Am. J. Physiol. 301:C1325-C1343(2011).
RN [27]
RP CHARACTERIZATION OF VARIANT OHST SER-65, FUNCTION, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=22012326; DOI=10.1152/ajpcell.00092.2011;
RA Genetet S., Ripoche P., Picot J., Bigot S., Delaunay J., Armari-Alla C.,
RA Colin Y., Mouro-Chanteloup I.;
RT "Human RhAG ammonia channel is impaired by the Phe65Ser mutation in
RT overhydrated stomatocytic red cells.";
RL Am. J. Physiol. 302:C419-C428(2012).
RN [28]
RP VARIANT ILE-270.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex
CC involved in the stability and shape of the erythrocyte membrane
CC (PubMed:35835865). Heterotrimer with RHCE (RHAG)2(RHCE), that
CC transports ammonium and its related derivative methylammonium, in both
CC neutral and ionic forms, across the erythrocyte membrane
CC (PubMed:11062476, PubMed:11861637, PubMed:15572441, PubMed:15856280,
CC PubMed:19273840, PubMed:21849667, PubMed:22012326, PubMed:24077989,
CC PubMed:26354748). The transport of NH4(+) is electrogenic and masks the
CC NH3 transport (PubMed:26354748). Also, may act as a CO2 channel
CC (PubMed:17712059, PubMed:19273840, PubMed:24077989). In vitro, leaks
CC monovalent cations (PubMed:18931342, PubMed:21849667). Moreover in
CC erythrocyte, regulates RHD membrane expression (PubMed:12130520) and is
CC associated with rhesus blood group antigen expression (PubMed:12130520,
CC PubMed:19744193). {ECO:0000269|PubMed:11062476,
CC ECO:0000269|PubMed:11861637, ECO:0000269|PubMed:12130520,
CC ECO:0000269|PubMed:15572441, ECO:0000269|PubMed:15856280,
CC ECO:0000269|PubMed:17712059, ECO:0000269|PubMed:18931342,
CC ECO:0000269|PubMed:19273840, ECO:0000269|PubMed:19744193,
CC ECO:0000269|PubMed:21849667, ECO:0000269|PubMed:22012326,
CC ECO:0000269|PubMed:24077989, ECO:0000269|PubMed:26354748,
CC ECO:0000269|PubMed:35835865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=methylamine(out) = methylamine(in); Xref=Rhea:RHEA:74391,
CC ChEBI:CHEBI:59338; Evidence={ECO:0000269|PubMed:15856280,
CC ECO:0000269|PubMed:21849667, ECO:0000269|PubMed:26354748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:15856280,
CC ECO:0000269|PubMed:19273840, ECO:0000269|PubMed:21849667,
CC ECO:0000269|PubMed:24077989, ECO:0000269|PubMed:26354748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2(out) = CO2(in); Xref=Rhea:RHEA:74891, ChEBI:CHEBI:16526;
CC Evidence={ECO:0000269|PubMed:17712059, ECO:0000269|PubMed:19273840,
CC ECO:0000269|PubMed:24077989};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for methylamine {ECO:0000269|PubMed:11861637};
CC -!- SUBUNIT: Homodimer (PubMed:35835865). Heterotrimer; a RHCE monomer
CC interacts with a RHAG homodimer (PubMed:35835865). Component of the
CC ankyrin-1 complex in the erythrocyte, composed of ANK1, RHCE, RHAG,
CC SLC4A1, EPB42, GYPA, GYPB and AQP1 (PubMed:35835865). Interacts with
CC GYPB (via the N-terminal); this interaction bridges the (RHAG)2(RHCE)
CC heterotrimer with the SLC4A1 Band 3 I dimer complexed with GYPA
CC (PubMed:35835865). {ECO:0000269|PubMed:35835865}.
CC -!- INTERACTION:
CC Q02094; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-14772355, EBI-852194;
CC Q02094; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-14772355, EBI-781551;
CC Q02094; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-14772355, EBI-18304435;
CC Q02094; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-14772355, EBI-19027521;
CC Q02094; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-14772355, EBI-13356252;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15856280,
CC ECO:0000269|PubMed:18931342, ECO:0000269|PubMed:22012326,
CC ECO:0000269|PubMed:27247322}; Multi-pass membrane protein.
CC Note=Localization at the plasma membrane is regulated by ANK1.
