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UAPC_EMENI
ID   UAPC_EMENI              Reviewed;         580 AA.
AC   P48777; C8V1W9; Q5AYA0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Purine permease;
GN   Name=uapC; ORFNames=AN6730;
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 [GENOMIC DNA].
RX   PubMed=7721763; DOI=10.1074/jbc.270.15.8610;
RA   Diallinas G., Gorfinkiel L., Arst H.N. Jr., Cecchetto G., Scazzocchio C.;
RT   "Genetic and molecular characterization of a gene encoding a wide
RT   specificity purine permease of Aspergillus nidulans reveals a novel family
RT   of transporters conserved in prokaryotes and eukaryotes.";
RL   J. Biol. Chem. 270:8610-8622(1995).
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: Able to transport with low efficiency all natural purines as
CC       well as purine analogs.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Inducible by 2-thiouric acid, and highly repressible by
CC       ammonium.
CC   -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC       2.A.40) family. {ECO:0000305}.
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DR   EMBL; X79796; CAA56190.1; -; Genomic_DNA.
DR   EMBL; AACD01000112; EAA58548.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF71344.1; -; Genomic_DNA.
DR   PIR; A56382; A56382.
DR   RefSeq; XP_664334.1; XM_659242.1.
DR   AlphaFoldDB; P48777; -.
DR   SMR; P48777; -.
DR   STRING; 162425.CADANIAP00007522; -.
DR   TCDB; 2.A.40.4.4; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR   EnsemblFungi; CBF71344; CBF71344; ANIA_06730.
DR   EnsemblFungi; EAA58548; EAA58548; AN6730.2.
DR   GeneID; 2870356; -.
DR   KEGG; ani:AN6730.2; -.
DR   VEuPathDB; FungiDB:AN6730; -.
DR   eggNOG; ENOG502QQD4; Eukaryota.
DR   HOGENOM; CLU_017959_7_0_1; -.
DR   InParanoid; P48777; -.
DR   OMA; RKSAPFF; -.
DR   OrthoDB; 387031at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:AspGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR   GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IMP:AspGD.
DR   GO; GO:0042907; F:xanthine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006863; P:purine nucleobase transport; IMP:AspGD.
DR   GO; GO:0042906; P:xanthine transport; IBA:GO_Central.
DR   InterPro; IPR006043; NCS2.
DR   InterPro; IPR006042; Xan_ur_permease.
DR   Pfam; PF00860; Xan_ur_permease; 1.
DR   TIGRFAMs; TIGR00801; ncs2; 1.
DR   PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..580
FT                   /note="Purine permease"
FT                   /id="PRO_0000165953"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        151
FT                   /note="A -> G (in Ref. 1; CAA56190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="R -> P (in Ref. 1; CAA56190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="S -> C (in Ref. 1; CAA56190)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  61349 MW;  8F3B8F9BF6C129CF CRC64;
     MDGPDQIGPD VRPRRTFGDR VRRAARAFTT RDGLIGDYDY GFLFTPRLPF VKQKRRAAPF
     FGLEDKIPLV LALLLGLQHA LAMLAGVITP PILLAGSSGA NFGADESQYL VSTSLIVSGL
     LSAVQMFRLH VYKTRYYVGT GLVSVVGTSF ATITVATGTF NQMYSTGYCP VDGSGNRLPC
     PKGYGALLAT SCLCSLLEIG LSFMSSRLLK ALFPPIVTGP TVFLIGASLI GNAMKDWAGG
     SGTCSSNPGN GALCPSADAP HPLPWGSAEF IGLGFLVFAT IILCERFGSP IMKSCAVIVG
     LLVGCIVAAA CGYFDRSGID AAPVASFIWV KTFPLTIYAP LILPLLAVYM VIMMESIGDI
     TATCDVSRLQ VEGATFDSRI QGGVLGNGIT CLLAGLCTIT PMSVFAQNNG VIALTRCANR
     KAGYCCCFFL VVMGIFAKFA AALVAIPSSV LGGMTTFLFS SVAISGVRIM CSVDWTRRNR
     FILTASFAVG MAATLVPDWF SYFFTYSGDN HALEGLLQAV ELVMANGFAV TGFLGLLLNL
     ILPEDMEEDV VESEEDYEAT TVVGMQGGSE PGSSGQNVKA
 
 
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