FCY2_EMENI
ID FCY2_EMENI Reviewed; 508 AA.
AC C8V329; B1PXD0; Q5B0B3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Purine-cytosine permease fcyB;
DE Short=PCP fcyB;
DE AltName: Full=Cytosine/purine transport protein fcyB;
DE AltName: Full=Fluorocytosine resistance protein fcyB;
GN Name=fcyB; ORFNames=AN10767;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18384518; DOI=10.1111/j.1365-2958.2008.06198.x;
RA Vlanti A., Diallinas G.;
RT "The Aspergillus nidulans FcyB cytosine-purine scavenger is highly
RT expressed during germination and in reproductive compartments and is
RT downregulated by endocytosis.";
RL Mol. Microbiol. 68:959-977(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: This permease has a broad specificity towards purines, and
CC also transports cytosine, but neither uracil nor thymine. Contributes
CC very little in purine uptake. Its major role may be the uptake of
CC cytosine. {ECO:0000269|PubMed:18384518}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for adenine {ECO:0000269|PubMed:18384518};
CC KM=11.5 uM for guanine {ECO:0000269|PubMed:18384518};
CC KM=20 uM for hypoxanthine {ECO:0000269|PubMed:18384518};
CC KM=20 uM for cytosine {ECO:0000269|PubMed:18384518};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18384518};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18384518}.
CC -!- INDUCTION: Highly induced during germination and drops to a low
CC constant level throughout vegetative development. Repressed by
CC ammonium. Down-regulated by endocytosis in responde to ammonia or the
CC presence of cytosine. {ECO:0000269|PubMed:18384518}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA57658.1; Type=Erroneous gene model prediction; Note=The predicted gene AN6017 has been split into 2 genes: AN10765 and AN10767.; Evidence={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; EU502921; ACA81792.1; -; mRNA.
DR EMBL; AACD01000103; EAA57658.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001301; CBF70354.1; -; Genomic_DNA.
DR RefSeq; XP_663621.1; XM_658529.1.
DR AlphaFoldDB; C8V329; -.
DR SMR; C8V329; -.
DR STRING; 162425.CADANIAP00007001; -.
DR TCDB; 2.A.39.2.4; the nucleobase:cation symporter-1 (ncs1) family.
DR EnsemblFungi; CBF70354; CBF70354; ANIA_10767.
DR EnsemblFungi; EAA57658; EAA57658; AN6017.2.
DR GeneID; 2870983; -.
DR KEGG; ani:AN6017.2; -.
DR VEuPathDB; FungiDB:AN10767; -.
DR eggNOG; ENOG502QQ8Y; Eukaryota.
DR HOGENOM; CLU_019836_0_0_1; -.
DR InParanoid; C8V329; -.
DR OMA; ASWQIAF; -.
DR OrthoDB; 488201at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006863; P:purine nucleobase transport; IDA:AspGD.
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.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="Purine-cytosine permease fcyB"
FT /id="PRO_0000413173"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 508 AA; 55197 MW; 84E1E168D6CF3D4A CRC64;
MAGAFDFDLE KNPPVVQSTA DNSSDGAVPG ETFTYGDSTY AKIQRLAAEL NIEQRGIERV
PAAEQTDTSV FNIGSMWLAA NMVVSSFAIG VLGKSVYSLG FVDAILTVLF FNLLGIMTVC
FFSCFGPFGL RQMVFSRLWF GWYVTKGFAV LNILACLGWS AANAIVGAQM LHAVNSDVPG
FAAILIISIC TLLVTFAGYK VVHLYEYWSW IPTFIVFMII LGTFAHSGDF QNIPMGVGTS
EMGSVLSFGS AVYGFATGWT SYAADYTVYQ PANRSKRKIF LSTWLGLIVP LLFVEMLGVA
VMTATDIKGS KYDVGYATSG NGGLIAAVLQ PLGGFGDFCL VILALSIVAN NCPNFYSVAL
TVQVLSRYAQ RVPRFIWTLF GTGVSIAIAI PGYSHFETVL ENFMNFIAYW LAIYSAIAIM
DHFVFKRGFS GYVVENFDKR EKLPVGIAAT IAFGFGVAGM ITGMSQPWYV GPIARHAAGG
DVGFELGFAF AAFSYLCLRP FEIKFFGR