CC {ECO:0000269|PubMed:27247322}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02094-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02094-2; Sequence=VSP_047629, VSP_047630;
CC -!- TISSUE SPECIFICITY: Erythrocytes. {ECO:0000269|PubMed:18931342,
CC ECO:0000269|PubMed:22012326, ECO:0000269|PubMed:9473510}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18931342,
CC ECO:0000269|PubMed:22012326}.
CC -!- DISEASE: Regulator type Rh-null hemolytic anemia (RHN) [MIM:268150]:
CC Form of chronic hemolytic anemia in which the red blood cells have a
CC stomatocytosis and spherocytosis morphology, an increased osmotic
CC fragility, an altered ion transport system, and abnormal membrane
CC phospholipid organization. {ECO:0000269|PubMed:10467273,
CC ECO:0000269|PubMed:8563755, ECO:0000269|PubMed:9454778,
CC ECO:0000269|PubMed:9716608}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Overhydrated hereditary stomatocytosis (OHST) [MIM:185000]: An
CC autosomal dominant disorder of red cell membrane permeability to
CC monovalent cations, characterized by macrocytic hemolytic anemia of
CC fluctuating severity, circulating erythrocytes with slit-like lucencies
CC (stomata) evident on fixed, stained peripheral blood smears. OHST red
CC cells exhibit cation leak, resulting in elevated cell sodium content
CC with reduced potassium content. The disease is marked by splenomegaly
CC or hepatosplenomegaly, cholelithiasis and a strong tendency for iron
CC overload. {ECO:0000269|PubMed:18931342, ECO:0000269|PubMed:21849667,
CC ECO:0000269|PubMed:22012326}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Several mechanisms of transport has been proposed, namely
CC electroneutral NH3 transport (PubMed:15572441, PubMed:19273840) and
CC electroneutral NH4(+)/H(+) exchange (PubMed:11861637, PubMed:15572441,
CC PubMed:19273840). However, Caner T. et al demonstrates that RHAG is
CC unlikely to be NH4(+)/H(+) exchanger, but transports the ionic NH4(+)
CC and the neutral NH3 species and that the transport of NH4(+) is
CC electrogenic (PubMed:26354748). {ECO:0000269|PubMed:11861637,
CC ECO:0000269|PubMed:15572441, ECO:0000269|PubMed:19273840,
CC ECO:0000269|PubMed:26354748}.
CC ---------------------------------------------------------------------------
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DR EMBL; X64594; CAA45883.1; -; mRNA.
DR EMBL; AF031548; AAC04247.1; -; mRNA.
DR EMBL; AF031549; AAC04248.1; -; mRNA.
DR EMBL; AF237387; AAF78209.1; -; Genomic_DNA.
DR EMBL; AF237382; AAF78209.1; JOINED; Genomic_DNA.
DR EMBL; AF237383; AAF78209.1; JOINED; Genomic_DNA.
DR EMBL; AF237384; AAF78209.1; JOINED; Genomic_DNA.
DR EMBL; AF237385; AAF78209.1; JOINED; Genomic_DNA.
DR EMBL; AF237386; AAF78209.1; JOINED; Genomic_DNA.
DR EMBL; AK313505; BAG36285.1; -; mRNA.
DR EMBL; AL121950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04337.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04338.1; -; Genomic_DNA.
DR CCDS; CCDS4927.1; -. [Q02094-1]
DR PIR; S29124; S29124.
DR RefSeq; NP_000315.2; NM_000324.2. [Q02094-1]
DR PDB; 7UZQ; EM; 2.17 A; L/Q=1-409.
DR PDB; 7V0K; EM; 2.40 A; L/Q=1-409.
DR PDB; 7V0S; EM; 2.50 A; L/Q=1-409.
DR PDB; 8CRT; EM; 3.00 A; L/Q=1-409.
DR PDB; 8CS9; EM; 2.74 A; L/Q=1-409.
DR PDB; 8CSL; EM; 25.00 A; L/Q=1-409.
DR PDB; 8CSX; EM; 2.40 A; L/Q=1-409.
DR PDB; 8CTE; EM; 2.90 A; L/Q=1-409.
DR PDBsum; 7UZQ; -.
DR PDBsum; 7V0K; -.
DR PDBsum; 7V0S; -.
DR PDBsum; 8CRT; -.
DR PDBsum; 8CS9; -.
DR PDBsum; 8CSL; -.
DR PDBsum; 8CSX; -.
DR PDBsum; 8CTE; -.
DR AlphaFoldDB; Q02094; -.
DR EMDB; EMD-26916; -.
DR EMDB; EMD-26943; -.
DR EMDB; EMD-26949; -.
