ID   CNSO_PENEN              Reviewed;         518 AA.
AC   A0A0A2IBP6;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=MFS-type transporter cnsO {ECO:0000303|PubMed:25571861};
DE   AltName: Full=Communesin biosynthesis cluster protein O {ECO:0000303|PubMed:25571861};
GN   Name=cnsO {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055490;
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8;
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
RN   [2]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=25571861; DOI=10.1002/anie.201411297;
RA   Lin H.C., Chiou G., Chooi Y.H., McMahon T.C., Xu W., Garg N.K., Tang Y.;
RT   "Elucidation of the concise biosynthetic pathway of the communesin indole
RT   alkaloids.";
RL   Angew. Chem. Int. Ed. 54:3004-3007(2015).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of communesins, a prominent class of indole alkaloids
CC       with great potential as pharmaceuticals (PubMed:25571861). With the MFS
CC       transporter cnsL, is most likely responsible for cummunesins secretion
CC       and thereby may contribute to intrinsic resistance (Probable).
CC       {ECO:0000269|PubMed:25571861, ECO:0000305|PubMed:25571861}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {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; JQFZ01000090; KGO59708.1; -; Genomic_DNA.
DR   RefSeq; XP_016600821.1; XM_016742823.1.
DR   AlphaFoldDB; A0A0A2IBP6; -.
DR   SMR; A0A0A2IBP6; -.
DR   EnsemblFungi; KGO40484; KGO40484; PEXP_030600.
DR   EnsemblFungi; KGO59708; KGO59708; PEX2_055490.
DR   GeneID; 27678242; -.
DR   HOGENOM; CLU_001265_0_1_1; -.
DR   OrthoDB; 619250at2759; -.
DR   PhylomeDB; A0A0A2IBP6; -.
DR   Proteomes; UP000030143; 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   Gene3D; 1.20.1250.20; -; 2.
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   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..518
FT                   /note="MFS-type transporter cnsO"
FT                   /id="PRO_0000446472"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   518 AA;  56864 MW;  DDB45E6942E1A290 CRC64;
     MESTDSSPPL SMTDTEKKGD AVTTVTDESS VSEYERFLHL ENVFSGASRK KLLRKLDLRL
     LPTLSFLYLM CSLDKSNAGN AKLFGLLEDL GMSGTQYNLA LMYFFFTYGL SEPVSNIMLR
     RVGPKIWFPF IVCAWGLITT LTSQASSYAG FVVIRLMLGI TEAGLYPGAY FILSMWYTPK
     EIGTRMAIFY GANTTAGAFG GVIAYGVGSL DGNLGWRAWR WLFLIEGCIT IFAGLACLFC
     LPAFPHQYQA GKGTKWLTDE ELEYASLRVK YANGPVSSTY TFRWSDVVAA AKDRKTYFMM
     MLFWWGGSVP TYSLSYTLPT MVANLGYTAV KAQVMTTPPY IFATCVCVAV GYISDQTQRR
     YLCIMGAYTL GLIGIIILWI TVHHPSIPGV SYFAIFLAAA GYSAQAPIVG AWTASNITNP
     SKRAAAIGLL MLLGSVGGGS IGSNIYISSE APTYPLGFGF SVGATVLGAM IPATIHWFLM
     RKENKRRGGL DVAEIERKYT TEELGEMGED SPLFRFVL