ID   FEN2_YEAST              Reviewed;         512 AA.
AC   P25621; D6VR38;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Pantothenate transporter FEN2;
DE   AltName: Full=Fenpropimorph resistance protein 2;
GN   Name=FEN2; OrderedLocusNames=YCR028C; ORFNames=YCR28C;
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 204511 / S288c / AB972;
RX   PubMed=1332309; DOI=10.1002/yea.320080915;
RA   Carbone M.L.A., Panzeri L., Falconi M.M., Carcano C., Plevani P.,
RA   Lucchini G.;
RT   "Nucleotide sequence of 9.2 kb left of CRY1 on yeast chromosome III from
RT   strain AB972: evidence for a Ty insertion and functional analysis of open
RT   reading frame YCR28.";
RL   Yeast 8:805-812(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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   SIMILARITY TO DAL5 FAMILY.
RX   PubMed=8313894; DOI=10.1002/j.1460-2075.1994.tb06287.x;
RA   Koonin E.V., Bork P., Sander C.;
RT   "Yeast chromosome III: new gene functions.";
RL   EMBO J. 13:493-503(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=8771708;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<531::aid-yea934>3.0.co;2-e;
RA   Marcireau C., Joets J., Pousset D., Guilloton M., Karst F.;
RT   "FEN2: a gene implicated in the catabolite repression-mediated regulation
RT   of ergosterol biosynthesis in yeast.";
RL   Yeast 12:531-539(1996).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10373490; DOI=10.1074/jbc.274.26.18747;
RA   Stolz J., Sauer N.;
RT   "The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae
RT   encodes a plasma membrane H+-pantothenate symporter.";
RL   J. Biol. Chem. 274:18747-18752(1999).
RN   [7]
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   [8]
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).
CC   -!- FUNCTION: Transports pantothenate into the cell. Also involved in the
CC       catabolite repression-mediated regulation of ergosterol biosynthesis
CC       and in fenpropimorph resistance. {ECO:0000269|PubMed:10373490,
CC       ECO:0000269|PubMed:8771708}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10373490};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:10373490}.
CC   -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC       permease family. {ECO:0000305}.
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DR   EMBL; X59720; CAA42320.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07507.1; -; Genomic_DNA.
DR   PIR; S19439; S19439.
DR   RefSeq; NP_009957.1; NM_001178743.1.
DR   AlphaFoldDB; P25621; -.
DR   SMR; P25621; -.
DR   BioGRID; 31011; 46.
DR   DIP; DIP-7672N; -.
DR   IntAct; P25621; 6.
DR   MINT; P25621; -.
DR   STRING; 4932.YCR028C; -.
DR   TCDB; 2.A.1.14.18; the major facilitator superfamily (mfs).
DR   iPTMnet; P25621; -.
DR   MaxQB; P25621; -.
DR   PaxDb; 4932-YCR028C; -.
DR   PeptideAtlas; P25621; -.
DR   EnsemblFungi; YCR028C_mRNA; YCR028C; YCR028C.
DR   GeneID; 850394; -.
DR   KEGG; sce:YCR028C; -.
DR   AGR; SGD:S000000623; -.
DR   SGD; S000000623; FEN2.
DR   VEuPathDB; FungiDB:YCR028C; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_4_2_1; -.
DR   InParanoid; P25621; -.
DR   OMA; FTTWYWW; -.
DR   OrthoDB; 3598420at2759; -.
DR   BioCyc; YEAST:G3O-29343-MONOMER; -.
DR   BioGRID-ORCS; 850394; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P25621; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25621; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR   GO; GO:0015233; F:pantothenate transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0098717; P:pantothenate import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0015887; P:pantothenate transmembrane transport; IMP:SGD.
DR   CDD; cd17327; MFS_FEN2_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR43791:SF4; PANTOTHENATE TRANSPORTER FEN2; 1.
DR   PANTHER; PTHR43791; PERMEASE-RELATED; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Pantothenate transporter FEN2"
FT                   /id="PRO_0000121367"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..132
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..372
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..401
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..434
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        456..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          468..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..499
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  58256 MW;  361942E74C62B3B4 CRC64;
     MMKESKSITQ HEVERESVSS KRAIKKRLLL FKIDLFVLSF VCLQYWINYV DRVGFTNAYI
     SGMKEDLKMV GNDLTVSNTV FMIGYIVGMV PNNLMLLCVP PRIWLSFCTF AWGLLTLGMY
     KVTSFKHICA IRFFQALFES CTFSGTHFVL GSWYKEDELP IRSAIFTGSG LVGSMFSGFM
     QTSIFTHLNG RNGLAGWRWL FIIDFCITLP IAIYGFIFFP GLPDQTSAVS KFSMTRYIFN
     EQELHYARRR LPARDESTRL DWSTIPRVLK RWHWWMFSLV WVLGGENLGF ASNSTFALWL
     QNQKYTLAQR NNYPSGIFAV GIVSTLCSAV YMSKIPRARH WHVSVFISLV MVIVAVLIRA
     DPLNPKVVFS AQYLGGVAYA GQAVFFSWAN IICHADLQER AIVLASMNMF SGAVNAWWSI
     LFFASDMVPK FERGCYALLA TAISSGIVSV VIRSLQIKEN LSKKQVPYID ANDMPGEDDD
     DDNQDNENDG DDESMEVELH NEEMAEISNP FR
//