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Database: UniProt
Entry: M2YI75
LinkDB: M2YI75
Original site: M2YI75 
ID   DOTC_DOTSN              Reviewed;         580 AA.
AC   M2YI75;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Efflux pump dotC {ECO:0000305};
DE   AltName: Full=Dothistromin biosynthesis protein C {ECO:0000303|PubMed:22069539};
GN   Name=dotC {ECO:0000303|PubMed:22069539}; ORFNames=DOTSEDRAFT_75413;
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990;
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=12039746; DOI=10.1128/aem.68.6.2885-2892.2002;
RA   Bradshaw R.E., Bhatnagar D., Ganley R.J., Gillman C.J., Monahan B.J.,
RA   Seconi J.M.;
RT   "Dothistroma pini, a forest pathogen, contains homologs of aflatoxin
RT   biosynthetic pathway genes.";
RL   Appl. Environ. Microbiol. 68:2885-2892(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=17683963; DOI=10.1016/j.fgb.2007.06.005;
RA   Zhang S., Schwelm A., Jin H., Collins L.J., Bradshaw R.E.;
RT   "A fragmented aflatoxin-like gene cluster in the forest pathogen
RT   Dothistroma septosporum.";
RL   Fungal Genet. Biol. 44:1342-1354(2007).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=22069539; DOI=10.3390/toxins1020173;
RA   Bradshaw R.E., Feng Z., Schwelm A., Yang Y., Zhang S.;
RT   "Functional analysis of a putative dothistromin toxin MFS transporter
RT   gene.";
RL   Toxins 1:173-187(2009).
RN   [6]
RP   INDUCTION.
RX   PubMed=23207690; DOI=10.1016/j.fgb.2012.11.006;
RA   Chettri P., Ehrlich K.C., Cary J.W., Collemare J., Cox M.P.,
RA   Griffiths S.A., Olson M.A., de Wit P.J., Bradshaw R.E.;
RT   "Dothistromin genes at multiple separate loci are regulated by AflR.";
RL   Fungal Genet. Biol. 51:12-20(2013).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in
CC       structure to the aflatoxin precursor, versicolorin B (PubMed:12039746,
CC       PubMed:17683963). One function of dotC may be to transport early-stage
CC       dothistromin biosynthetic intermediates from the cytoplasm into
CC       vacuoles, thereby affecting the rate of dothistromin production
CC       (PubMed:22069539). {ECO:0000269|PubMed:22069539,
CC       ECO:0000305|PubMed:12039746, ECO:0000305|PubMed:17683963}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22069539};
CC       Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC       {ECO:0000269|PubMed:22069539}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the dothistromin-
CC       specific transcription factor aflR (PubMed:23207690).
CC       {ECO:0000269|PubMed:23207690}.
CC   -!- DISRUPTION PHENOTYPE: Decreases the expression of ver1, pksA and vbsA,
CC       and subsequent production of dothistromin, but does not affect the
CC       resistance to the toxin (PubMed:22069539).
CC       {ECO:0000269|PubMed:22069539}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; KB446546; EME38645.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2YI75; -.
DR   SMR; M2YI75; -.
DR   STRING; 675120.M2YI75; -.
DR   GlyCosmos; M2YI75; 2 sites, No reported glycans.
DR   EnsemblFungi; EME38645; EME38645; DOTSEDRAFT_75413.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_000960_22_0_1; -.
DR   OMA; WCILAFG; -.
DR   OrthoDB; 1655250at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd17502; MFS_Azr1_MDR_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23501:SF102; DRUG TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G08530)-RELATED; 1.
DR   PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR01036; TCRTETB.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..580
FT                   /note="Efflux pump dotC"
FT                   /id="PRO_0000443453"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   580 AA;  61879 MW;  74F20E3BE1689080 CRC64;
     MSEDHTKADN LSEKDPHSPE RSDSSSHEDA HAREEEESSD DDGALDGKPA SLIAIVMIAL
     SLAVFLSALD TTIVTVALPA ISAHFNSTAA YTWVGSAYLL ANAASTPIWG KLADIFGRKP
     MLLLANALFM IGSLVCALSI NVGMLITARA IQGAAGGGLL TLVDTIIGDL FSLRTRGTYL
     GMIGGVWAIA CALGPIVGGA FTSSVTWRWC FYINLPIDGL AFGIIFFFLK LKTPKTPILE
     GFAAIDWAGS FFIIGGTLMF LFGLQYGGIT FPWDSATVIC LLVFGVVCIV LFGLVEWKFA
     RFPIIPLRLF QYRNNCGALL VAFFHSFVFI SAFYYLPLYF QAVKGATPIL AGVYILPAVL
     STGVSAAATG AFIGNTGNYL IPMYFGMSMM ILGYGLLINF DAGSGWAKLI IYQLIAGIGN
     GPNFQAPLVA LQTKIKQSDI ATGTATFNFV RNIATAISVV AGQVLYQNQL KKMTSTLQQL
     GPAASLIAAG DAGANTQAIN ALPTPQRDLA RSAIADALSP MWIMYTAFAA AGLFCILLVS
     KTELTTTHEV TEVGLEAQKK AEAERKAERQ AKDLEKAQKS
//
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