MMF1_USTMA
ID MMF1_USTMA Reviewed; 619 AA.
AC A0A0D1DYJ6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=MFS-type efflux pump MMF1 {ECO:0000303|PubMed:16885300};
DE AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MMF1 {ECO:0000303|PubMed:16885300};
GN Name=MMF1 {ECO:0000303|PubMed:16885300}; ORFNames=UMAG_03115;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=16233292; DOI=10.1263/jbb.94.187;
RA Kitamoto D., Isoda H., Nakahara T.;
RT "Functions and potential applications of glycolipid biosurfactants--from
RT energy-saving materials to gene delivery carriers.";
RL J. Biosci. Bioeng. 94:187-201(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16885300; DOI=10.1128/aem.00506-06;
RA Hewald S., Linne U., Scherer M., Marahiel M.A., Kaemper J., Boelker M.;
RT "Identification of a gene cluster for biosynthesis of mannosylerythritol
RT lipids in the basidiomycetous fungus Ustilago maydis.";
RL Appl. Environ. Microbiol. 72:5469-5477(2006).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=17428643; DOI=10.1016/j.colsurfb.2007.03.003;
RA Ito S., Imura T., Fukuoka T., Morita T., Sakai H., Abe M., Kitamoto D.;
RT "Kinetic studies on the interactions between glycolipid biosurfactant
RT assembled monolayers and various classes of immunoglobulins using surface
RT plasmon resonance.";
RL Colloids Surf. B Biointerfaces 58:165-171(2007).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=17279642; DOI=10.1021/la0620814;
RA Imura T., Hikosaka Y., Worakitkanchanakul W., Sakai H., Abe M., Konishi M.,
RA Minamikawa H., Kitamoto D.;
RT "Aqueous-phase behavior of natural glycolipid biosurfactant
RT mannosylerythritol lipid A: sponge, cubic, and lamellar phases.";
RL Langmuir 23:1659-1663(2007).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=19341364; DOI=10.1042/ba20090033;
RA Morita T., Fukuoka T., Imura T., Kitamoto D.;
RT "Production of glycolipid biosurfactants by basidiomycetous yeasts.";
RL Biotechnol. Appl. Biochem. 53:39-49(2009).
RN [8]
RP BIOTECHNOLOGY.
RX DOI=10.1016/j.cocis.2009.05.009;
RA Kitamoto D., Morita T., Fukuoka T., Konishi M., Imura T.;
RT "Self-assembling properties of glycolipid biosurfactants and their
RT potential applications.";
RL Curr. Opin. Colloid Interface Sci. 14:315-328(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24835306; DOI=10.1111/mmi.12642;
RA Freitag J., Ast J., Linne U., Stehlik T., Martorana D., Boelker M.,
RA Sandrock B.;
RT "Peroxisomes contribute to biosynthesis of extracellular glycolipids in
RT fungi.";
RL Mol. Microbiol. 93:24-36(2014).
CC -!- FUNCTION: MFS-type efflux pump; part of the gene cluster that mediates
CC the biosynthesis of mannosylerythritol lipids (MELs), surface-active
CC substances that enhance the availability of water-insoluble substrates
CC (PubMed:16885300, PubMed:24835306). Mannosylerythritol lipid production
CC is responsible for hemolytic activity of Ustilago maydis
CC (PubMed:16885300). MMF1 is directly involved in the secretion of MELs
CC (PubMed:16885300, PubMed:24835306). {ECO:0000269|PubMed:16885300,
CC ECO:0000269|PubMed:24835306}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24835306};
CC Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:24835306}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the secretion of mannosylerythritol
CC lipids (MELs). {ECO:0000269|PubMed:16885300}.
CC -!- BIOTECHNOLOGY: MELs not only have high potential as eco-friendly
CC biosurfactants due to their excellent surface activity, but also have
CC attracted considerable recent interest because of thei runique
CC properties, including self-assembly, anti-tumor and cell
CC differentiation induction activities, and moisturizing and hair-
CC repairing properties. {ECO:0000269|PubMed:16233292,
CC ECO:0000269|PubMed:17279642, ECO:0000269|PubMed:17428643,
CC ECO:0000269|PubMed:19341364, ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003146; KIS69144.1; -; Genomic_DNA.
DR RefSeq; XP_011389466.1; XM_011391164.1.
DR AlphaFoldDB; A0A0D1DYJ6; -.
DR SMR; A0A0D1DYJ6; -.
DR EnsemblFungi; KIS69144; KIS69144; UMAG_03115.
DR GeneID; 23563676; -.
DR KEGG; uma:UMAG_03115; -.
DR VEuPathDB; FungiDB:UMAG_03115; -.
DR eggNOG; KOG0254; Eukaryota.
DR OMA; NWITSAF; -.
DR OrthoDB; 672661at2759; -.
DR Proteomes; UP000000561; Chromosome 7.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..619
FT /note="MFS-type efflux pump MMF1"
FT /id="PRO_0000449541"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
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 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 619 AA; 67091 MW; F44A67842372C63C CRC64;
MADEKRTSIE EPGTPMSYST AASPELLSSS NNASALPAYP SSQTKQDKES LSHDQAVRVE
PESSTPLTDS VEDNESGAKV KKDLHFWIIF SALMLIAFVA ALDMTMISTA LPAITANLPP
STIAANWITS AFLLPMVASQ PIFGGLSCSI GRKWSINSAL VIFLVGSVVC ATAKTFLVLV
IGRGIQGLGG GGIHSMCEII MSDLTTLRER GLFFGVIALV FAVAGFAAPV LGGVFSEHSW
PWIFWINLPI GAISLVLLII FLNIRVPLLT GKEKWQKLDL VGNAVLFGSV TAILIAVTEG
GIKYRWSAWQ IWVPLVVGLL GIMLFLVIEW VPNRIAPKPV FPLDLFRNRT ASVAYVQTFV
HGVIFYGVIY MVPIYFQAIK DRTPLQSAIW SFPLSAPSFP FAMGAGVLIS ITGKYKLLIF
CGWMLMAAGI GWMTHWHVGT SKFEWAFSQV ILGAGLGIMF PITLPPIQAA LPASRLESAT
AAYAFTRTFG AVWGITAATT IFSTQAAKNL RPYYDQLNPL GLSDFTVVAF SEQLRNLPQP
IQGVVKGVYA DAISDSYWLF VPLAIIGFFT TFGMKELPLP DFIKSEAKLE QKQDVTPALK
SSAAHAVVNV KTEVPSTLP
