MAL11_YEAST
ID MAL11_YEAST Reviewed; 616 AA.
AC P53048; D6VV66;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=General alpha-glucoside permease;
DE AltName: Full=Maltose permease MAL11;
DE AltName: Full=Maltose transport protein MAL11;
GN Name=MAL11; Synonyms=AGT1, MAL1T, MTP1; OrderedLocusNames=YGR289C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=8594329; DOI=10.1111/j.1365-2958.1995.mmi_17061093.x;
RA Han E.-K., Cotty F., Sottas C., Jiang H., Michels C.A.;
RT "Characterization of AGT1 encoding a general alpha-glucoside transporter
RT from Saccharomyces.";
RL Mol. Microbiol. 17:1093-1107(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=10618490; DOI=10.1016/s0014-5793(99)01698-1;
RA Wieczorke R., Krampe S., Weierstall T., Freidel K., Hollenberg C.P.,
RA Boles E.;
RT "Concurrent knock-out of at least 20 transporter genes is required to block
RT uptake of hexoses in Saccharomyces cerevisiae.";
RL FEBS Lett. 464:123-128(1999).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=12210897; DOI=10.1002/yea.894;
RA Day R.E., Higgins V.J., Rogers P.J., Dawes I.W.;
RT "Characterization of the putative maltose transporters encoded by YDL247w
RT and YJR160c.";
RL Yeast 19:1015-1027(2002).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: High-affinity uptake of alpha-glucosides such as maltose,
CC turanose, isomaltose, alpha-methylglucoside, maltotriose, palatinose,
CC trehalose, melezitose and glucose. Acts with the concomitant transport
CC of protons into the cell (symport system).
CC {ECO:0000269|PubMed:10618490, ECO:0000269|PubMed:12210897,
CC ECO:0000269|PubMed:8594329}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8594329};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: By maltose and maltotriose (PubMed:10618490,
CC PubMed:12210897, PubMed:8594329). Repressed by glucose
CC (PubMed:10618490, PubMed:12210897, PubMed:8594329).
CC {ECO:0000269|PubMed:10618490, ECO:0000269|PubMed:12210897,
CC ECO:0000269|PubMed:8594329}.
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; L47346; AAB07600.1; -; Genomic_DNA.
DR EMBL; Z73074; CAA97322.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08377.1; -; Genomic_DNA.
DR PIR; S64624; S64624.
DR RefSeq; NP_011805.3; NM_001181418.3.
DR AlphaFoldDB; P53048; -.
DR SMR; P53048; -.
DR BioGRID; 33539; 113.
DR DIP; DIP-5567N; -.
DR IntAct; P53048; 2.
DR MINT; P53048; -.
DR STRING; 4932.YGR289C; -.
DR TCDB; 2.A.1.1.11; the major facilitator superfamily (mfs).
DR PaxDb; P53048; -.
DR PRIDE; P53048; -.
DR EnsemblFungi; YGR289C_mRNA; YGR289C; YGR289C.
DR GeneID; 853207; -.
DR KEGG; sce:YGR289C; -.
DR SGD; S000003521; MAL11.
DR VEuPathDB; FungiDB:YGR289C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176341; -.
DR HOGENOM; CLU_001265_11_5_1; -.
DR InParanoid; P53048; -.
DR OMA; YELTAAW; -.
DR BioCyc; YEAST:G3O-30949-MON; -.
DR PRO; PR:P53048; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53048; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005352; F:alpha-glucoside:proton symporter activity; IDA:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005364; F:maltose:proton symporter activity; IMP:SGD.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0000017; P:alpha-glucoside transport; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0046352; P:disaccharide catabolic process; IMP:SGD.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015768; P:maltose transport; IMP:SGD.
DR GO; GO:0015771; P:trehalose transport; IDA:SGD.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Maltose metabolism; Membrane;
KW Reference proteome; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..616
FT /note="General alpha-glucoside permease"
FT /id="PRO_0000050425"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 396..398
FT /note="RAG -> KKQV (in Ref. 1; AAB07600)"
FT /evidence="ECO:0000305"
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