DR EMDB; EMD-26958; -.
DR EMDB; EMD-26960; -.
DR EMDB; EMD-26965; -.
DR EMDB; EMD-26974; -.
DR EMDB; EMD-26988; -.
DR SMR; Q02094; -.
DR BioGRID; 111937; 8.
DR IntAct; Q02094; 5.
DR STRING; 9606.ENSP00000360217; -.
DR TCDB; 1.A.11.4.3; the ammonium transporter channel (amt) family.
DR GlyCosmos; Q02094; 3 sites, 1 glycan.
DR GlyGen; Q02094; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q02094; -.
DR PhosphoSitePlus; Q02094; -.
DR BioMuta; RHAG; -.
DR DMDM; 218511807; -.
DR jPOST; Q02094; -.
DR MassIVE; Q02094; -.
DR PaxDb; 9606-ENSP00000360217; -.
DR PeptideAtlas; Q02094; -.
DR ProteomicsDB; 58049; -. [Q02094-1]
DR Pumba; Q02094; -.
DR Antibodypedia; 17000; 65 antibodies from 23 providers.
DR DNASU; 6005; -.
DR Ensembl; ENST00000371175.10; ENSP00000360217.4; ENSG00000112077.18. [Q02094-1]
DR Ensembl; ENST00000646939.1; ENSP00000494709.1; ENSG00000112077.18. [Q02094-2]
DR GeneID; 6005; -.
DR KEGG; hsa:6005; -.
DR MANE-Select; ENST00000371175.10; ENSP00000360217.4; NM_000324.3; NP_000315.2.
DR UCSC; uc003ozk.5; human. [Q02094-1]
DR AGR; HGNC:10006; -.
DR CTD; 6005; -.
DR DisGeNET; 6005; -.
DR GeneCards; RHAG; -.
DR HGNC; HGNC:10006; RHAG.
DR HPA; ENSG00000112077; Tissue enriched (bone).
DR MalaCards; RHAG; -.
DR MIM; 180297; gene.
DR MIM; 185000; phenotype.
DR MIM; 268150; phenotype.
DR neXtProt; NX_Q02094; -.
DR OpenTargets; ENSG00000112077; -.
DR Orphanet; 3203; Overhydrated hereditary stomatocytosis.
DR Orphanet; 71275; Rh deficiency syndrome.
DR PharmGKB; PA34381; -.
DR VEuPathDB; HostDB:ENSG00000112077; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR InParanoid; Q02094; -.
DR OMA; VYWEVPI; -.
DR OrthoDB; 5483564at2759; -.
DR PhylomeDB; Q02094; -.
DR TreeFam; TF314450; -.
DR PathwayCommons; Q02094; -.
DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-HSA-444411; Rhesus glycoproteins mediate ammonium transport.
DR Reactome; R-HSA-5619042; Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN).
DR SignaLink; Q02094; -.
DR SIGNOR; Q02094; -.
DR BioGRID-ORCS; 6005; 3 hits in 1153 CRISPR screens.
DR ChiTaRS; RHAG; human.
DR GeneWiki; RHAG; -.
DR GenomeRNAi; 6005; -.
DR Pharos; Q02094; Tbio.
DR PRO; PR:Q02094; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q02094; protein.
DR Bgee; ENSG00000112077; Expressed in trabecular bone tissue and 116 other cell types or tissues.
DR ExpressionAtlas; Q02094; baseline and differential.
DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008519; F:ammonium channel activity; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; IPI:UniProtKB.
DR GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022840; F:leak channel activity; IDA:UniProtKB.
DR GO; GO:0015200; F:methylammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
DR GO; GO:0035378; P:carbon dioxide transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IDA:UniProtKB.
DR GO; GO:0072489; P:methylammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR FunFam; 1.10.3430.10:FF:000001; Ammonium transporter Rh type C; 1.
DR Gene3D; 1.10.3430.10; Ammonium transporter AmtB like domains; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR002229; RhesusRHD.
DR PANTHER; PTHR11730; AMMONIUM TRANSPORTER; 1.
DR PANTHER; PTHR11730:SF32; AMMONIUM TRANSPORTER RH TYPE A; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR PRINTS; PR00342; RHESUSRHD.
