ID   PC17_PENCR              Reviewed;         543 AA.
AC   A0A0E3D8L1;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=MFS-type transporter PC-17 {ECO:0000303|PubMed:26213965};
DE   AltName: Full=Penitrem biosynthesis cluster protein PC-17 {ECO:0000303|PubMed:26213965};
GN   Name=PC-17 {ECO:0000303|PubMed:26213965};
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
RC   STRAIN=PN2402;
RX   PubMed=26213965; DOI=10.3390/toxins7082701;
RA   Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT   "Molecular cloning and functional analysis of gene clusters for the
RT   biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT   janthinellum.";
RL   Toxins 7:2701-2722(2015).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of the indole diterpenes penitrems (PubMed:26213965).
CC       May be involved in the efflux of penitrems (Probable).
CC       {ECO:0000269|PubMed:26213965, ECO:0000305|PubMed:26213965}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; KC963408; AGZ20198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8L1; -.
DR   SMR; A0A0E3D8L1; -.
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   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; 2.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..543
FT                   /note="MFS-type transporter PC-17"
FT                   /id="PRO_0000446592"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        517..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  58374 MW;  1258F4FEE6F76CA5 CRC64;
     MPDKGNIQLD TLQHQDHSQE TASRYGGGSQ LPEQERLDTN IQDDPVEYPG LIRVILITLG
     VALCSFCVGL DNTILATAIP KITSEFNSLE DMSWYVSAYL LVTSAFILSF GKIYTYYSVK
     WTYLVSLGLF ELGSLICATT PSSAGLIVGR AISGMGSAGI FPGSVIILSN IAPLHQRPLL
     TAFIGIMSGI ATVTGPILGG VFTDRLSWRW CFYINLPIGG VTAVVVFFFL KTTKVKKNVP
     TSHKIKGLDW IGTVVFIPAI VSLLLALQWG GARYNWQNVR IIMLFIIAGV LGIVWLLIQC
     WKQEEATIPP RLMQRRSIVG TCVYTIPFVG CVIVFGYYLP IWFQSVKGVS ASQSGIMNLP
     TVVGTIVVGL LSSVIIMKVG YMVPFLVLGS VLLAVGAGLC STFQRSSGSA EWIGYQAMIG
     MGSGLGYQLP LLVVQADVPA ADVPVATAVV IFMQNLAGSI FSAIAQTVFQ NQLAKSVQIL
     VPSVNPKSIL DGGTVGLSDR FPSDVLPSIL QAYNTAVTHT FYAGVAAASL SVFGAFIVRW
     NVT