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Polyamine transporter 1

 TPO1_YEAST              Reviewed;         586 AA.
Q07824; D6VXX6;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 143.
RecName: Full=Polyamine transporter 1;
Name=TPO1; OrderedLocusNames=YLL028W; ORFNames=L0939;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=9920864; DOI=10.1074/jbc.274.6.3265;
Tomitori H., Kashiwagi K., Sakata K., Kakinuma Y., Igarashi K.;
"Identification of a gene for a polyamine transport protein in
yeast.";
J. Biol. Chem. 274:3265-3267(1999).
[4]
FUNCTION, AND MUTAGENESIS OF GLU-207; GLU-323; GLU-324 AND GLU-574.
PubMed=11171066; DOI=10.1042/0264-6021:3530681;
Tomitori H., Kashiwagi K., Asakawa T., Kakinuma Y., Michael A.J.,
Igarashi K.;
"Multiple polyamine transport systems on the vacuolar membrane in
yeast.";
Biochem. J. 353:681-688(2001).
[5]
INDUCTION.
PubMed=11470516; DOI=10.1016/S0378-1119(01)00558-3;
do Valle Matta M.A., Jonniaux J.-L., Balzi E., Goffeau A.,
van den Hazel B.;
"Novel target genes of the yeast regulator Pdr1p: a contribution of
the TPO1 gene in resistance to quinidine and other drugs.";
Gene 272:111-119(2001).
[6]
TOPOLOGY.
PubMed=12524434; DOI=10.1074/jbc.M300163200;
Kim H., Melen K., von Heijne G.;
"Topology models for 37 Saccharomyces cerevisiae membrane proteins
based on C-terminal reporter fusions and predictions.";
J. Biol. Chem. 278:10208-10213(2003).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12562762; DOI=10.1074/jbc.M210715200;
Albertsen M., Bellahn I., Kraemer R., Waffenschmidt S.;
"Localization and function of the yeast multidrug transporter Tpo1p.";
J. Biol. Chem. 278:12820-12825(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
SUBCELLULAR LOCATION.
PubMed=13679573; DOI=10.1073/pnas.2033246100;
Shepard K.A., Gerber A.P., Jambhekar A., Takizawa P.A., Brown P.O.,
Herschlag D., DeRisi J.L., Vale R.D.;
"Widespread cytoplasmic mRNA transport in yeast: identification of 22
bud-localized transcripts using DNA microarray analysis.";
Proc. Natl. Acad. Sci. U.S.A. 100:11429-11434(2003).
[11]
INDUCTION.
PubMed=15066780; DOI=10.1128/AEM.70.4.1913-1922.2004;
Aranda A., del Olmo M.;
"Exposure of Saccharomyces cerevisiae to acetaldehyde induces sulfur
amino acid metabolism and polyamine transporter genes, which depend on
Met4p and Haa1p transcription factors, respectively.";
Appl. Environ. Microbiol. 70:1913-1922(2004).
[12]
FUNCTION, PHOSPHORYLATION AT SER-19; THR-52 AND SER-342, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-19; THR-52 AND SER-342.
PubMed=15637075; DOI=10.1074/jbc.M410274200;
Uemura T., Tachihara K., Tomitori H., Kashiwagi K., Igarashi K.;
"Characteristics of the polyamine transporter TPO1 and regulation of
its activity and cellular localization by phosphorylation.";
J. Biol. Chem. 280:9646-9652(2005).
[13]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[14]
FUNCTION, AND INDUCTION.
PubMed=17362938; DOI=10.1016/j.febslet.2007.03.001;
Mima S., Ushijima H., Hwang H.-J., Tsutsumi S., Makise M.,
Yamaguchi Y., Tsuchiya T., Mizushima H., Mizushima T.;
"Identification of the TPO1 gene in yeast, and its human orthologue
TETRAN, which cause resistance to NSAIDs.";
FEBS Lett. 581:1457-1463(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-76; THR-89 AND
SER-91, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-76; THR-89 AND
SER-91, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Cell membrane polyamine/proton antiporter, involved in
the detoxification of excess polyamines in the cytoplasm.
Catalyzes polyamine uptake at alkaline pH and excretion at acidic
pH. Recognizes spermidine, spermine and putrescine, the polyamine
analogs methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat,
the antimalarial drug quinidine, and cycloheximide. Confers
resistance to the non-steroidal anti-inflammatory drug
indomethacin. {ECO:0000269|PubMed:11171066,
ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:15637075,
ECO:0000269|PubMed:17362938, ECO:0000269|PubMed:9920864}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12562762,
ECO:0000269|PubMed:13679573, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:15637075}; Multi-pass membrane protein
{ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:13679573,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15637075}.
Note=Enriched on the cell membrane of growing buds.
