YPQ3_YEAST
ID YPQ3_YEAST Reviewed; 296 AA.
AC P38279; D6VQE2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable vacuolar amino acid transporter YPQ3;
DE AltName: Full=PQ-loop repeat-containing protein 3;
DE AltName: Full=Protein RTC2;
DE AltName: Full=Restriction of telomere capping protein 2;
GN Name=RTC2; Synonyms=YPQ3; OrderedLocusNames=YBR147W; ORFNames=YBR1124;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=12702675; DOI=10.1093/genetics/163.4.1287;
RA Anderson J.B., Sirjusingh C., Parsons A.B., Boone C., Wickens C.,
RA Cowen L.E., Kohn L.M.;
RT "Mode of selection and experimental evolution of antifungal drug resistance
RT in Saccharomyces cerevisiae.";
RL Genetics 163:1287-1298(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15388447; DOI=10.1128/aac.48.10.3871-3876.2004;
RA Markovich S., Yekutiel A., Shalit I., Shadkchan Y., Osherov N.;
RT "Genomic approach to identification of mutations affecting caspofungin
RT susceptibility in Saccharomyces cerevisiae.";
RL Antimicrob. Agents Chemother. 48:3871-3876(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=17986253; DOI=10.1111/j.1567-1364.2007.00325.x;
RA Jimenez-Marti E., del Olmo M.-L.;
RT "Addition of ammonia or amino acids to a nitrogen-depleted medium affects
RT gene expression patterns in yeast cells during alcoholic fermentation.";
RL FEMS Yeast Res. 8:245-256(2008).
RN [8]
RP GENE NAME, AND DISRUPTION PHENOTYPE.
RX PubMed=18845848; DOI=10.1534/genetics.108.092577;
RA Addinall S.G., Downey M., Yu M., Zubko M.K., Dewar J., Leake A.,
RA Hallinan J., Shaw O., James K., Wilkinson D.J., Wipat A., Durocher D.,
RA Lydall D.;
RT "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied
RT cellular processes influencing telomere capping in Saccharomyces
RT cerevisiae.";
RL Genetics 180:2251-2266(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23169667; DOI=10.1073/pnas.1211198109;
RA Jezegou A., Llinares E., Anne C., Kieffer-Jaquinod S., O'Regan S.,
RA Aupetit J., Chabli A., Sagne C., Debacker C., Chadefaux-Vekemans B.,
RA Journet A., Andre B., Gasnier B.;
RT "Heptahelical protein PQLC2 is a lysosomal cationic amino acid exporter
RT underlying the action of cysteamine in cystinosis therapy.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E3434-E3443(2012).
CC -!- FUNCTION: May function as an amino acid transporter mediating the
CC export of cationic amino acids from the vacuole. Required for optimal
CC growth in synthetic medium. {ECO:0000269|PubMed:17986253,
CC ECO:0000269|PubMed:23169667}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:23169667};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23169667}.
CC Mitochondrion membrane {ECO:0000269|PubMed:16823961}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16823961}.
CC -!- INDUCTION: Up-regulated by addition of ammonia or amino acids to a
CC nitrogen-depleted medium. Down-regulated by excess lysine.
CC {ECO:0000269|PubMed:17986253, ECO:0000269|PubMed:23169667}.
CC -!- DISRUPTION PHENOTYPE: Resistant to fluconazole. Increased resistance to
CC caspofungin. Suppresses CDC13-1 temperature sensitivity.
CC {ECO:0000269|PubMed:12702675, ECO:0000269|PubMed:15388447,
CC ECO:0000269|PubMed:18845848}.
CC -!- SIMILARITY: Belongs to the laat-1 family. {ECO:0000305}.
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DR EMBL; Z36016; CAA85105.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07262.1; -; Genomic_DNA.
DR PIR; S46018; S46018.
DR RefSeq; NP_009705.1; NM_001178495.1.
DR AlphaFoldDB; P38279; -.
DR BioGRID; 32846; 161.
DR STRING; 4932.YBR147W; -.
DR TCDB; 2.A.43.2.7; the lysosomal cystine transporter (lct) family.
DR PaxDb; P38279; -.
DR PRIDE; P38279; -.
DR EnsemblFungi; YBR147W_mRNA; YBR147W; YBR147W.
DR GeneID; 852444; -.
DR KEGG; sce:YBR147W; -.
DR SGD; S000000351; RTC2.
DR VEuPathDB; FungiDB:YBR147W; -.
DR eggNOG; KOG2913; Eukaryota.
DR GeneTree; ENSGT00940000176777; -.
DR HOGENOM; CLU_019699_1_0_1; -.
DR InParanoid; P38279; -.
DR OMA; ALSLGCW; -.
DR BioCyc; YEAST:G3O-29099-MON; -.
DR PRO; PR:P38279; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38279; protein.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IMP:SGD.
DR GO; GO:0034488; P:basic amino acid transmembrane export from vacuole; IMP:SGD.
DR InterPro; IPR006603; PQ-loop_rpt.
DR Pfam; PF04193; PQ-loop; 2.
DR SMART; SM00679; CTNS; 2.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Mitochondrion; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..296
FT /note="Probable vacuolar amino acid transporter YPQ3"
FT /id="PRO_0000202496"
FT TOPO_DOM 1..12
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..68
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..199
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..262
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 10..76
FT /note="PQ-loop 1"
FT DOMAIN 208..270
FT /note="PQ-loop 2"
SQ SEQUENCE 296 AA; 33497 MW; 50D65896A1BAFB43 CRC64;
MKLIPIILNA KNLSGMAGSI SICCWIVVFV PQIYENFRRQ SAEGLSLLFI VLWLLGDIFN
VMGAMMQNLL PTMIILAAYY TLADLILLIQ CMWYDKEKKS ILQEVKKNVD PVHLPPANPI
NETVLQDVFN EYEPLLPRIE EEDSQSYSSL ELGRTIVVKE RENFFNDFLI VSGVLIAGIL
SWYISYCSGL DNGIPKKKPA FEQINLPAQI LGYLSAILYL GSRIPQIVLN FKRKSCEGVS
FLFFLFACLG NTSFIISVLS ASWLIGSAGT LLMDFTVFIQ FFLYAKPKYE KILIDN
