ID   CTB4_CERBT              Reviewed;         512 AA.
AC   A0A2G5ID46;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Cercosporin MFS transporter CTB4 {ECO:0000303|PubMed:29844193};
DE   AltName: Full=Cercosporin toxin biosynthesis cluster protein 4 {ECO:0000303|PubMed:29844193};
GN   Name=CTB4 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00831;
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=09-40;
RX   PubMed=29844193; DOI=10.1073/pnas.1712798115;
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M. II, Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Gene cluster conservation provides insight into cercosporin biosynthesis
RT   and extends production to the genus Colletotrichum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E5459-E5466(2018).
RN   [2]
RP   REVIEW ON CERCOSPORIN.
RX   PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA   Daub M.E., Ehrenshaft M.;
RT   "The photoactivated cercospora toxin cercosporin: contributions to plant
RT   disease and fundamental biology.";
RL   Annu. Rev. Phytopathol. 38:461-490(2000).
CC   -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC       biosynthesis of cercosporin, a light-activated, non-host-selective
CC       toxin (By similarity). The perylenequinone chromophore of cercosporin
CC       absorbs light energy to attain an electronically-activated triplet
CC       state and produces active oxygen species such as the hydroxyl radical,
CC       superoxide, hydrogen peroxide or singlet oxygen upon reaction with
CC       oxygen molecules (PubMed:11701851). These reactive oxygen species cause
CC       damage to various cellular components including lipids, proteins and
CC       nucleic acids (PubMed:11701851). Responsible for secretion and
CC       accumulation of cercosporin, but does not play any roles in self-
CC       protection against the toxicity of cercosporin (By similarity).
CC       {ECO:0000250|UniProtKB:A0ST42, ECO:0000303|PubMed:11701851}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC       {ECO:0000255}.
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DR   EMBL; LKMD01000100; PIB02403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5ID46; -.
DR   OrthoDB; 911338at2759; -.
DR   Proteomes; UP000230605; Chromosome 1.
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; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="Cercosporin MFS transporter CTB4"
FT                   /id="PRO_0000449867"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   512 AA;  56047 MW;  BD321384E9191C90 CRC64;
     MALPITDDDL DGLKQPYVTF SSGSASPPQS TTDAMDLEEQ VLDAIKSDAF LVDWVGEDDK
     GNPQNLPYWR KWVITMSLAL YALSTTFSSS VFGAATHVLA EEFALPAETV VLGCTSLFMV
     GFATGPIFWG PFSEAFGRTR PLLAGYLAFA VLQLPIADAR SLTSICILRF LGGFFGAAPS
     SILSGILADI WSPRERGFAM PTVGAFLTIG PILGPLIGSV LVQSVLGWRW IANVVAIASF
     FIAVFTFPFL PETYTPLLLA RRAERMRHMT RNWAYRSKSE EAQSSIGDFA ERYLLRPARM
     LALEPILLMM TLYVSVSFGL LYNFFLAYPT SFIQERGWDQ TTASLPLISI LVGVIIAGAL
     LSFTTNSRWA PNAKEGRPQE TRLLLMMVGA VSLPAGMFLF AWTSSATMNP WPQILSGIPT
     GFGIHLINMQ GMNYIIDSYK IYANSAIAAN TFLRSLFAAG FPILATSMYA AIGVKWGTTI
     LALLAVAMIP IPILFYYFGA KIRAKSKWQP PL