ID   FUI1_YEAST              Reviewed;         639 AA.
AC   P38196; D6VPV6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Uridine permease;
GN   Name=FUI1; OrderedLocusNames=YBL042C; ORFNames=YBL0406;
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=7871888; DOI=10.1002/yea.320101113;
RA   de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA   Goffeau A.;
RT   "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT   chromosome II reveals homologues to bacterial proline synthetase and murine
RT   alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL   Yeast 10:1489-1496(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(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   CHARACTERIZATION.
RX   PubMed=9485596; DOI=10.1111/j.1574-6968.1998.tb12843.x;
RA   Wagner R., de Montigny J., de Wergifosse P., Souciet J.-L., Potier S.;
RT   "The ORF YBL042 of Saccharomyces cerevisiae encodes a uridine permease.";
RL   FEMS Microbiol. Lett. 159:69-75(1998).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=10827169; DOI=10.1074/jbc.m000239200;
RA   Vickers M.F., Yao S.Y., Baldwin S.A., Young J.D., Cass C.E.;
RT   "Nucleoside transporter proteins of Saccharomyces cerevisiae. Demonstration
RT   of a transporter (FUI1) with high uridine selectivity in plasma membranes
RT   and a transporter (FUN26) with broad nucleoside selectivity in
RT   intracellular membranes.";
RL   J. Biol. Chem. 275:25931-25938(2000).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND SER-56, AND
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   [8]
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   [9]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-635, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: High-affinity transport of uridine.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC       {ECO:0000305}.
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DR   EMBL; X78214; CAA55059.1; -; Genomic_DNA.
DR   EMBL; Z35803; CAA84862.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07076.1; -; Genomic_DNA.
DR   PIR; S45776; S45776.
DR   RefSeq; NP_009511.1; NM_001178282.1.
DR   AlphaFoldDB; P38196; -.
DR   SMR; P38196; -.
DR   BioGRID; 32655; 56.
DR   DIP; DIP-1321N; -.
DR   IntAct; P38196; 6.
DR   MINT; P38196; -.
DR   STRING; 4932.YBL042C; -.
DR   TCDB; 2.A.39.3.3; the nucleobase:cation symporter-1 (ncs1) family.
DR   iPTMnet; P38196; -.
DR   MaxQB; P38196; -.
DR   PaxDb; 4932-YBL042C; -.
DR   PeptideAtlas; P38196; -.
DR   EnsemblFungi; YBL042C_mRNA; YBL042C; YBL042C.
DR   GeneID; 852238; -.
DR   KEGG; sce:YBL042C; -.
DR   AGR; SGD:S000000138; -.
DR   SGD; S000000138; FUI1.
DR   VEuPathDB; FungiDB:YBL042C; -.
DR   eggNOG; KOG2466; Eukaryota.
DR   GeneTree; ENSGT00940000176299; -.
DR   HOGENOM; CLU_021555_2_2_1; -.
DR   InParanoid; P38196; -.
DR   OMA; CIPTYML; -.
DR   OrthoDB; 1218881at2759; -.
DR   BioCyc; YEAST:G3O-28943-MONOMER; -.
DR   BioGRID-ORCS; 852238; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P38196; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38196; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR   GO; GO:0015862; P:uridine transport; IDA:SGD.
DR   CDD; cd11482; SLC-NCS1sbd_NRT1-like; 1.
DR   Gene3D; 1.10.4160.10; Hydantoin permease; 1.
DR   InterPro; IPR012681; NCS1.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR   NCBIfam; TIGR00800; ncs1; 1.
DR   PANTHER; PTHR30618; NCS1 FAMILY PURINE/PYRIMIDINE TRANSPORTER; 1.
DR   PANTHER; PTHR30618:SF5; URIDINE PERMEASE; 1.
DR   Pfam; PF02133; Transp_cyt_pur; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..639
FT                   /note="Uridine permease"
FT                   /id="PRO_0000197923"
FT   TOPO_DOM        1..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..416
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        478..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..537
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        538..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..572
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        573..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        591..639
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   CROSSLNK        635
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   639 AA;  72165 MW;  757325DEF4100399 CRC64;
     MPVSDSGFDN SSKTMKDDTI PTEDYEEITK ESEMGDATKI TSKIDANVIE KKDTDSENNI
     TIAQDDEKVS WLQRVVEFFE VKNDSTDLAD HKPENPIRTF KDLQESLRST YLYNTDLRPV
     EAKRRTWTWK QYIFFWISGS FNVNTWQISA TGLQLGLNWW QTWICIWVGY TFVAFFLILG
     SKVGNNYHIS FPISSRVSFG IYFSIWIVIN RVVMACVWNS TLAYIGSQCV QLMLKAIFGT
     NLNTRIKDTI KNPNLTNFEF MCFMVFWVAC LPFLWFPPDK LRHIFALKSA ITPFAAFGFL
     IWTLCKAKGH LALGSLNDNG GAISKTVLAW SVIRAIMSAL DNFSTLILNA PDFTRFGKTY
     KSSVYSQLIA LPVCYAIISL IGILSVSAAY TLYGVNYWSP LDILNRYLDN YTSGNRAGVF
     LISFIFAFDQ LGANLSGNSI PAGTDLTALL PKFINIRRGS YICALISLAI CPWDLLSSSS
     KFTTALAAYA VFLSAIAGVI SADYFIVRKG YVNIFHCYTD KPGSYYMYNK YGTNWRAVVA
     YIFGIAPNFA GFLGSVGVSV PIGAMKVYYL NYFVGYLLAA LSYCILVYFY PIKGIPGDAK
     ITDRKWLEEW VEVEEFGTER EAFEEYGGVS TGYEKIRYI
//