FCY2_YEAST
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 03-AUG-2022, entry version 174.
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;
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; 111.
DR DIP; DIP-7593N; -.
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 MaxQB; P17064; -.
DR PaxDb; P17064; -.
DR PRIDE; P17064; -.
DR EnsemblFungi; YER056C_mRNA; YER056C; YER056C.
DR GeneID; 856783; -.
DR KEGG; sce:YER056C; -.
DR SGD; S000000858; FCY2.
DR VEuPathDB; FungiDB:YER056C; -.
DR eggNOG; ENOG502QQ8Y; Eukaryota.
DR GeneTree; ENSGT00940000176331; -.
DR HOGENOM; CLU_026016_2_2_1; -.
DR InParanoid; P17064; -.
DR OMA; ASWQIAF; -.
DR BioCyc; YEAST:G3O-30233-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 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 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
