DOTC_DOTSN
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 25-MAY-2022, entry version 33.
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; 64363.EME38645; -.
DR EnsemblFungi; EME38645; EME38645; DOTSEDRAFT_75413.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_0_1; -.
DR OMA; IPGWVWR; -.
DR OrthoDB; 653366at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
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:0005774; C:vacuolar 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; 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
