TPO4_YEAST
ID TPO4_YEAST Reviewed; 659 AA.
AC Q12256; D6W2X3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Polyamine transporter 4;
GN Name=TPO4; OrderedLocusNames=YOR273C; ORFNames=O5440;
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 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
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 FUNCTION.
RX PubMed=9593122; DOI=10.1128/aac.42.5.1034;
RA Delling U., Raymond M., Schurr E.;
RT "Identification of Saccharomyces cerevisiae genes conferring resistance to
RT quinoline ring-containing antimalarial drugs.";
RL Antimicrob. Agents Chemother. 42:1034-1041(1998).
RN [5]
RP FUNCTION.
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606 AND THR-608, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-589, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-646, AND
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).
CC -!- FUNCTION: Cell membrane polyamine/proton antiporter, involved in the
CC detoxification of excess polyamines in the cytoplasm. Recognizes
CC spermidine, spermine and the antimalarial drug quinidine, but not
CC quinine, chloroquine and mefloquine. {ECO:0000269|PubMed:11171066,
CC ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:9593122}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12562762,
CC ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By transcription factor HAA1 in response to acetaldehyde
CC accumulation. {ECO:0000269|PubMed:15066780}.
CC -!- MISCELLANEOUS: Present with 21400 molecules/cell in log phase SD
CC medium. {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; X89633; CAA61779.1; -; Genomic_DNA.
DR EMBL; Z75181; CAA99498.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11039.1; -; Genomic_DNA.
DR PIR; S67175; S67175.
DR RefSeq; NP_014916.1; NM_001183692.1.
DR AlphaFoldDB; Q12256; -.
DR BioGRID; 34662; 72.
DR DIP; DIP-4096N; -.
DR IntAct; Q12256; 22.
DR MINT; Q12256; -.
DR STRING; 4932.YOR273C; -.
DR TCDB; 2.A.1.2.64; the major facilitator superfamily (mfs).
DR iPTMnet; Q12256; -.
DR MaxQB; Q12256; -.
DR PaxDb; Q12256; -.
DR PRIDE; Q12256; -.
DR EnsemblFungi; YOR273C_mRNA; YOR273C; YOR273C.
DR GeneID; 854447; -.
DR KEGG; sce:YOR273C; -.
DR SGD; S000005799; TPO4.
DR VEuPathDB; FungiDB:YOR273C; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_11_3_1; -.
DR InParanoid; Q12256; -.
DR OMA; LMPETHK; -.
DR BioCyc; YEAST:G3O-33763-MON; -.
DR PRO; PR:Q12256; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12256; protein.
DR GO; GO:0071944; C:cell periphery; HDA: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; IMP:SGD.
DR GO; GO:0000297; F:spermine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015848; P:spermidine transport; IMP:SGD.
DR GO; GO:0000296; P:spermine transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..659
FT /note="Polyamine transporter 4"
FT /id="PRO_0000262732"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 608
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 659 AA; 73223 MW; 7F2BD0EEC5E408FC CRC64;
MPSSLTKTES NSDPRTNIQQ VPKALDKNVT NSGNLDSTSS STGSITEDEK RSEPNADSNN
MTGGEPIDPR DLDWDGPDDP DNPHNWSSLK KWYTTMTSAF LCLVVTMGSS LYVSSVPELV
ERYHVSQTLA LAGLTFYLLG LSTVIGAPLS EVFGRKPVYL FSLPVSMLFT MGVGLSNGHM
RIILPLRFLS GVFASPALSV GSGTILDIFD VDQVSVAMTY FVLSPFLGPV LSPIMAGFAT
EAKGWRWSEW IQLIAGGLIL PFIALMPETH KGIILRKRAK KRNIALKKFS REAQKEFLKT
TVTITILRPL KMLVVEPIVF VFSVYVAFIF AILFGFFEAY AVIYRGVYHM SMGISGLPFI
GIGVGLWIGA FFYLYIDRKY LFPKPPAGTQ PLTEKERTSK RTTPYRGARD AETGELLPVV
PEKFLIACKF GSVALPIGLF WQAWTARSDV HWMAPVAAGV PFGFGLILIF FSVLMYFSTC
YPPLTVASCL AANNLLRYVM SSVFPLFTIQ MYTKMKIKWA STLFALVCVV MIPIPWVFEK
WGSKLRHKSQ FGYAAMEKEA ETEGGIDDVN AVDGELNLTR MTTLRTMETD PSTREKPGER
LSLRRTHTQP VPASFDREDG QHAQNRNEPI SNSLYSAIKD NEDGYSYTEM ATDASARMV
