YPQ1_YEAST
ID YPQ1_YEAST Reviewed; 308 AA.
AC Q12010; D6W1X6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable vacuolar amino acid transporter YPQ1;
DE AltName: Full=PQ-loop repeat-containing protein 1;
GN Name=YPQ1; OrderedLocusNames=YOL092W; ORFNames=O0929;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
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 [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 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 [8]
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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 1800 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; Z74834; CAA99104.1; -; Genomic_DNA.
DR EMBL; X83121; CAA58187.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10692.1; -; Genomic_DNA.
DR PIR; S57377; S57377.
DR RefSeq; NP_014549.1; NM_001183346.1.
DR AlphaFoldDB; Q12010; -.
DR SMR; Q12010; -.
DR BioGRID; 34310; 52.
DR DIP; DIP-8883N; -.
DR STRING; 4932.YOL092W; -.
DR TCDB; 2.A.43.2.3; the lysosomal cystine transporter (lct) family.
DR iPTMnet; Q12010; -.
DR PaxDb; Q12010; -.
DR PRIDE; Q12010; -.
DR EnsemblFungi; YOL092W_mRNA; YOL092W; YOL092W.
DR GeneID; 854061; -.
DR KEGG; sce:YOL092W; -.
DR SGD; S000005452; YPQ1.
DR VEuPathDB; FungiDB:YOL092W; -.
DR eggNOG; KOG2913; Eukaryota.
DR GeneTree; ENSGT00940000176777; -.
DR HOGENOM; CLU_019699_1_0_1; -.
DR InParanoid; Q12010; -.
DR OMA; MDFVIFS; -.
DR BioCyc; YEAST:G3O-33492-MON; -.
DR Reactome; R-SCE-5223345; Miscellaneous transport and binding events.
DR PRO; PR:Q12010; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12010; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..308
FT /note="Probable vacuolar amino acid transporter YPQ1"
FT /id="PRO_0000235929"
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..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..277
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 10..76
FT /note="PQ-loop 1"
FT DOMAIN 211..274
FT /note="PQ-loop 2"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 34873 MW; 38EB1645FA034812 CRC64;
MQLVPLELNR STLSGISGSI SISCWIIVFV PQIYENFYRK SSDGLSLLFV VLWLAGDVFN
LMGAVMQHLL STMIILAAYY TVADIILLGQ CLWYDNEEKP AVDPIHLSPA NPINENVLHD
VFNEQQPLLN SQGQPNRIDE EMAAPSSDGN AGDDNLREVN SRNLIKDIFI VSGVVFVGFI
SWYVTYCVNY TQPPPVEDPS LPVPELQINW MAQIFGYLSA LLYLGSRIPQ ILLNFKRKSC
EGISFLFFLF ACLGNTTFIF SVIVISLDWK YLIMNASWLV GSIGTLFMDF VIFSQFFIYK
RNKKFILN
