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 22-FEB-2023, entry version 16. 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}. 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; LKMD01000100; PIB02403.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2G5ID46; -. DR OrthoDB; 3672446at2759; -. DR Proteomes; UP000230605; Chromosome 1. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro. DR CDD; cd17323; MFS_Tpo1_MDR_like; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR23502; MAJOR FACILITATOR SUPERFAMILY; 1. DR PANTHER; PTHR23502:SF130; MFS DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 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 //