ID   MFM2_PHOSM              Reviewed;         563 AA.
AC   A0A3G1DJG1;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=MFS-type transporter M2 {ECO:0000303|PubMed:27056201};
DE   AltName: Full=Squalestatin S1 biosynthesis cluster protein M2 {ECO:0000303|PubMed:27056201};
GN   Name=M2 {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], FUNCTION, AND INDUCTION.
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   -!- INDUCTION: Expression is induced on squalestatin S1-producing YMG
CC       medium. {ECO:0000269|PubMed:27056201}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; KU946987; AMY15059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G1DJG1; -.
DR   SMR; A0A3G1DJG1; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..563
FT                   /note="MFS-type transporter M2"
FT                   /id="PRO_0000447830"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          504..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   563 AA;  60408 MW;  A5DCCFE746FD2036 CRC64;
     MAHTNTSTAL HEQENFLPKN RLLLVILTLG TVLFVINIDH NGLSTLLPTI AEDLGAQKSI
     TWAGSSQLIA TTVFSVLYGR LSDIFGRKAL FVSALGVFSI AELGCGFANS PRMLYAMRAL
     TGASGGGIGN LSIIIATDVV SLRHRGQYMA VVAPFMVLGN VCGPLVAAGV AKSSLTWRGL
     FWLISPLGGL SAILAGYILP STAPTDTFKQ NLAKVDWLGS LTSTVAIVGF MVAVSGTGTY
     HPGYSPLAIS LLSVSGAAFL AFLFIEWKFA TLPIIPLTIF AIPDVSALLM QTFTLGWVNQ
     ANVYFIPIYA QNLRQWSPVI SGVLLFPIIA VQVIVSMIAG RWMSKSGQYG TTIRLGVAFL
     LIGSLLETQF GRSTHPAYVV IVLLVIGIGV GAANQPMVIA MQAHTKKSER AVVTSSRNFF
     RFLGSACGVA MSAAILQSTL RASLPVAYKH LAESPYALAG LSPQERDVIA PSYERAIRHV
     FIASAGASVL CSLGLFVWKD DGYESRPNED NDNDQHASTR ETDEEDEQST LIDNREPSAV
     SYGTVEAGER DRYKAPDRLR RGL