ID   MFM6_PHOSM              Reviewed;         547 AA.
AC   A0A3G1DIJ8;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=MFS-type transporter M6 {ECO:0000303|PubMed:27056201};
DE   AltName: Full=Squalestatin S1 biosynthesis cluster protein M6 {ECO:0000303|PubMed:27056201};
GN   Name=M6 {ECO:0000303|PubMed:27056201};
OS   Phoma sp. (strain ATCC 20986 / MF5453).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Phoma.
OX   NCBI_TaxID=1828523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=27056201; DOI=10.1039/c6cc02130a;
RA   Bonsch B., Belt V., Bartel C., Duensing N., Koziol M., Lazarus C.M.,
RA   Bailey A.M., Simpson T.J., Cox R.J.;
RT   "Identification of genes encoding squalestatin S1 biosynthesis and in vitro
RT   production of new squalestatin analogues.";
RL   Chem. Commun. (Camb.) 52:6777-6780(2016).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid
CC       A), a heavily oxidized fungal polyketide that offers potent cholesterol
CC       lowering activity by targeting squalene synthase (SS).
CC       {ECO:0000305|PubMed:27056201}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC       {ECO:0000305}.
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DR   EMBL; KU946987; AMY15063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G1DIJ8; -.
DR   SMR; A0A3G1DIJ8; -.
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..547
FT                   /note="MFS-type transporter M6"
FT                   /id="PRO_0000447831"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   547 AA;  59863 MW;  F344C16A8AEA6B6D CRC64;
     MHRRRRDNLM TPAEMVASMK PPQSLSTEDD DGSRRDSESS ADVLKSNEEF QARMIPEDDD
     ANSVTAQPTW TVLSDTEIKS VLVVASFAAA ISPFSTSTYY PAVFAISQDL GVSVSKINLT
     MSSYQIFQGV APTITAAFAD TYGRRPMFLV CFAIYFVANV GLALQNNFTT LLVLRCLQST
     GSSGTFALAQ AVTADITTRA ERGRYLIYAT LGSTLGPFLG PVIGGLLVKF LGWRSVFWFL
     LCMGTVFALL IFIFFGETAR PIVGDGSVPP QSWNRSFLQI RSKGITSLKP NLASLERRKS
     RPNPLTSLAL LWDRENFILS VSGGLLYAGY SSVTSVLASQ LQQRYKYDAV QVGLCYLPVG
     FGSLLAYRTT VRLMDWNFER EAKKQGLVIV KNQQTDITRF DLEKARLGFV FPMILVCSVL
     LVAYGWQMHY HAPLAPILVT MFLIAIILTG VMNAIAALLT DVNRENAAAV GAAMNLTRLL
     LGAGAVAVVG PLNKSAGIGW TATVTAGLWV LMMPTLRMVY RDGFVWRAGE NERVHASNVE
     LAALVRS