YPQ2_YEAST
ID YPQ2_YEAST Reviewed; 317 AA.
AC Q06328; D6VSY2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable vacuolar amino acid transporter YPQ2;
DE AltName: Full=PQ-loop repeat-containing protein 2;
GN Name=YPQ2; OrderedLocusNames=YDR352W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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.
CC {ECO:0000269|PubMed:23169667}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23169667}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23169667}.
CC -!- DISRUPTION PHENOTYPE: Resistant to canavanine.
CC {ECO:0000269|PubMed:23169667}.
CC -!- MISCELLANEOUS: Present with 6350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the laat-1 family. {ECO:0000305}.
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DR EMBL; U28372; AAB64788.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12192.1; -; Genomic_DNA.
DR PIR; S61149; S61149.
DR RefSeq; NP_010639.1; NM_001180660.1.
DR AlphaFoldDB; Q06328; -.
DR BioGRID; 32409; 84.
DR IntAct; Q06328; 3.
DR MINT; Q06328; -.
DR STRING; 4932.YDR352W; -.
DR TCDB; 2.A.43.2.8; the lysosomal cystine transporter (lct) family.
DR iPTMnet; Q06328; -.
DR PaxDb; Q06328; -.
DR PRIDE; Q06328; -.
DR EnsemblFungi; YDR352W_mRNA; YDR352W; YDR352W.
DR GeneID; 851954; -.
DR KEGG; sce:YDR352W; -.
DR SGD; S000002760; YPQ2.
DR VEuPathDB; FungiDB:YDR352W; -.
DR eggNOG; KOG2913; Eukaryota.
DR GeneTree; ENSGT00940000175512; -.
DR HOGENOM; CLU_019699_3_1_1; -.
DR InParanoid; Q06328; -.
DR OMA; IYFYQHY; -.
DR BioCyc; YEAST:G3O-29906-MON; -.
DR PRO; PR:Q06328; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06328; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
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: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; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..317
FT /note="Probable vacuolar amino acid transporter YPQ2"
FT /id="PRO_0000253843"
FT TOPO_DOM 1..13
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..71
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..184
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..249
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..71
FT /note="PQ-loop 1"
FT DOMAIN 185..247
FT /note="PQ-loop 2"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 317 AA; 35179 MW; F6A41A2175E05C75 CRC64;
MSCSNGIWPT VSNLCGSLSF FTSVISLFPQ IIETYRDKSV DGLSPYFLLA WLCGDITSLI
GAKLTGQLLF QILLAIYFLL NDSFVCGQYY YYGVLHENKL ATVGHEPKPL LPELVENGEL
LREEEDMIQG GSSAESPRSS RRRSAITAAL AIAHTISTAS AYPLNVGSTQ SQVGPPGDGK
NSQLGTILSW IGASFYVGAR IPQLIKNYNR KSTDGLSPFL FATTLLCNIT YNLSIFTSCR
FLDNQNKREF IVNELPFIFG SAGTIAFDLI YFYQYYILYA TDMQLRELER ELYSPEEDSA
AQLVTERTSL LSGETQT
