ID   FCY21_YEAST             Reviewed;         528 AA.
AC   P40039; D3DLW4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   04-NOV-2026, entry version 166.
DE   RecName: Full=Purine-cytosine permease FCY21;
DE            Short=PCP FCY21;
DE   AltName: Full=Cytosine/purine transport protein FCY21;
DE   AltName: Full=Fluorocytosine resistance protein 21;
GN   Name=FCY21; Synonyms=FCYY; OrderedLocusNames=YER060W;
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;
RA   Straub M.L., Souciet J.-L., Potier S., de Montigny J.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND THR-46, AND
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).
CC   -!- FUNCTION: Probable purine-cytosine permease. {ECO:0000250}.
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; X97346; CAA66032.1; -; Genomic_DNA.
DR   EMBL; U18813; AAB64596.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07718.1; -; Genomic_DNA.
DR   PIR; S50563; S50563.
DR   RefSeq; NP_010981.3; NM_001178951.3.
DR   AlphaFoldDB; P40039; -.
DR   SMR; P40039; -.
DR   BioGRID; 36801; 50.
DR   FunCoup; P40039; 57.
DR   STRING; 4932.YER060W; -.
DR   GlyGen; P40039; 1 site.
DR   iPTMnet; P40039; -.
DR   PaxDb; 4932-YER060W; -.
DR   PeptideAtlas; P40039; -.
DR   EnsemblFungi; YER060W_mRNA; YER060W; YER060W.
DR   GeneID; 856788; -.
DR   KEGG; sce:YER060W; -.
DR   AGR; SGD:S000000862; -.
DR   SGD; S000000862; FCY21.
DR   VEuPathDB; FungiDB:YER060W; -.
DR   eggNOG; ENOG502QQ8Y; Eukaryota.
DR   HOGENOM; CLU_026016_2_2_1; -.
DR   InParanoid; P40039; -.
DR   OMA; AAMHTFD; -.
DR   OrthoDB; 2116389at2759; -.
DR   BioCyc; YEAST:G3O-30237-MONOMER; -.
DR   BioGRID-ORCS; 856788; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P40039; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40039; protein.
DR   GO; GO:0005886; C:plasma membrane; ISA:SGD.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0015856; P:cytosine transport; IMP:SGD.
DR   GO; GO:0072530; P:purine-containing compound transmembrane transport; ISA: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   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..528
FT                   /note="Purine-cytosine permease FCY21"
FT                   /id="PRO_0000197921"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..260
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..416
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        438..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   528 AA;  58050 MW;  1FD333C54E81D8CA CRC64;
     MPQTHEMSLN GTQYLKYELK DLESRAHDAK TPSTNEFYDD VESHGTEELV EAKLSFLNRI
     AAGLSAETKG IEPITEDEKT DDSILNAASM WFSANMVLPA YAIGALGPMV FDLNFGQSVF
     VIIFFNLLGL VSVAFFSVFG AELGLRQMIL SRYLVGNIAA RIFSFINFIA CIGWGIVNTV
     ASSQVLNMVN PGHQCPLWAG CIVIIGATVI VTFFGYGVIH AYEKWAWVPN FAVFLVIIAR
     LARSKKFVLG EWTSGPTTAG NVLSFGSTVY GFAAGWTTYA ADYTVYMPRK TNKYKIFFSL
     VVGLATPLYF TMILGAAVAM AAIGDPAWKT YYDENSIGGL TFAVLVPNSV HGFGQFCCVL
     LSLSTIANNV PNMYTIALSV QATWEPLAKV PRVIWTLLGN AAALGIAIPA CYYFSTFMNY
     FMDSIGYYLA IYIAIACSEH FIYRRSFSAY NVDDWDSWER LPIGIAGTAA LIVGAFGVAL
     GMCQTYWVGE ISRLIGDYGG DIGFELGLSW AFIVYNIARP FELKYFGR
//