FEN2_YEAST
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 03-AUG-2022, entry version 152.
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; 44.
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; P25621; -.
DR PRIDE; P25621; -.
DR EnsemblFungi; YCR028C_mRNA; YCR028C; YCR028C.
DR GeneID; 850394; -.
DR KEGG; sce:YCR028C; -.
DR SGD; S000000623; FEN2.
DR VEuPathDB; FungiDB:YCR028C; -.
DR eggNOG; KOG2533; Eukaryota.
DR HOGENOM; CLU_001265_4_2_1; -.
DR InParanoid; P25621; -.
DR OMA; FPDTPRN; -.
DR BioCyc; YEAST:G3O-29343-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0015233; F:pantothenate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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
