FCY22_YEAST
ID FCY22_YEAST Reviewed; 530 AA.
AC Q12119; D3DLW5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Purine-cytosine permease FCY22;
DE Short=PCP FCY22;
DE AltName: Full=Cytosine/purine transport protein FCY22;
DE AltName: Full=Fluorocytosine resistance protein 22;
GN Name=FCY22; Synonyms=FCYX; OrderedLocusNames=YER060W-A;
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 (APR-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).
CC -!- FUNCTION: Probable purine-cytosine permease. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR EMBL; X97346; CAA66033.1; -; Genomic_DNA.
DR EMBL; U18813; AAB64610.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07719.1; -; Genomic_DNA.
DR RefSeq; NP_010982.1; NM_001180858.1.
DR AlphaFoldDB; Q12119; -.
DR BioGRID; 36802; 104.
DR DIP; DIP-8900N; -.
DR STRING; 4932.YER060W-A; -.
DR PaxDb; Q12119; -.
DR PRIDE; Q12119; -.
DR EnsemblFungi; YER060W-A_mRNA; YER060W-A; YER060W-A.
DR GeneID; 856789; -.
DR KEGG; sce:YER060W-A; -.
DR SGD; S000002958; FCY22.
DR VEuPathDB; FungiDB:YER060W-A; -.
DR eggNOG; ENOG502QQ8Y; Eukaryota.
DR GeneTree; ENSGT00940000176331; -.
DR HOGENOM; CLU_026016_2_2_1; -.
DR InParanoid; Q12119; -.
DR OMA; GRWANYE; -.
DR BioCyc; YEAST:G3O-30354-MON; -.
DR PRO; PR:Q12119; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; Q12119; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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 3: Inferred from homology;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Purine-cytosine permease FCY22"
FT /id="PRO_0000197922"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40039"
SQ SEQUENCE 530 AA; 57327 MW; 620FF2F2F3A2702D CRC64;
MPEKLAMSMV DIKDAGSELR DLESGALDTK SSAADVYYEG VELHRTNEFI DNKPSFFNRI
AAALNAETKG IEPVTEDEKN DDSILNAATI WFSANMVIVA YSVGALGPLV FGLNFGQSVL
VIIFFNILGL IPVALFSLFG VELGLRQMIL SRYLAGNITA RFFSLVNVIA CVGWCVLNIS
VSAQLLNMVN EGSGHNCPIW AGCLIIAGGT VLVTFFGYSV VHAYEKWSWV PNFAAFLVII
AQLSRSGKFK GGEWVGGATT AGGVLSFGSS VFGSAAGWAT YAADYTVYMP KTTSKYKIFF
SVVAGLAFPL FFTMILGAAC GMAALNDPTW KSYYDKNAMG GVIYAILVPN SLNGFGQFCC
VLLALSTVAN NVPGMYTVAL SAQALWAPLA KIPRVVWTMA GNAATLGISI PATYYFDGFM
ENFMDSIGYY LAIYIAIACS EHFIYRRSFS AYNIDDWDNW EHLPIGIAGT AALIAGAFGV
ALGMCQTYWV GEISRLIGEY GGDIGFELGG SWAFIIYNIV RPLELKYFGR
