FCY21_YEAST
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 03-AUG-2022, entry version 149.
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;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 48.
DR MINT; P40039; -.
DR STRING; 4932.YER060W; -.
DR iPTMnet; P40039; -.
DR PaxDb; P40039; -.
DR PRIDE; P40039; -.
DR EnsemblFungi; YER060W_mRNA; YER060W; YER060W.
DR GeneID; 856788; -.
DR KEGG; sce:YER060W; -.
DR SGD; S000000862; FCY21.
DR VEuPathDB; FungiDB:YER060W; -.
DR eggNOG; ENOG502QQ8Y; Eukaryota.
DR GeneTree; ENSGT00940000176331; -.
DR HOGENOM; CLU_026016_2_2_1; -.
DR InParanoid; P40039; -.
DR OMA; ADYNRNC; -.
DR BioCyc; YEAST:G3O-30237-MON; -.
DR PRO; PR:P40039; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40039; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISA:SGD.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015856; P:cytosine transport; IMP:SGD.
DR GO; GO:0072530; P:purine-containing compound transmembrane transport; ISA:SGD.
DR InterPro; IPR012681; NCS1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR026030; Pur-cyt_permease_Fcy2/21/22.
DR PANTHER; PTHR31806; PTHR31806; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR PIRSF; PIRSF002744; Pur-cyt_permease; 1.
DR TIGRFAMs; TIGR00800; ncs1; 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
