ID   LUC4_FUSSX              Reviewed;         564 AA.
AC   A0A6J4B6H5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=MFS-type efflux pump LUC4 {ECO:0000303|PubMed:32043422};
DE   AltName: Full=Lucilactaene biosynthesis cluster protein 4 {ECO:0000303|PubMed:32043422};
GN   Name=LUC4 {ECO:0000303|PubMed:32043422};
OS   Fusarium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=29916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=RK97-94;
RX   PubMed=32043422; DOI=10.1080/09168451.2020.1725419;
RA   Kato S., Motoyama T., Futamura Y., Uramoto M., Nogawa T., Hayashi T.,
RA   Hirota H., Tanaka A., Takahashi-Ando N., Kamakura T., Osada H.;
RT   "Biosynthetic gene cluster identification and biological activity of
RT   lucilactaene from Fusarium sp. RK97-94.";
RL   Biosci. Biotechnol. Biochem. 84:1303-1307(2020).
CC   -!- FUNCTION: MFS-type efflux pump; part of the gene cluster that mediates
CC       the biosynthesis of the mycotoxin lucilactaene and the lucilactaene-
CC       related compound NG-391 that act as cell cycle inhibitors with potent
CC       growth inhibitory activity against malarial parasites, moderate growth
CC       inhibitory activity against cancer cells, and no activity against
CC       bacteria and fungi. {ECO:0000269|PubMed:32043422}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; LC515193; BBQ09589.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..564
FT                   /note="MFS-type efflux pump LUC4"
FT                   /id="PRO_0000454636"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        436..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        512..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   564 AA;  60644 MW;  35D7FC4C923578E3 CRC64;
     MGQSQDNTQL TTASPQAEKD LSSNDNPPES EPAAPKKGAR FWLVFIAIAL TTFLAALDTS
     IISTALPTIT SDLGSNSLYV WIVDSYLLAS TATIPIFAQA ANIYGRRSLT LIAVCLFTLG
     SGLCGGAHNT AMMIGGRSVQ GVGGGGILTM SEIVVCDMVS VRERGMYAGI IGGVWAIASV
     IAPIMGGAFA QNVSWRWIFY INLPIAGVVL VALIVFLKLA RPPTGTFKEQ MSRIDWGGSV
     LLIASVTAVV LALSWGGSEH PWSSWRTLVP LILGLVGQLA FFAYQGAPWL KEPTMPLRLF
     GNRTSSTLFV ISFVHSMLLF WVCYFLPVYF QAVKEASPAR SAVMLFPIAT TSAPGGVIAG
     IFITKTGKYR VWHFVGFALM SISCGLFTLL DDKSSIGRWV GFQLLFGFGT GFVFTSCLPP
     ILASLPDSDV ATATGAWTFL RNFGSIWGIA IPAAAFNTRV NSSLDKVSSG TVRDMLVNGG
     AYEHATKTFI QAFNNTPRLK AEIVQVYMDG LKLVWQVSIA FSVLGFVLAF LVKSLTLRDE
     LNTEYGLEEK DTSKEKSSEE GNAS