DOTC_DOTSE
ID DOTC_DOTSE Reviewed; 585 AA.
AC Q8TFD3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Efflux pump dotC {ECO:0000305};
DE AltName: Full=Dothistromin biosynthesis protein C {ECO:0000303|PubMed:12039746};
GN Name=dotC {ECO:0000303|PubMed:12039746};
OS Dothistroma septosporum (Red band needle blight fungus) (Mycosphaerella
OS pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=64363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NZE1 / ATCC MYA-605;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NZE7;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NZE1 / ATCC MYA-605;
RA Bradshaw R.E., Monahan B.J., Gillman C.J.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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; AF448056; AAL87047.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8TFD3; -.
DR SMR; Q8TFD3; -.
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; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..585
FT /note="Efflux pump dotC"
FT /id="PRO_0000443454"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..585
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 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 585 AA; 62392 MW; CA55A4BBB7661099 CRC64;
MSEDHTKADN LSEKDPHSPE RSDSSSHEDA HAREEEESSD DDGALDGKPA SLIAIVMIAL
SLIGLQLAVF LSALDTTIVT VALPAISAHF NSTAAYTWVG SAYLLANAAS TPIWGKLADI
FGRKPMLLLA NALFMIGSLV CALSINVGML ITARAIQGAA GGGLLTLVDT IIGDLFSLRT
RGTYLGMIGG VWAIACALGP IVGGAFTSSV TWRWCFYINL PIDGLAFGII FFFLKLKTPK
TPILEGFAAI DWAGSFFIIG GTLMFLFGLQ YGGITFPWDS ATVICLLVFG VVCIVLFGLV
EWKFARFPII PLRLFQYRNN CGALLVAFFH SFVFTSAFYY LPLYFQAVKG ATPILAGVYI
LPAVLSTGVS AAATGAFIGN TGNYLIPMYF GMSMMILGYG LLINFDAGSG WAKLIIYQLI
AGIGNGPNFQ APLVALQTKI KQSDIATGTA TFNFVRNIAT AISVVAGQVL YQNQLKKMTS
TLQQLGPAAS LIAAGDAGAN TQAINALPTP QRDLARSAIA DALSPMWIMY TAFAAAGLFC
ILLVSKTELT TTHEVTEVGL EAQKKAEAER KAERQAKDLE KAQKS
