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Rhesus-like glycoprotein A (Rh50-like protein rhgA)

 RHGA_DICDI              Reviewed;         527 AA.
Q9NIV0; Q54R49;
15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 94.
RecName: Full=Rhesus-like glycoprotein A;
AltName: Full=Rh50-like protein rhgA;
Name=rhgA; ORFNames=DDB_G0283389;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AX2;
PubMed=10852913; DOI=10.1074/jbc.M003353200;
Liu Z., Chen Y., Mo R., Hui C.-C., Cheng J.-F., Mohandas N.,
Huang C.-H.;
"Characterization of human RhCG and mouse Rhcg as novel nonerythroid
Rh glycoprotein homologues predominantly expressed in kidney and
testis.";
J. Biol. Chem. 275:25641-25651(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[3]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=11220631; DOI=10.1007/s002510000279;
Benghezal M., Gotthardt D., Cornillon S., Cosson P.;
"Localization of the Rh50-like protein to the contractile vacuole in
Dictyostelium.";
Immunogenetics 52:284-288(2001).
[4]
SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH AP1G1,
AND MUTAGENESIS OF 478-ASP--GLU-482.
PubMed=16478785; DOI=10.1242/jcs.02808;
Mercanti V., Blanc C., Lefkir Y., Cosson P., Letourneur F.;
"Acidic clusters target transmembrane proteins to the contractile
vacuole in Dictyostelium cells.";
J. Cell Sci. 119:837-845(2006).
[5]
IDENTIFICATION.
PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
"High-throughput analysis of spatio-temporal dynamics in
Dictyostelium.";
Genome Biol. 8:R144.1-R144.15(2007).
-!- FUNCTION: May be a carbon dioxide/bicarbonate transporter.
{ECO:0000250}.
-!- SUBUNIT: Interacts with ap1g1. {ECO:0000269|PubMed:16478785}.
-!- SUBCELLULAR LOCATION: Contractile vacuole
{ECO:0000269|PubMed:11220631, ECO:0000269|PubMed:16478785}.
Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- DOMAIN: Acidic motifs (DDEEE) in the C-terminal domain are
necessary and sufficient for efficient transport to the
contractile vacuole.
-!- DISRUPTION PHENOTYPE: Does not appear to exhibit a phenotype
related to osmoregulation perhaps due to functional redundancy
with rhgB. {ECO:0000269|PubMed:11220631,
ECO:0000269|PubMed:16478785}.
-!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49)
family. Rh subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF193811; AAF63243.1; -; mRNA.
EMBL; AF510714; AAP47143.1; -; Genomic_DNA.
EMBL; AAFI02000055; EAL65679.1; -; Genomic_DNA.
RefSeq; XP_639042.1; XM_633950.1.
ProteinModelPortal; Q9NIV0; -.
STRING; 44689.DDB0191180; -.
TCDB; 1.A.11.4.6; the ammonium transporter channel (amt) family.
PaxDb; Q9NIV0; -.
EnsemblProtists; EAL65679; EAL65679; DDB_G0283389.
GeneID; 8624067; -.
KEGG; ddi:DDB_G0283389; -.
dictyBase; DDB_G0283389; rhgA.
eggNOG; KOG3796; Eukaryota.
eggNOG; ENOG410XTF8; LUCA.
InParanoid; Q9NIV0; -.
KO; K06580; -.
OMA; DLENEFY; -.
PhylomeDB; Q9NIV0; -.
Reactome; R-DDI-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-DDI-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-DDI-444411; Rhesus glycoproteins mediate ammonium transport.
PRO; PR:Q9NIV0; -.
Proteomes; UP000002195; Chromosome 4.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:dictyBase.
GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
GO; GO:0015696; P:ammonium transport; ISS:dictyBase.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
InterPro; IPR002229; RhesusRHD.
Pfam; PF00909; Ammonium_transp; 1.
PRINTS; PR00342; RHESUSRHD.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Vacuole.
CHAIN 1 527 Rhesus-like glycoprotein A.
/FTId=PRO_0000390404.
TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.
TRANSMEM 19 39 Helical. {ECO:0000255}.
TOPO_DOM 40 70 Extracellular. {ECO:0000255}.
TRANSMEM 71 91 Helical. {ECO:0000255}.
TOPO_DOM 92 99 Cytoplasmic. {ECO:0000255}.
TRANSMEM 100 120 Helical. {ECO:0000255}.
TOPO_DOM 121 141 Extracellular. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 166 Cytoplasmic. {ECO:0000255}.
TRANSMEM 167 187 Helical. {ECO:0000255}.
TOPO_DOM 188 195 Extracellular. {ECO:0000255}.
TRANSMEM 196 216 Helical. {ECO:0000255}.
TOPO_DOM 217 236 Cytoplasmic. {ECO:0000255}.
TRANSMEM 237 257 Helical. {ECO:0000255}.
TOPO_DOM 258 263 Extracellular. {ECO:0000255}.
TRANSMEM 264 284 Helical. {ECO:0000255}.
TOPO_DOM 285 299 Cytoplasmic. {ECO:0000255}.
TRANSMEM 300 319 Helical. {ECO:0000255}.
TOPO_DOM 320 321 Extracellular. {ECO:0000255}.
TRANSMEM 322 342 Helical. {ECO:0000255}.
TOPO_DOM 343 357 Cytoplasmic. {ECO:0000255}.
TRANSMEM 358 378 Helical. {ECO:0000255}.
TOPO_DOM 379 406 Extracellular. {ECO:0000255}.
TRANSMEM 407 427 Helical. {ECO:0000255}.
TOPO_DOM 428 527 Cytoplasmic. {ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 478 482 DDEEE->AAAAA: Decreased interaction with
AP1G1, loss of transport to the
contractile vacuole and mislocalization
to the plasma membrane and small
vesicular structures.
{ECO:0000269|PubMed:16478785}.
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


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