TPO2_YEAST
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 03-AUG-2022, entry version 154.
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;
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 BioGRID; 33385; 66.
DR DIP; DIP-7902N; -.
DR IntAct; P53283; 26.
DR MINT; P53283; -.
DR STRING; 4932.YGR138C; -.
DR TCDB; 2.A.1.2.67; the major facilitator superfamily (mfs).
DR iPTMnet; P53283; -.
DR MaxQB; P53283; -.
DR PaxDb; P53283; -.
DR PRIDE; P53283; -.
DR EnsemblFungi; YGR138C_mRNA; YGR138C; YGR138C.
DR GeneID; 853039; -.
DR KEGG; sce:YGR138C; -.
DR SGD; S000003370; TPO2.
DR VEuPathDB; FungiDB:YGR138C; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000176486; -.
DR HOGENOM; CLU_008455_11_5_1; -.
DR InParanoid; P53283; -.
DR OMA; TWKEADP; -.
DR BioCyc; YEAST:G3O-30843-MON; -.
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: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:0000297; F:spermine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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; 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..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
