RHGA_DICDI
ID RHGA_DICDI Reviewed; 527 AA.
AC Q9NIV0; Q54R49;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Rhesus-like glycoprotein A;
DE AltName: Full=Rh50-like protein rhgA;
GN Name=rhgA; ORFNames=DDB_G0283389;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11220631; DOI=10.1007/s002510000279;
RA Benghezal M., Gotthardt D., Cornillon S., Cosson P.;
RT "Localization of the Rh50-like protein to the contractile vacuole in
RT Dictyostelium.";
RL Immunogenetics 52:284-288(2001).
RN [4]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH AP1G1, AND
RP MUTAGENESIS OF 478-ASP--GLU-482.
RX PubMed=16478785; DOI=10.1242/jcs.02808;
RA Mercanti V., Blanc C., Lefkir Y., Cosson P., Letourneur F.;
RT "Acidic clusters target transmembrane proteins to the contractile vacuole
RT in Dictyostelium cells.";
RL J. Cell Sci. 119:837-845(2006).
RN [5]
RP IDENTIFICATION.
RX PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL Genome Biol. 8:R144.1-R144.15(2007).
CC -!- FUNCTION: May be a carbon dioxide/bicarbonate transporter.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ap1g1. {ECO:0000269|PubMed:16478785}.
CC -!- SUBCELLULAR LOCATION: Contractile vacuole {ECO:0000269|PubMed:11220631,
CC ECO:0000269|PubMed:16478785}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Acidic motifs (DDEEE) in the C-terminal domain are necessary
CC and sufficient for efficient transport to the contractile vacuole.
CC -!- DISRUPTION PHENOTYPE: Does not appear to exhibit a phenotype related to
CC osmoregulation perhaps due to functional redundancy with rhgB.
CC {ECO:0000269|PubMed:11220631, ECO:0000269|PubMed:16478785}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
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DR EMBL; AF193811; AAF63243.1; -; mRNA.
DR EMBL; AF510714; AAP47143.1; -; Genomic_DNA.
DR EMBL; AAFI02000055; EAL65679.1; -; Genomic_DNA.
DR RefSeq; XP_639042.1; XM_633950.1.
DR AlphaFoldDB; Q9NIV0; -.
DR SMR; Q9NIV0; -.
DR STRING; 44689.DDB0191180; -.
DR TCDB; 1.A.11.4.6; the ammonium transporter channel (amt) family.
DR PaxDb; Q9NIV0; -.
DR ABCD; Q9NIV0; 1 sequenced antibody.
DR EnsemblProtists; EAL65679; EAL65679; DDB_G0283389.
DR GeneID; 8624067; -.
DR KEGG; ddi:DDB_G0283389; -.
DR dictyBase; DDB_G0283389; rhgA.
DR eggNOG; KOG3796; Eukaryota.
DR HOGENOM; CLU_021386_1_0_1; -.
DR InParanoid; Q9NIV0; -.
DR OMA; EITIFAC; -.
DR PhylomeDB; Q9NIV0; -.
DR Reactome; R-DDI-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-DDI-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-DDI-444411; Rhesus glycoproteins mediate ammonium transport.
DR PRO; PR:Q9NIV0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:dictyBase.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:dictyBase.
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 Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..527
FT /note="Rhesus-like glycoprotein A"
FT /id="PRO_0000390404"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..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..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 471..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 478..482
FT /note="DDEEE->AAAAA: Decreased interaction with AP1G1, loss
FT of transport to the contractile vacuole and mislocalization
FT to the plasma membrane and small vesicular structures."
FT /evidence="ECO:0000269|PubMed:16478785"
SQ SEQUENCE 527 AA; 58360 MW; 88E1EC35BAAC8C9D CRC64;
MTHNDDDHKW VTTKRKEPIF FTVILFIFQI FMIICFAALT GYDTNKNYTG SENPDEFKGG
EVQERVNNFY GYFRDINIMI FFGFGFLMTF LRRYGYSALG YTFIISALVS QWSVLLNGFF
EAWSHSNKHG EFPSTWEFSM DSLLQGFFCS GSVMISYGAI LGRVTPLHML IMGIIEPIFF
FLNVFIGEMN LEAIDVGGGM YIHLFGSVFG LTVAWFLTDR KSKECTDNAP SYSGDNFAMA
GTLFLWMMWP SFNAAIAPLG EPQFRAIANT FLSLTGSTVA TFIVSRLFSH LGNKLDMVHV
QNSSLAGGVV QGCIAHMNIN PGGAIAMGFI AGTISVCGYL FITPKVQRKL HIQDTCGILN
LHCIPGFLGS IAAIFAAIKG LNNPNMYSKV EFEQIFRAGD SQASANLIAT MVSIGLGIVG
GLLVGVILLQ LKKIKGLKSK EYYQDSAFWI LPIDYPKDVA TVVALNNAAT SEDTAGGDDE
EEGVGKEHGA VEMGKHNRIV QPKQDNKYHK QLPSDDEEED EFKQEPI
