TPO1_YEAST
ID TPO1_YEAST Reviewed; 586 AA.
AC Q07824; D6VXX6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Polyamine transporter 1;
GN Name=TPO1; OrderedLocusNames=YLL028W; ORFNames=L0939;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=9920864; DOI=10.1074/jbc.274.6.3265;
RA Tomitori H., Kashiwagi K., Sakata K., Kakinuma Y., Igarashi K.;
RT "Identification of a gene for a polyamine transport protein in yeast.";
RL J. Biol. Chem. 274:3265-3267(1999).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLU-207; GLU-323; GLU-324 AND GLU-574.
RX PubMed=11171066; DOI=10.1042/0264-6021:3530681;
RA Tomitori H., Kashiwagi K., Asakawa T., Kakinuma Y., Michael A.J.,
RA Igarashi K.;
RT "Multiple polyamine transport systems on the vacuolar membrane in yeast.";
RL Biochem. J. 353:681-688(2001).
RN [5]
RP INDUCTION.
RX PubMed=11470516; DOI=10.1016/s0378-1119(01)00558-3;
RA do Valle Matta M.A., Jonniaux J.-L., Balzi E., Goffeau A.,
RA van den Hazel B.;
RT "Novel target genes of the yeast regulator Pdr1p: a contribution of the
RT TPO1 gene in resistance to quinidine and other drugs.";
RL Gene 272:111-119(2001).
RN [6]
RP TOPOLOGY.
RX PubMed=12524434; DOI=10.1074/jbc.m300163200;
RA Kim H., Melen K., von Heijne G.;
RT "Topology models for 37 Saccharomyces cerevisiae membrane proteins based on
RT C-terminal reporter fusions and predictions.";
RL J. Biol. Chem. 278:10208-10213(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12562762; DOI=10.1074/jbc.m210715200;
RA Albertsen M., Bellahn I., Kraemer R., Waffenschmidt S.;
RT "Localization and function of the yeast multidrug transporter Tpo1p.";
RL J. Biol. Chem. 278:12820-12825(2003).
RN [8]
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 [9]
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=13679573; DOI=10.1073/pnas.2033246100;
RA Shepard K.A., Gerber A.P., Jambhekar A., Takizawa P.A., Brown P.O.,
RA Herschlag D., DeRisi J.L., Vale R.D.;
RT "Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-
RT localized transcripts using DNA microarray analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11429-11434(2003).
RN [11]
RP INDUCTION.
RX PubMed=15066780; DOI=10.1128/aem.70.4.1913-1922.2004;
RA Aranda A., del Olmo M.;
RT "Exposure of Saccharomyces cerevisiae to acetaldehyde induces sulfur amino
RT acid metabolism and polyamine transporter genes, which depend on Met4p and
RT Haa1p transcription factors, respectively.";
RL Appl. Environ. Microbiol. 70:1913-1922(2004).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT SER-19; THR-52 AND SER-342, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF SER-19; THR-52 AND SER-342.
RX PubMed=15637075; DOI=10.1074/jbc.m410274200;
RA Uemura T., Tachihara K., Tomitori H., Kashiwagi K., Igarashi K.;
RT "Characteristics of the polyamine transporter TPO1 and regulation of its
RT activity and cellular localization by phosphorylation.";
RL J. Biol. Chem. 280:9646-9652(2005).
RN [13]
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 [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=17362938; DOI=10.1016/j.febslet.2007.03.001;
RA Mima S., Ushijima H., Hwang H.-J., Tsutsumi S., Makise M., Yamaguchi Y.,
RA Tsuchiya T., Mizushima H., Mizushima T.;
RT "Identification of the TPO1 gene in yeast, and its human orthologue TETRAN,
RT which cause resistance to NSAIDs.";
RL FEBS Lett. 581:1457-1463(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-76; THR-89 AND
RP SER-91, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-76; THR-89 AND
RP SER-91, AND 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).
CC -!- FUNCTION: Cell membrane polyamine/proton antiporter, involved in the
CC detoxification of excess polyamines in the cytoplasm. Catalyzes
CC polyamine uptake at alkaline pH and excretion at acidic pH. Recognizes
CC spermidine, spermine and putrescine, the polyamine analogs
CC methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat, the
CC antimalarial drug quinidine, and cycloheximide. Confers resistance to
CC the non-steroidal anti-inflammatory drug indomethacin.
CC {ECO:0000269|PubMed:11171066, ECO:0000269|PubMed:12562762,
CC ECO:0000269|PubMed:15637075, ECO:0000269|PubMed:17362938,
CC ECO:0000269|PubMed:9920864}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12562762,
CC ECO:0000269|PubMed:13679573, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15637075}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:13679573,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15637075}.
