TPO5_YEAST
ID TPO5_YEAST Reviewed; 618 AA.
AC P36029; D6VX26;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Polyamine transporter TPO5;
GN Name=TPO5; OrderedLocusNames=YKL174C; ORFNames=YKL639;
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=8091858; DOI=10.1002/yea.320100004;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT of yeast chromosome XI.";
RL Yeast 10:S25-S33(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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, AND SUBCELLULAR LOCATION.
RX PubMed=15668236; DOI=10.1074/jbc.m410778200;
RA Tachihara K., Uemura T., Kashiwagi K., Igarashi K.;
RT "Excretion of putrescine and spermidine by the protein encoded by YKL174c
RT (TPO5) in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:12637-12642(2005).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, 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 [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for polyamine transport. Transports putrescine
CC effectively and spermidine less effectively.
CC {ECO:0000269|PubMed:15668236}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15668236}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15668236}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; Z26878; CAA81512.1; -; Genomic_DNA.
DR EMBL; Z28174; CAA82016.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08992.1; -; Genomic_DNA.
DR PIR; S38004; S38004.
DR RefSeq; NP_012747.1; NM_001179740.1.
DR AlphaFoldDB; P36029; -.
DR SMR; P36029; -.
DR BioGRID; 33964; 62.
DR DIP; DIP-4038N; -.
DR IntAct; P36029; 3.
DR MINT; P36029; -.
DR STRING; 4932.YKL174C; -.
DR TCDB; 2.A.3.4.5; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P36029; -.
DR MaxQB; P36029; -.
DR PaxDb; P36029; -.
DR PRIDE; P36029; -.
DR TopDownProteomics; P36029; -.
DR EnsemblFungi; YKL174C_mRNA; YKL174C; YKL174C.
DR GeneID; 853680; -.
DR KEGG; sce:YKL174C; -.
DR SGD; S000001657; TPO5.
DR VEuPathDB; FungiDB:YKL174C; -.
DR eggNOG; KOG1289; Eukaryota.
DR HOGENOM; CLU_004495_5_3_1; -.
DR InParanoid; P36029; -.
DR OMA; CGMASVT; -.
DR BioCyc; YEAST:G3O-31941-MON; -.
DR PRO; PR:P36029; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36029; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0006865; P:amino acid transport; IEA:InterPro.
DR GO; GO:0015846; P:polyamine transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..618
FT /note="Polyamine transporter TPO5"
FT /id="PRO_0000054165"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..498
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 576..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 618 AA; 69243 MW; 035CB927C624CE74 CRC64;
MPEYTLLADN IRENIVHFDP NGLFDNLHTI VHEDDSQENE EAEHFNYDQV LDKSLLSRGS
IVGLGLGLMS PVLGMCTSMA IGLINGGPLT IMLGFLISGV CIWFSSLSLG EIVSKFPMEL
HVGSAMLAPE KLKLVCSWYT GWLMLIGNWT MSTSITFAGA QLTISLILMT NSNLISEAHL
IFYTVIVFYL VVTVVGLVNL KFARFIETIN KVCVYWIIYA IIFIDILLLV FHKGKFRSLK
YALFHFDNNL SGYKSAFLSF IIGFQQSNFT LQGFSMLPAL ADEVKVPEKD IPRGMSNAVL
LSAFSGVIFL IPIMLILPDN DLLFTNHKVL PIVNIFTKST DSVVLSFFLV LLILGNLLFS
GIGSITTSSR AVYSFSRDQA IPYYDKWTYV EPDSQSKVPK NSVVLSMIIS YFLGLLALIS
TAAFNAFIGA AVLCLCSATF IPLVLVLFTR RRAIRSAPVK IRYKFGWFIN IVSIVWLLLS
MVSVCLPTQV PVTFKTMNYA LMVYVFCILV ITGLYFKWGK YNFRLPLADD IKAPIPSDAE
ETVFELEDSN VEHTLNSGTT VKESVENNSE EGFIKVHPKS STENPFEENE ENVITDYGDE
HHTAEQEFDL ADDRRYDI
