ID   CPAT_ASPOZ              Reviewed;         496 AA.
AC   F5HN69;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=MFS transporter cpaT {ECO:0000303|PubMed:21608094};
DE   AltName: Full=Cyclopiazonic acid biosynthesis cluster protein T {ECO:0000303|PubMed:21608094};
GN   Name=cpaT {ECO:0000303|PubMed:21608094};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=NBRC 4177;
RX   PubMed=21608094; DOI=10.1002/cbic.201000672;
RA   Kato N., Tokuoka M., Shinohara Y., Kawatani M., Uramoto M., Seshime Y.,
RA   Fujii I., Kitamoto K., Takahashi T., Takahashi S., Koyama Y., Osada H.;
RT   "Genetic safeguard against mycotoxin cyclopiazonic acid production in
RT   Aspergillus oryzae.";
RL   ChemBioChem 12:1376-1382(2011).
CC   -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC       biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a
CC       nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole
CC       tetramic acid scaffold. {ECO:0000269|PubMed:21608094}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Has no significant effect on the synthesis of 2-
CC       oxocyclopiazonic acid, cyclopiazonic acid (CPA) and their biosynthetic
CC       intermediates. {ECO:0000269|PubMed:21608094}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB506492; BAK26557.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5HN69; -.
DR   VEuPathDB; FungiDB:AO090026000005; -.
DR   OMA; GLQMYDG; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..496
FT                   /note="MFS transporter cpaT"
FT                   /id="PRO_0000445390"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   496 AA;  53808 MW;  E341E4067CB9B122 CRC64;
     MGHQEEPPRI CKTPSGHEQG EGPAEKTSKP STEEVGWDGP TDPARPVNWS RKKKWWNMGI
     ISYLTFLTPL TSSIVAPAQG LVMKDFHSTN RTLASFVVSI YLVGFAVGPL FLAPLSEIYG
     RLRVYQVGTF IFTIWNIAGA VAPNVGALLV FRLFAGISGS GPVTLGAGSV ADMFARQERG
     VAMSLYGLGP LLGPVIGPIA GGYLSQAQGW RWVFWLLAIV SGVAVILVLF VLSESYEPVL
     LRQKAKRIRR ENSSVEVNAG QALKLDSRKV FIQAITRPTK LLFLTPNVAL FSLYTGVVFG
     YLYLLFTTVT EVYETTYHFS QGATGLVYIG IGVGALIGIS CFGALSDKIQ NILIARNNGQ
     AEPEFRLPPL IPGSFLIPIG LFWYGWSTQM HIHWIMPIIG LGWVGCGMIA TLLPIQAYLV
     DAFGEYAASA IAANTVVRSI VGAFLPLAGP SMYATLGLGW GNSLLGFVAL GLLPVPVVFY
     FYGKKIRMNS RYQVSV