-!- INDUCTION: By transcription factor PDR1, by transcription factor
HAA1 in response to acetaldehyde accumulation and by the non-
steroidal anti-inflammatory drug indomethacin.
{ECO:0000269|PubMed:11470516, ECO:0000269|PubMed:15066780,
ECO:0000269|PubMed:17362938}.
-!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1
family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z73133; CAA97477.1; -; Genomic_DNA.
EMBL; BK006945; DAA09292.1; -; Genomic_DNA.
PIR; S64779; S64779.
RefSeq; NP_013072.1; NM_001181848.1.
ProteinModelPortal; Q07824; -.
BioGrid; 31224; 137.
DIP; DIP-1706N; -.
IntAct; Q07824; 29.
MINT; Q07824; -.
STRING; 4932.YLL028W; -.
TCDB; 2.A.1.2.16; the major facilitator superfamily (mfs).
iPTMnet; Q07824; -.
MaxQB; Q07824; -.
PaxDb; Q07824; -.
PRIDE; Q07824; -.
EnsemblFungi; YLL028W; YLL028W; YLL028W.
GeneID; 850631; -.
KEGG; sce:YLL028W; -.
EuPathDB; FungiDB:YLL028W; -.
SGD; S000003951; TPO1.
GeneTree; ENSGT00620000088227; -.
HOGENOM; HOG000160689; -.
InParanoid; Q07824; -.
KO; K08157; -.
OMA; GACPLAV; -.
OrthoDB; EOG092C2079; -.
BioCyc; YEAST:G3O-32132-MONOMER; -.
PRO; PR:Q07824; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
GO; GO:0015606; F:spermidine transmembrane transporter activity; IDA:SGD.
GO; GO:0000297; F:spermine transmembrane transporter activity; IDA:SGD.
GO; GO:1902047; P:polyamine transmembrane transport; IMP:SGD.
GO; GO:0015847; P:putrescine transport; IMP:SGD.
GO; GO:0015848; P:spermidine transport; IDA:SGD.
GO; GO:0000296; P:spermine transport; IDA:SGD.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Antiport; Cell membrane; Complete proteome; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 586 Polyamine transporter 1.
/FTId=PRO_0000262730.
TOPO_DOM 1 145 Cytoplasmic. {ECO:0000255}.
TRANSMEM 146 166 Helical. {ECO:0000255}.
TOPO_DOM 167 181 Extracellular. {ECO:0000255}.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TOPO_DOM 203 212 Cytoplasmic. {ECO:0000255}.
TRANSMEM 213 233 Helical. {ECO:0000255}.
TOPO_DOM 234 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TOPO_DOM 264 271 Cytoplasmic. {ECO:0000255}.
TRANSMEM 272 292 Helical. {ECO:0000255}.
TOPO_DOM 293 301 Extracellular. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 414 Extracellular. {ECO:0000255}.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TOPO_DOM 436 454 Cytoplasmic. {ECO:0000255}.
TRANSMEM 455 475 Helical. {ECO:0000255}.
TOPO_DOM 476 483 Extracellular. {ECO:0000255}.
TRANSMEM 484 504 Helical. {ECO:0000255}.
TOPO_DOM 505 505 Cytoplasmic. {ECO:0000255}.
TRANSMEM 506 526 Helical. {ECO:0000255}.
TOPO_DOM 527 528 Extracellular. {ECO:0000255}.
TRANSMEM 529 549 Helical. {ECO:0000255}.
TRANSMEM 550 570 Helical. {ECO:0000255}.
TOPO_DOM 571 586 Cytoplasmic. {ECO:0000255}.
COMPBIAS 17 25 Poly-Ser.
MOD_RES 19 19 Phosphoserine; by PKC.
{ECO:0000269|PubMed:15637075}.
MOD_RES 52 52 Phosphothreonine; by CK1.
{ECO:0000269|PubMed:15637075}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 89 89 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 342 342 Phosphoserine; by PKA.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 19 19 S->A: Reduces transport activity.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 19 19 S->E: Enhances transport activity.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 52 52 T->A: Reduces transport activity.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 52 52 T->E: Enhances transport activity.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 207 207 E->Q: Loss of function.
{ECO:0000269|PubMed:11171066}.
MUTAGEN 323 323 E->Q: Loss of function; when associated
with Q-324.
{ECO:0000269|PubMed:11171066}.
MUTAGEN 324 324 E->Q: Loss of function; when associated
with Q-323.
{ECO:0000269|PubMed:11171066}.
MUTAGEN 342 342 S->A: Interferes with correct plasma
membrane localization.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 342 342 S->E: Enhances transport activity.
{ECO:0000269|PubMed:15637075}.
MUTAGEN 574 574 E->Q: Loss of function.
{ECO:0000269|PubMed:11171066}.
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


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