DEP3_FUSLA
ID DEP3_FUSLA Reviewed; 550 AA.
AC A0A0M9EQT6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Efflux pump DEP3 {ECO:0000303|PubMed:19737099};
DE AltName: Full=Depudecin biosynthesis cluster protein 3 {ECO:0000303|PubMed:19737099};
GN Name=DEP3 {ECO:0000303|PubMed:19737099}; ORFNames=FLAG1_09234;
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059;
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=19737099; DOI=10.1094/mpmi-22-10-1258;
RA Wight W.D., Kim K.-H., Lawrence C.B., Walton J.D.;
RT "Biosynthesis and role in virulence of the histone deacetylase inhibitor
RT depudecin from Alternaria brassicicola.";
RL Mol. Plant Microbe Interact. 22:1258-1267(2009).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=28460114; DOI=10.1093/molbev/msx145;
RA Reynolds H., Slot J.C., Divon H.H., Lysoee E., Proctor R.H., Brown D.W.;
RT "Differential retention of gene functions in a secondary metabolite
RT cluster.";
RL Mol. Biol. Evol. 34:2002-2015(2017).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of depudecin, a highly oxidized eleven-carbon linear
CC polyketide that acts as a histone deacetylase (HDAC) inhibitor and
CC makes a small contribution to pathogenesis (PubMed:19737099,
CC PubMed:28460114). Is presumed either to be responsible for exporting
CC depudecin, to provide self-protection, or both (PubMed:19737099).
CC {ECO:0000269|PubMed:19737099, ECO:0000269|PubMed:28460114}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression correlates with the production of depudecin with
CC high levels on oat grain medium, and minimal levels on oat flower
CC medium and complete medium (PubMed:28460114).
CC {ECO:0000269|PubMed:28460114}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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; JXCE01000338; KPA37943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9EQT6; -.
DR SMR; A0A0M9EQT6; -.
DR EnsemblFungi; KPA37943; KPA37943; FLAG1_09234.
DR OrthoDB; 503593at2759; -.
DR Proteomes; UP000037904; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
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; 2.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..550
FT /note="Efflux pump DEP3"
FT /id="PRO_0000441940"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 550 AA; 58918 MW; 26E05815594AB658 CRC64;
MSEQSTLAGP YTEKPGVESQ NPTGDGKASF DETSPRDIHG WRWAIAYAAM LSTTFLFALD
NTIVANIQPS IINDFGHLEL ISWIGTGFAL GTMFILLWGK IYGVFNIKWV YIFNILLFEV
GSAVCGAAPN IQALIIGRVI AGIGGSGMYS GTLTYVSVLS NQKEKPAYLA GSTVVWGVGS
VVGPVVGGAF AASSATWRWG FYINLPIGAV FAPAYMILFP NWDPNPTLTL AEKFRLVDWI
NAVIFLAGSA CLTVALTFGG VVYSFNSGTI IALWTVTGVL LVAFIVLLKL HPLVSKENRL
YPLHFFKQMT LINMQLQVFL ASGIILAMTY YVPLYFQFIK GDGALQAGVR LLPLIMFMVA
FSMVNGFLMP KYGLIPIWYI VGSALTLIGS ALMYTIDENT SNGNVYGYNI LVGAGAGCYI
VAGFAIVQSL VPTHEIANAV GAMTISQDLG MVLFLAICGS LFHNVAVDKV GKALPSASET
EIGNLIAGTS SSAFQALSEA DKDLVIPEIA SAMKSIWAFF MAAAALSFVC SWPLFKTKLG
GKKVEASVVV
