ID   TPO2_YEAST              Reviewed;         614 AA.
AC   P53283; D6VUR9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 168.
DE   RecName: Full=Polyamine transporter 2;
GN   Name=TPO2; OrderedLocusNames=YGR138C; ORFNames=G6417;
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=9169869; DOI=10.1038/387s081;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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=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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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).
CC   -!- FUNCTION: Cell membrane polyamine/proton antiporter, involved in the
CC       detoxification of excess polyamines in the cytoplasm. Recognizes
CC       spermine, but not spermidine. {ECO:0000269|PubMed:11171066,
CC       ECO:0000269|PubMed:12562762}.
CC   -!- INTERACTION:
CC       P53283; Q06451: TPO3; NbExp=3; IntAct=EBI-2044753, EBI-34275;
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   -!- 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; Z72923; CAA97151.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08230.1; -; Genomic_DNA.
DR   PIR; S64447; S64447.
DR   RefSeq; NP_011654.1; NM_001181267.1.
DR   AlphaFoldDB; P53283; -.
DR   SMR; P53283; -.
DR   BioGRID; 33385; 71.
DR   DIP; DIP-7902N; -.
DR   FunCoup; P53283; 112.
DR   IntAct; P53283; 29.
DR   MINT; P53283; -.
DR   STRING; 4932.YGR138C; -.
DR   TCDB; 2.A.1.2.67; the major facilitator superfamily (mfs).
DR   iPTMnet; P53283; -.
DR   PaxDb; 4932-YGR138C; -.
DR   PeptideAtlas; P53283; -.
DR   EnsemblFungi; YGR138C_mRNA; YGR138C; YGR138C.
DR   GeneID; 853039; -.
DR   KEGG; sce:YGR138C; -.
DR   AGR; SGD:S000003370; -.
DR   SGD; S000003370; TPO2.
DR   VEuPathDB; FungiDB:YGR138C; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_008455_11_5_1; -.
DR   InParanoid; P53283; -.
DR   OMA; TWKEADP; -.
DR   OrthoDB; 3936150at2759; -.
DR   BioCyc; YEAST:G3O-30843-MONOMER; -.
DR   BioGRID-ORCS; 853039; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53283; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53283; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0000297; F:spermine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0000296; P:spermine transport; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd17323; MFS_Tpo1_MDR_like; 1.
DR   FunFam; 1.20.1250.20:FF:000011; MFS multidrug transporter, putative; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23502; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   PANTHER; PTHR23502:SF132; POLYAMINE TRANSPORTER 2-RELATED; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 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..614
FT                   /note="Polyamine transporter 2"
FT                   /id="PRO_0000173439"
FT   TOPO_DOM        1..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..437
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        500..503
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        525..541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..574
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        575..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        596..614
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   614 AA;  67589 MW;  C6B9D48720D4F2D2 CRC64;
     MSDQESVVSF NSQNTSMVDV EGQQPQQYVP SKTNSRANQL KLTKTETVKS LQDLGVTSAA
     PVPDINAPQT AKNNIFPEEY TMETPSGLVP VATLQSMGRT ASALSRTRTK QLNRTATNSS
     STGKEEMEEE ETEEREDQSG ENELDPEIEF VTFVTGDPEN PHNWPSWVRW SYTVLLSILV
     ICVAYGSACI SGGLGTVEKK YHVGMEAAIL SCSLMVIGFS LGPLIWSPVS DLYGRRVAYF
     VSMGLYVIFN IPCALAPNLG CLLACRFLCG VWSSSGLCLV GGSIADMFPS ETRGKAIAFF
     AFAPYVGPVV GPLVNGFISV STGRMDLIFW VNMAFAGVMW IISSAIPETY APVILKRKAA
     RLRKETGNPK IMTEQEAQGV SMSEMMRACL LRPLYFAVTE PVLVATCFYV CLIYSLLYAF
     FFAFPVIFGE LYGYKDNLVG LMFIPIVIGA LWALATTFYC ENKYLQIVKQ RKPTPEDRLL
     GAKIGAPFAA IALWILGATA YKHIIWVGPA SAGLAFGFGM VLIYYSLNNY IIDCYVQYAS
     SALATKVFLR SAGGAAFPLF TIQMYHKLNL HWGSWLLAFI STAMIALPFA FSYWGKGLRH
     KLSKKDYSID SVEM
//