MPH3_YEAS8
ID MPH3_YEAS8 Reviewed; 602 AA.
AC C8Z6M6;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Alpha-glucosides permease MPH3;
DE AltName: Full=Maltose transport protein 3;
GN Name=MPH3; ORFNames=EC1118_1D22_0023g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- FUNCTION: High-affinity uptake of maltose and maltotriose. Also
CC transports alpha-methylglucoside, glucose and turanose but not
CC melezitose or trehalose (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By maltose and maltotriose. Repressed by glucose (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; FN393064; CAY79042.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z6M6; -.
DR SMR; C8Z6M6; -.
DR EnsemblFungi; CAY79042; CAY79042; EC1118_1D22_0023g.
DR HOGENOM; CLU_001265_11_5_1; -.
DR Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D22.
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 GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 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 Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Maltose metabolism; Membrane; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="Alpha-glucosides permease MPH3"
FT /id="PRO_0000391713"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 107..127
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..163
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..199
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..221
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 235..255
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..270
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 271..291
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 364..384
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..397
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 398..418
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 427..447
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..459
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 460..480
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 493..513
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..525
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 526..546
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 580..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 67323 MW; 75BDDAFC1DEC3693 CRC64;
MKNLSFLINR RKENTSDSNV YPGKAKSHEP SWIEMDDQTK KDGLDIVHVE FSPDTRAPSD
SNKVITEIFD ATEDAKEADE SERGMPLATA LNTYPKAAAW SLLVSTTLIM EGYDTAILGA
FYALPIFQRK FGSQNDKTGE WEISASWQIG LTLCYMAGEI VGLQLTGPSV DLVGNRYTLI
IALFFLAAFT FILYFCNSLG MIAVGQALCG MPWGCFQCLT VSYASEICPL ALRYYLTTYS
NLCWLFGQLF AAGIMKNSQK KYADSELGYK LPFALQWILP VPLALGIFFA PESPWWLVKK
GRFDEARRSL RRTLSGKGPE KEILVTLEVD KIKVTIDKEK RLTSKEGSYS DCFEDKINRR
RTRITCLCWA GQATCGSILI GYSTYFYEKA GVSTEMSFTF SIIQYCLGIC ATFLSWWASK
YFGRYDLYAF GLAFQTIVFF IIGGLGCSST HGSKMGSGSL LMAVAFFYNL GIAPVVFRLV
SEMPSSRLRT KTIILARNTY NVVSIICSVL ILYQLNSKKW NWGAKSGFFW GVLCFCTLIW
AVVDLPETAG KTFVEINELF KLGVSARKFK STKVDPFVVK NPPKDVSHND PKGDIEASIA
EE
