ID   ECT1_ELSFA              Reviewed;         505 AA.
AC   B1A0U4;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Elsinochrome transporter 1 {ECO:0000303|PubMed:18957608};
DE   AltName: Full=Elsinochromes biosynthesis cluster protein ECT1 {ECO:0000303|PubMed:18957608};
GN   Name=ECT1 {ECO:0000303|PubMed:18957608};
OS   Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND INDUCTION.
RX   PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA   Chung K.R., Liao H.L.;
RT   "Determination of a transcriptional regulator-like gene involved in
RT   biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT   fawcettii.";
RL   Microbiology 154:3556-3566(2008).
RN   [2]
RP   REVIEW.
RX   PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA   Chung K.R.;
RT   "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT   citrus scab.";
RL   Mol. Plant Pathol. 12:123-135(2011).
CC   -!- FUNCTION: Major facilitator-type transporter; part of the gene cluster
CC       that mediates the biosynthesis of elsinochromes, pigments consisting of
CC       at least four interconvertible tautomers (A, B, C and D) that have a
CC       core phenolic quinone to which various side chains are attached and
CC       which play an important role in fungal pathogenesis (PubMed:18957608).
CC       Once elsinochrome is synthesized, it must be exported outside the
CC       fungal cells, which is probably accomplished by the ECT1 transporter,
CC       to avoid toxicity (PubMed:21199563). {ECO:0000269|PubMed:18957608,
CC       ECO:0000303|PubMed:21199563}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is induced by the presence of the cluster-
CC       specific polyketide synthase PKS1 (PubMed:18957608). Expression is up-
CC       regulated in the presence of large amounts of glucose, during nitrogen
CC       starvation or at alkaline pH, conditions highly conducive to
CC       elsinochrome accumulation (PubMed:18957608).
CC       {ECO:0000269|PubMed:18957608}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Nitrate/nitrite porter (TC 2.A.1.8) family. {ECO:0000305}.
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DR   EMBL; EU414198; ABZ82008.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1A0U4; -.
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:0015112; F:nitrate transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR044772; NO3_transporter.
DR   PANTHER; PTHR23515; PTHR23515; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..505
FT                   /note="Elsinochrome transporter 1"
FT                   /id="PRO_0000445821"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   505 AA;  54058 MW;  ABB220F1146D6350 CRC64;
     MALSGLGSGP EGNPNNHQGK AIPTLNPSHG QGPSFLFSWV SFLVPFWSWY PFSPLPLKGI
     PGENSSSPNG LKNFHGIGLN GTERGMGHFH PISGNRLGLR LTLVAGWFLE PFPTFLAVLI
     RTQGDSTPSR SFVAFFVGTL GLGQEGITGS FNRKIAGPAT IDPQDWAMEE GVLTNFLWPP
     FTTFFRTTKG FPVQWHGEGS FVVPGIFSLP QPLPWWLLLP DTPTGAGKPP ESRQHQPSHS
     MNGAIVDIPG GLTQTPSSPD RSSSTNSIAD EEKKLDYKPT SPTSDTEKGE SLPLTASQSE
     IIASPTFSEM IRVIFSGPTL VLGACYFCTF GAELSINSVL GTFYQRQLGL GLQNAGNLAA
     IFGLLNIVMR PLGGMASDLL YRKTGSVWSK KALLHTYCVM TGVFCIAIGL ARSRSQATLV
     GLVSGGLAFF LEGANGLTYS HVHPYANGVV SGFTGACGNL GGIVFAIVFR YNSLDYSKVF
     WIIGAIIIGL QVATCWIKPV PKSVI