MFS1B_MAGO7
ID MFS1B_MAGO7 Reviewed; 577 AA.
AC G4MWA9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=MFS-type efflux transporter MFS1 {ECO:0000303|PubMed:18433432};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein MFS1 {ECO:0000303|PubMed:18433432};
GN Name=MFS1 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08384;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=18433432; DOI=10.1111/j.1469-8137.2008.02459.x;
RA Collemare J., Pianfetti M., Houlle A.E., Morin D., Camborde L., Gagey M.J.,
RA Barbisan C., Fudal I., Lebrun M.H., Boehnert H.U.;
RT "Magnaporthe grisea avirulence gene ACE1 belongs to an infection-specific
RT gene cluster involved in secondary metabolism.";
RL New Phytol. 179:196-208(2008).
CC -!- FUNCTION: MFS-type efflux transporter; part of the gene cluster that
CC mediates the biosynthesis of a tyrosine-derived cytochalasan acting as
CC a fungal signal recognized by resistant rice plants and leads to
CC avirulence in Pi33 resistant rice cultivars (PubMed:18433432). MFS1
CC might be involved in the excretion of the signaling tyrosine-derived
CC cytochalasan (Probable). {ECO:0000269|PubMed:18433432,
CC ECO:0000305|PubMed:18433432}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed exclusively during fungal penetration of host
CC leaves, the time point at which plant defense reactions are triggered.
CC {ECO:0000269|PubMed:18433432}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CM001232; EHA55869.1; -; Genomic_DNA.
DR RefSeq; XP_003715676.1; XM_003715628.1.
DR AlphaFoldDB; G4MWA9; -.
DR SMR; G4MWA9; -.
DR EnsemblFungi; MGG_08384T0; MGG_08384T0; MGG_08384.
DR GeneID; 2678484; -.
DR KEGG; mgr:MGG_08384; -.
DR VEuPathDB; FungiDB:MGG_08384; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_0_1; -.
DR InParanoid; G4MWA9; -.
DR OMA; IWVPNAY; -.
DR OrthoDB; 672661at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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; -; 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 Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..577
FT /note="MFS-type efflux transporter MFS1"
FT /id="PRO_0000449446"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 577 AA; 61724 MW; EB459EFCE16B6EE3 CRC64;
MSNEGTNTVL KNPGSNQEEA DPDSPSSLGD KSKLDELADS TSDGSQANSG RGIAFWAIFI
SLSVTGFLSS MEGGIMSTAL PAVSRAVNAE SDYVWIINVY FLTSAAFQPL YGQLADIWGR
RWPMLSAVTI FAAGSAICGA ANNSGTLIGG RAIQGLGAAG INTLVELILC DLLPLRERGQ
FMGLLFLFIV VGSVLGPMLG GIIVDKTSWR WIFFINLPIC ALCFGLLFFA LNLKHRRDDN
STSLQKLKKI DFVGVLILCV AVTLLIYALT YGGGAKYAWS HPVIITTLVL GIFGHGLFIA
FEASPWCSNP TTPLTLFQNR TSVAAYTLEA VQILVSWGAL YFLPLYFQSV LALTPSRSGV
LILAFSISYC LSAAIGGGLV TKLGKYRLVH IISFAIMTIM MGVFTILNRN SSLAVNVILG
LIAGVGVGLP NASILTAVQA SLPDSLNAAS TALFAFIRSL ATVFAVTIPA AIFNSRFDDL
LSTSALDNDV KNSLDLGKAY QQASPDFLHS FPAPVQDQIV GLYELSLKLV WQVLIGIAAV
GVIASLLEKD LECRTEQTTE EFGLKDRDEK APKKSEV
