MFL2_PHOSM
ID MFL2_PHOSM Reviewed; 598 AA.
AC A0A3G1DJE2;
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 transporter L2 {ECO:0000303|PubMed:27056201};
DE AltName: Full=Squalestatin S1 biosynthesis cluster protein L2 {ECO:0000303|PubMed:27056201};
GN Name=L2 {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 transporter; part of the gene cluster that mediates the
CC biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A),
CC a lead compound for the treatment of hyper-cholesterolemia by targeting
CC squalene synthase (SS). {ECO:0000269|PubMed:27056201}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; KU946987; AMY15055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G1DJE2; -.
DR SMR; A0A3G1DJE2; -.
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..598
FT /note="MFS transporter L2"
FT /id="PRO_0000447828"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 598 AA; 64911 MW; 5DD366CE6126841B CRC64;
MEHNTDISTT QYNSHTVSTT TLSSFLVNVV TSSKRGNKMT TITAQPPRDE VEPAVPAPQL
LSSDSASELS PKAEKFQPGW RFIAAFLSLC IIVLMAALDA TSISVALPSM ARALGGSAIE
AFWAGTSFLL TSTIFQPVLG SFSHIFGRKS LIYISLVFFL AGSIIPAVAN NFTTILVGRS
IQGVGGGGII ALTEMVVVDT VPLRERGKWF SFFGMMWSFG TVAGPLIGGA FAQKVSWRWV
FWINLPFLGI GTVLITVFLK LNQRHGEFLA RLREVDWIGM VLFLGSTTGF LIPITWGGVQ
YPWDSWRTLV PLIVSAAGIV AFIVHQEKFA PHPLIRTSVF KNKSAALLYL TTVIHGIILW
AILYFMPLYF EAVKGMGPIM AGVALFPWTF TVAPGAVATG IAIAVTGKYR WANWAGWFLA
TLGSGLLILL KPDTSTPAWI FLNLVGGIGT GILFPAMALA VQASASVKDQ AYAANMFSFF
RAFGQTLGVA IGGVVFQNQM KAKLLTYPLL ADMADTYSKD AAGLVEIIKG MPAGLMKDQL
KESYTDALKY IWIVATVLAG VSLVATLFID EFDMDIEMDT ERGFKEKSKV KDAEKETH