ID A0A0C2ZMX5_9AGAM Unreviewed; 538 AA.
AC A0A0C2ZMX5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=SCLCIDRAFT_137709 {ECO:0000313|EMBL:KIM53987.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM53987.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM53987.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM53987.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC Evidence={ECO:0000256|ARBA:ARBA00034449};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992,
CC ECO:0000256|RuleBase:RU003346}.
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DR EMBL; KN822165; KIM53987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2ZMX5; -.
DR STRING; 1036808.A0A0C2ZMX5; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; A0A0C2ZMX5; -.
DR OrthoDB; 2013244at2759; -.
DR Proteomes; UP000053989; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015798; P:myo-inositol transport; IEA:UniProt.
DR GO; GO:0015791; P:polyol transmembrane transport; IEA:UniProt.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48020:SF12; MFS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48020; PROTON MYO-INOSITOL COTRANSPORTER; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053989};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003346}.
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..496
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 538 AA; 58072 MW; C3524E6A5632573E CRC64;
MDQRVEDNEH SPAVKADAYR EVAQCTAAGE ISEFAVIAEG EERTTWFIWL LVCCCTISGL
LFGYDTGVIS GALVTIKGDL GPSQLSNGEK EFITSATTLG ALLGGLAAGV MSDWTGRRPV
LGIADFTFIG GAVGQAVSRT VWSMVGCRFL VGIGVGLASC VAPLYIQELS PTRLRGRMVV
LNVVMITLGQ VIAYGIDAGF TNVSGGWRWM VGLGCVPAAF QLVMLAYLPE SPRVLVRRGN
MEAARKVLSR LYVLASSSQV DLKLKVLHAT VKQSIEIANS TTFWERFISM STNPVNRRAL
VVGCGMQAFQ QLCGFNTLMY YSASLFQEIG FNQPTAVGLI ISGTNFLFTL FALKYIDLVG
RRRIMIFSAP GMVVGLALAS IAFHYMTIHT GGSLVAGAHY SQGWAGVVLL SMIIFVASYA
TGLGNVPWQQ GELFSLEVRG IGTSLSTAIN WAANLLIGST YLSLMSAITP AGAFGFYAGL
CLLGWLFCVF CFPDLSGLSL EEVQNVFKTG YGIKESARLR RVKREIKERE KLICESQP
//
