CTB4_CERNC
ID CTB4_CERNC Reviewed; 512 AA.
AC A0ST42;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Cercosporin MFS transporter CTB4 {ECO:0000303|PubMed:17250832};
DE AltName: Full=Cercosporin toxin biosynthesis cluster protein 4 {ECO:0000303|PubMed:17462021};
GN Name=CTB4 {ECO:0000303|PubMed:17250832};
OS Cercospora nicotianae (Barn spot disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=29003;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17250832; DOI=10.1016/j.febslet.2007.01.011;
RA Choquer M., Lee M.H., Bau H.J., Chung K.R.;
RT "Deletion of a MFS transporter-like gene in Cercospora nicotianae reduces
RT cercosporin toxin accumulation and fungal virulence.";
RL FEBS Lett. 581:489-494(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=17462021; DOI=10.1111/j.1365-2958.2007.05689.x;
RA Chen H., Lee M.H., Daub M.E., Chung K.R.;
RT "Molecular analysis of the cercosporin biosynthetic gene cluster in
RT Cercospora nicotianae.";
RL Mol. Microbiol. 64:755-770(2007).
RN [3]
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).
RN [4]
RP FUNCTION.
RX PubMed=26938470; DOI=10.1021/jacs.6b00633;
RA Newman A.G., Townsend C.A.;
RT "Molecular characterization of the cercosporin biosynthetic pathway in the
RT fungal plant pathogen Cercospora nicotianae.";
RL J. Am. Chem. Soc. 138:4219-4228(2016).
CC -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC biosynthesis of cercosporin, a light-activated, non-host-selective
CC toxin (PubMed:17250832, PubMed:17462021, PubMed:26938470). The
CC perylenequinone chromophore of cercosporin absorbs light energy to
CC attain an electronically-activated triplet state and produces active
CC oxygen species such as the hydroxyl radical, superoxide, hydrogen
CC peroxide or singlet oxygen upon reaction with oxygen molecules. These
CC reactive oxygen species cause damage to various cellular components
CC including lipids, proteins and nucleic acids (PubMed:11701851).
CC Responsible for secretion and accumulation of cercosporin, but does not
CC play any roles in self-protection against the toxicity of cercosporin
CC (PubMed:17250832). {ECO:0000269|PubMed:17250832,
CC ECO:0000269|PubMed:17462021, ECO:0000269|PubMed:26938470,
CC ECO:0000303|PubMed:11701851}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17250832};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cercosporin
CC cluster-specific transcription factor CTB8 (PubMed:17462021).
CC Expression is also affected by nitrogen and carbon sources and pH, and
CC is also controlled by another transcription activator, CRG1, previously
CC shown to regulate cercosporin production and resistance
CC (PubMed:17462021). {ECO:0000269|PubMed:17462021}.
CC -!- DISRUPTION PHENOTYPE: Reduces cercosporin toxin accumulation and fungal
CC virulence. {ECO:0000269|PubMed:17250832}.
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; DQ991506; ABK64181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0ST42; -.
DR SMR; A0ST42; -.
DR TCDB; 2.A.1.2.79; the major facilitator superfamily (mfs).
DR PHI-base; PHI:2329; -.
DR PHI-base; PHI:737; -.
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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport;
KW Virulence.
FT CHAIN 1..512
FT /note="Cercosporin MFS transporter CTB4"
FT /id="PRO_0000444968"
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; 55982 MW; CEEADD46ADF35BAE CRC64;
MAPPITDDDL DGLKQPYVTF SSGSASPPRS TAEAMDFEEQ ILEAIKSDAF LVDWIGEDDK
GNPQNLPYWR KWVITMSLAL YALSTTFSSS VFGAATHVLA EEFALPAETV VLGCTSLFMV
GFATGPIFWG PFSEAFGRTR PLLAGYLGFA VLQLPIADAR SLTSICILRF LGGFFGAAPS
SILSGILADI WSPRERGFAM PTVGAFLTIG PILGPLIGSV LVQSVLGWRW IANVVAIASF
LIALSTFPFL PETYTPLLLA RRAERMRHMT RNWAYRSKSE EAQSSIGDFA ERYLLRPARM
LALEPILLMM TLYVSVSFGL LYNFFLAYPT SFIQERGWDQ TTASLPLISI LVGAIIAGAL
LSFSTNSRWA PNAKEGRPQE TRLLLMMVGA VSLPAGMFLF AWTSSATMNP WPQILSGIPT
GFGIHLINMQ GMNYIIDSYK IYANSAIAAN TFLRSLFAAG FPILATSMYA AIGVKWGTTI
LALLAVAMIP IPILFYYFGA KIRAKSKWQP PL