CC Note=Enriched on the cell membrane of growing buds.
CC -!- INDUCTION: By transcription factor PDR1, by transcription factor HAA1
CC in response to acetaldehyde accumulation and by the non-steroidal anti-
CC inflammatory drug indomethacin. {ECO:0000269|PubMed:11470516,
CC ECO:0000269|PubMed:15066780, ECO:0000269|PubMed:17362938}.
CC -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily. {ECO:0000305}.
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DR EMBL; Z73133; CAA97477.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09292.1; -; Genomic_DNA.
DR PIR; S64779; S64779.
DR RefSeq; NP_013072.1; NM_001181848.1.
DR AlphaFoldDB; Q07824; -.
DR SMR; Q07824; -.
DR BioGRID; 31224; 139.
DR DIP; DIP-1706N; -.
DR IntAct; Q07824; 29.
DR MINT; Q07824; -.
DR STRING; 4932.YLL028W; -.
DR TCDB; 2.A.1.2.16; the major facilitator superfamily (mfs).
DR iPTMnet; Q07824; -.
DR MaxQB; Q07824; -.
DR PaxDb; Q07824; -.
DR PRIDE; Q07824; -.
DR EnsemblFungi; YLL028W_mRNA; YLL028W; YLL028W.
DR GeneID; 850631; -.
DR KEGG; sce:YLL028W; -.
DR SGD; S000003951; TPO1.
DR VEuPathDB; FungiDB:YLL028W; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_11_4_1; -.
DR InParanoid; Q07824; -.
DR OMA; WRWLEYV; -.
DR BioCyc; YEAST:G3O-32132-MON; -.
DR PRO; PR:Q07824; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07824; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015606; F:spermidine transmembrane transporter activity; IDA:SGD.
DR GO; GO:0000297; F:spermine transmembrane transporter activity; IDA:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IMP:SGD.
DR GO; GO:0015847; P:putrescine transport; IMP:SGD.
DR GO; GO:0015848; P:spermidine transport; IDA:SGD.
DR GO; GO:0000296; P:spermine transport; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..586
FT /note="Polyamine transporter 1"
FT /id="PRO_0000262730"
FT TOPO_DOM 1..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:15637075"
FT MOD_RES 52
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000269|PubMed:15637075"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 342
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 19
FT /note="S->A: Reduces transport activity."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 19
FT /note="S->E: Enhances transport activity."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 52
FT /note="T->A: Reduces transport activity."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 52
FT /note="T->E: Enhances transport activity."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 207
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:11171066"
FT MUTAGEN 323
FT /note="E->Q: Loss of function; when associated with Q-324."
FT /evidence="ECO:0000269|PubMed:11171066"
FT MUTAGEN 324
FT /note="E->Q: Loss of function; when associated with Q-323."
FT /evidence="ECO:0000269|PubMed:11171066"
FT MUTAGEN 342
FT /note="S->A: Interferes with correct plasma membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 342
FT /note="S->E: Enhances transport activity."
FT /evidence="ECO:0000269|PubMed:15637075"
FT MUTAGEN 574
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:11171066"
SQ SEQUENCE 586 AA; 64272 MW; 32DBFB795617D036 CRC64;
MSDHSPISNK ENHLLPSDSS RSSSSDMHST GTTGTTGVEP VDFTGEGAKY TTATEGNGGA
DLAIQRTTTM NSAAESEVNI TRRLTKILTG SVNEPDRVEV DYTNCAPMGG DRPYPPSLPS
RDLYEVTFDG PNDPLHPFNW PMKKKVLLCL VLCLDSIAIA MCSSIFASAV PQICEIYHVI
EVVAILGITL FVLGFAASPV IYAPLSELYG RKGVLVLSAF GFALFQFAVA TAENLQTIFI
CRFFGGFIGA APMAVVPAAF ADMFDTNVRG KAIALFSLGV FVGPILSPVM GSYIAQRTTW
RWLEYVVGCF ASAVFVAIVL FFEETHHPTI LVNKAKQMRK QSNNWGIHAA HEDVELSIKD
IVQKTVTRPI IMLFVEPLLL FVTIYNSFVY GILYLLLEAY PLVFVEGYGF TENGELPYIA
LIIGMMVCAA FIWYMDNDYL KRCRAKGKLV PEARLYAMVI AGTVFPIGIL WFCWTGYYPH
KIHWMVPTVG GAFIGFGLMG IFLPCLNYII ESYLLLAASA VAANTFMRSA FGACFPLFAG
YMFRGMGIGW AGLLLGLFAA AMIPVPLLFL KYGESIRKKS KYAYAA