DR SUPFAM; SSF111352; Ammonium transporter; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Ammonia transport;
KW Direct protein sequencing; Disease variant; Glycoprotein;
KW Hereditary hemolytic anemia; Membrane; Proteomics identification;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..409
FT /note="Ammonium transporter Rh type A"
FT /id="PRO_0000168199"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 316..351
FT /note="PLFTTKLRIHDTCGVHNLHGLPGVVGGLAGIVAVAM -> VYGHAGSCTGFL
FT YRNSSCWRSDDRFNSKVASLGTAI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9442063"
FT /id="VSP_047629"
FT VAR_SEQ 352..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9442063"
FT /id="VSP_047630"
FT VARIANT 61
FT /note="I -> R (in OHST; strongly enhances monovalent cation
FT leak; dbSNP:rs863225469)"
FT /evidence="ECO:0000269|PubMed:18931342"
FT /id="VAR_076283"
FT VARIANT 65
FT /note="F -> S (in OHST; enhances monovalent cation leak;
FT decreases ammonium fluxes; highly decreases STOM
FT expression; decreases membrane expression; no effect on
FT water permeability; dbSNP:rs863225468)"
FT /evidence="ECO:0000269|PubMed:18931342,
FT ECO:0000269|PubMed:21849667, ECO:0000269|PubMed:22012326"
FT /id="VAR_076284"
FT VARIANT 79
FT /note="S -> N (in RHN; dbSNP:rs121918586)"
FT /evidence="ECO:0000269|PubMed:8563755"
FT /id="VAR_006921"
FT VARIANT 106
FT /note="Q -> E (in Duclos or RHAG1 antigen (030001);
FT dbSNP:rs1180686517)"
FT /evidence="ECO:0000269|PubMed:19744193"
FT /id="VAR_076285"
FT VARIANT 164
FT /note="K -> Q (in DSLK or RHAG3 antigen (030003);
FT dbSNP:rs144305805)"
FT /evidence="ECO:0000269|PubMed:19744193"
FT /id="VAR_076286"
FT VARIANT 227
FT /note="S -> L (in Ol(a) or RHAG2 antigen (030002);
FT dbSNP:rs902283342)"
FT /evidence="ECO:0000269|PubMed:19744193"
FT /id="VAR_076287"
FT VARIANT 242
FT /note="N -> D (in dbSNP:rs1058063)"
FT /evidence="ECO:0000269|PubMed:1417776"
FT /id="VAR_047999"
FT VARIANT 270
FT /note="V -> I (in dbSNP:rs16879498)"
FT /evidence="ECO:0000269|PubMed:10467273,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:27535533"
FT /id="VAR_015855"
FT VARIANT 279
FT /note="G -> E (in RHN; dbSNP:rs121918587)"
FT /evidence="ECO:0000269|PubMed:9454778,
FT ECO:0000269|PubMed:9716608"
FT /id="VAR_015856"
FT VARIANT 280
FT /note="G -> R (in RHN; dbSNP:rs104893987)"
FT /evidence="ECO:0000269|PubMed:10467273"
FT /id="VAR_015857"
FT VARIANT 380
FT /note="G -> V (in RHN; dbSNP:rs121918589)"
FT /evidence="ECO:0000269|PubMed:10467273"
FT /id="VAR_015858"
FT CONFLICT 2
FT /note="R -> C (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="N -> P (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:7UZQ"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7V0S"
FT HELIX 138..161
FT /evidence="ECO:0007829|PDB:7UZQ"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 205..227
FT /evidence="ECO:0007829|PDB:7UZQ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:8CTE"
FT HELIX 234..261
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:7UZQ"
FT TURN 283..288
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 292..320
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:7UZQ"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 358..383
FT /evidence="ECO:0007829|PDB:7UZQ"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:7UZQ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:7UZQ"
SQ SEQUENCE 409 AA; 44198 MW; F6F024399CC0C88D CRC64;
MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL YPLFQDVHVM
IFVGFGFLMT FLKKYGFSSV GINLLVAALG LQWGTIVQGI LQSQGQKFNI GIKNMINADF
SAATVLISFG AVLGKTSPTQ MLIMTILEIV FFAHNEYLVS EIFKASDIGA SMTIHAFGAY
FGLAVAGILY RSGLRKGHEN EESAYYSDLF AMIGTLFLWM FWPSFNSAIA EPGDKQCRAI
VNTYFSLAAC VLTAFAFSSL VEHRGKLNMV HIQNATLAGG VAVGTCADMA IHPFGSMIIG
SIAGMVSVLG YKFLTPLFTT KLRIHDTCGV HNLHGLPGVV GGLAGIVAVA MGASNTSMAM
QAAALGSSIG TAVVGGLMTG LILKLPLWGQ PSDQNCYDDS VYWKVPKTR
//
