MAL11_YEASC
ID MAL11_YEASC Reviewed; 616 AA.
AC N1PA11;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=General alpha-glucoside permease {ECO:0000305};
DE AltName: Full=Maltose permease MAL11 {ECO:0000305};
DE AltName: Full=Maltose transport protein MAL11 {ECO:0000305};
GN Name=MAL11 {ECO:0000250|UniProtKB:P53048};
GN Synonyms=AGT1 {ECO:0000303|PubMed:10368160};
GN ORFNames=CENPK1137D_3313 {ECO:0000312|EMBL:EIW10695.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000312|Proteomes:UP000013192};
RN [1] {ECO:0000312|Proteomes:UP000013192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEN.PK113-7D {ECO:0000312|Proteomes:UP000013192};
RX PubMed=22448915; DOI=10.1186/1475-2859-11-36;
RA Nijkamp J.F., van den Broek M., Datema E., de Kok S., Bosman L.,
RA Luttik M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Paddon C.J., Platt D., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Microb. Cell Fact. 11:36-36(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10368160; DOI=10.1128/jb.181.12.3830-3832.1999;
RA Plourde-Owobi L., Durner S., Parrou J.L., Wieczorke R., Goma G.,
RA Francois J.;
RT "AGT1, encoding an alpha-glucoside transporter involved in uptake and
RT intracellular accumulation of trehalose in Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:3830-3832(1999).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15128531; DOI=10.1128/aem.70.5.2771-2778.2004;
RA Jules M., Guillou V., Francois J., Parrou J.L.;
RT "Two distinct pathways for trehalose assimilation in the yeast
RT Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 70:2771-2778(2004).
CC -!- FUNCTION: High-affinity uptake of alpha-glucosides such as maltose,
CC turanose, isomaltose, alpha-methylglucoside, maltotriose, palatinose,
CC trehalose, melezitose and glucose (PubMed:15128531, PubMed:10368160).
CC Acts with the concomitant transport of protons into the cell (symport
CC system) (By similarity). Provides an alternative and minor mechanism
CC for growth on trehalose carbon source by transporting trehalose into
CC the cytoplasm for conversion to glucose by neutral trehalase NTH1
CC (PubMed:15128531, PubMed:10368160). {ECO:0000250|UniProtKB:P53048,
CC ECO:0000269|PubMed:10368160, ECO:0000269|PubMed:15128531}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10368160,
CC ECO:0000305|PubMed:15128531}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Severely decreases intracellular trehalose during
CC growth on trehalose carbon source (PubMed:10368160). Decreases growth
CC on trehalose carbon source, simultaneous disruption of ATH1 abolishes
CC growth on trehalose carbon source (PubMed:15128531).
CC {ECO:0000269|PubMed:10368160, ECO:0000269|PubMed:15128531}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- CAUTION: The alternative and minor mechanism for utilizing trehalose as
CC a carbon source provided by the MAL11/AGT1 and NTH1 system is specific
CC to S.cerevisiae strains with constitutive and non-glucose-repressible
CC expression of the MAL genes. {ECO:0000305|PubMed:15128531}.
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DR EMBL; CM001528; EIW10695.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PA11; -.
DR SMR; N1PA11; -.
DR EnsemblFungi; EIW10695; EIW10695; CENPK1137D_3313.
DR HOGENOM; CLU_001265_11_5_1; -.
DR Proteomes; UP000013192; Chromosome VII.
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:0005352; F:alpha-glucoside:proton symporter activity; IMP:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015976; P:carbon utilization; IGI:UniProtKB.
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 Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..616
FT /note="General alpha-glucoside permease"
FT /id="PRO_0000452331"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..278
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..404
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..466
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..532
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 67980 MW; EE84AD9E15F7926D CRC64;
MKNIISLVSK KKAASKNEDK NISESSRDIV NQQEVFNTED FEEGKKDSAF ELDHLEFTTN
SAQLGDSDED NENVINEMNA TDDANEANSE EKSMTLKQAL LKYPKAALWS ILVSTTLVME
GYDTALLSAL YALPVFQRKF GTLNGEGSYE ITSQWQIGLN MCVLCGEMIG LQITTYMVEF
MGNRYTMITA LGLLTAYIFI LYYCKSLAMI AVGQILSAIP WGCFQSLAVT YASEVCPLAL
RYYMTSYSNI CWLFGQIFAS GIMKNSQENL GNSDLGYKLP FALQWIWPAP LMIGIFFAPE
SPWWLVRKDR VAEARKSLSR ILSGKGAEKD IQVDLTLKQI ELTIEKERLL ASKSGSFFNC
FKGVNGRRTR LACLTWVAQN SSGAVLLGYS TYFFERAGMA TDKAFTFSLI QYCLGLAGTL
CSWVISGRVG RWTILTYGLA FQMVCLFIIG GMGFGSGSSA SNGAGGLLLA LSFFYNAGIG
AVVYCIVAEI PSAELRTKTI VLARICYNLM AVINAILTPY MLNVSDWNWG AKTGLYWGGF
TAVTLAWVII DLPETTGRTF SEINELFNQG VPARKFASTV VDPFGKGKTQ HDSLADESIS
QSSSIKQREL NAADKC
