ID   FCY2_YEAST              Reviewed;         533 AA.
AC   P17064; D3DLV9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   04-NOV-2026, entry version 189.
DE   RecName: Full=Purine-cytosine permease FCY2;
DE            Short=PCP FCY2;
DE   AltName: Full=Cytosine/purine transport protein FCY2;
DE   AltName: Full=Fluorocytosine resistance protein 2;
GN   Name=FCY2; OrderedLocusNames=YER056C;
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 28383 / FL100 / VTT C-80102;
RX   PubMed=2191181; DOI=10.1111/j.1365-2958.1990.tb00627.x;
RA   Weber E., Rodriguez C., Chevalier M.R., Jund R.;
RT   "The purine-cytosine permease gene of Saccharomyces cerevisiae: primary
RT   structure and deduced protein sequence of the FCY2 gene product.";
RL   Mol. Microbiol. 4:585-596(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868; DOI=10.1038/387s078;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-533.
RX   PubMed=6300123; DOI=10.1016/s0021-9258(18)32564-x;
RA   Hinnebusch A.G., Fink G.R.;
RT   "Repeated DNA sequences upstream from HIS1 also occur at several other co-
RT   regulated genes in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 258:5238-5247(1983).
RN   [5]
RP   MUTAGENESIS.
RX   PubMed=7762297; DOI=10.1002/yea.320110103;
RA   Rodriguez C., Bloch J.C., Chevalier M.R.;
RT   "The immunodetected yeast purine-cytosine permease is not N-linked
RT   glycosylated, nor are glycosylation sequences required to have a functional
RT   permease.";
RL   Yeast 11:15-23(1995).
RN   [6]
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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).
RN   [9]
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).
RN   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP   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: This permease has a broad specificity towards purines, and
CC       also transport cytosine and 5-methylcytosine but neither uracil nor
CC       thymine.
CC   -!- INTERACTION:
CC       P17064; P38264: PHO88; NbExp=3; IntAct=EBI-2047850, EBI-13350;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Not N-glycosylated.
CC   -!- MISCELLANEOUS: Present with 23600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC       {ECO:0000305}.
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DR   EMBL; X51751; CAA36040.1; -; Genomic_DNA.
DR   EMBL; U18813; AAB64592.1; -; Genomic_DNA.
DR   EMBL; V01306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006939; DAA07713.1; -; Genomic_DNA.
DR   PIR; S50559; GRBYCP.
DR   RefSeq; NP_010976.1; NM_001178947.1.
DR   AlphaFoldDB; P17064; -.
DR   BioGRID; 36796; 115.
DR   DIP; DIP-7593N; -.
DR   FunCoup; P17064; 84.
DR   IntAct; P17064; 6.
DR   MINT; P17064; -.
DR   STRING; 4932.YER056C; -.
DR   TCDB; 2.A.39.2.1; the nucleobase:cation symporter-1 (ncs1) family.
DR   iPTMnet; P17064; -.
DR   PaxDb; 4932-YER056C; -.
DR   PeptideAtlas; P17064; -.
DR   EnsemblFungi; YER056C_mRNA; YER056C; YER056C.
DR   GeneID; 856783; -.
DR   KEGG; sce:YER056C; -.
DR   AGR; SGD:S000000858; -.
DR   SGD; S000000858; FCY2.
DR   VEuPathDB; FungiDB:YER056C; -.
DR   eggNOG; ENOG502QQ8Y; Eukaryota.
DR   HOGENOM; CLU_026016_2_2_1; -.
DR   InParanoid; P17064; -.
DR   OMA; AACYYFQ; -.
DR   OrthoDB; 2116389at2759; -.
DR   BioCyc; YEAST:G3O-30233-MONOMER; -.
DR   BioGRID-ORCS; 856783; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P17064; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P17064; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015212; F:cytidine transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0015861; P:cytidine transport; IDA:SGD.
DR   GO; GO:0015856; P:cytosine transport; IDA:SGD.
DR   GO; GO:0072530; P:purine-containing compound transmembrane transport; IDA:SGD.
DR   CDD; cd11484; SLC-NCS1sbd_CobB-like; 1.
DR   FunFam; 1.10.4160.10:FF:000002; Purine-cytosine permease fcyB; 1.
DR   Gene3D; 1.10.4160.10; Hydantoin permease; 1.
DR   InterPro; IPR012681; NCS1.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR026030; Pur-cyt_permease_Fcy2/21/22.
DR   NCBIfam; TIGR00800; ncs1; 1.
DR   PANTHER; PTHR31806; PURINE-CYTOSINE PERMEASE FCY2-RELATED; 1.
DR   PANTHER; PTHR31806:SF1; PURINE-CYTOSINE PERMEASE FCY2-RELATED; 1.
DR   Pfam; PF02133; Transp_cyt_pur; 1.
DR   PIRSF; PIRSF002744; Pur-cyt_permease; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..533
FT                   /note="Purine-cytosine permease FCY2"
FT                   /id="PRO_0000197920"
FT   TOPO_DOM        1..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..347
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        368..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        419..465
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        486..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          165..184
FT                   /note="Surface seeking"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        192
FT                   /note="V -> M (in Ref. 1; CAA36040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        261
FT                   /note="A -> G (in Ref. 1; CAA36040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="D -> Y (in Ref. 4; V01306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  58201 MW;  762DDB9483A546AC CRC64;
     MLEEGNNVYE IQDLEKRSPV IGSSLENEKK VAASETFTAT SEDDQQYIVE SSEATKLSWF
     HKFFASLNAE TKGVEPVTED EKTDDSILNA ASMWFSANMV IASYALGALG PMVFGLNFGQ
     SVLVIIFFNI MGLIFVAFFS VFGAELGLRQ MILSRYLVGN VTARIFSLIN VIACVGWGIV
     NTSVSAQLLN MVNEGSGHVC PIWAGCLIII GGTVLVTFFG YSVIHAYEKW SWVPNFAVFL
     VIIAQLSRSG KFKGGEWVGG ATTAGSVLSF GSSIFGFAAG WTTYAADYTV YMPKSTNKYK
     IFFSLVAGLA FPLFFTMILG AASAMAALND PTWKAYYDKN AMGGVIYAIL VPNSLNGFGQ
     FCCVLLALST IANNIPNMYT VALSAQALWA PLAKIPRVVW TMAGNAATLG ISIPATYYFD
     GFMENFMDSI GYYLAIYIAI SCSEHFFYRR SFSAYNIDDW DNWEHLPIGI AGTAALIVGA
     FGVALGMCQT YWVGEIGRLI GKYGGDIGFE LGASWAFIIY NILRPLELKY FGR
//