MAL31_YEAST
ID MAL31_YEAST Reviewed; 614 AA.
AC P38156; D6VQU3; Q3SCJ3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Maltose permease MAL31;
DE AltName: Full=Maltose transport protein MAL31;
GN Name=MAL31; Synonyms=MAL3T; OrderedLocusNames=YBR298C; ORFNames=YBR2116;
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].
RC STRAIN=CEN.PK 113-7D;
RX PubMed=16088872; DOI=10.1002/yea.1279;
RA Dietvorst J., Londesborough J., Steensma H.Y.;
RT "Maltotriose utilization in lager yeast strains: MTT1 encodes a maltotriose
RT transporter.";
RL Yeast 22:775-788(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483839; DOI=10.1002/yea.320110707;
RA Feuermann M., Charbonnel L., De Montigny J., Bloch J.C., Potier S.,
RA Souciet J.-L.;
RT "Sequence of a 9.8 kb segment of yeast chromosome II including the three
RT genes of the MAL3 locus and three unidentified open reading frames.";
RL Yeast 11:667-672(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 maltose and maltotriose. Also
CC transports turanose but not alpha-methylglucoside, melezitose or
CC trehalose. {ECO:0000269|PubMed:12210897}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By maltose and maltotriose. Repressed by glucose.
CC {ECO:0000269|PubMed:12210897}.
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; DQ010169; AAY67702.1; -; Genomic_DNA.
DR EMBL; Z36167; CAA85263.1; -; Genomic_DNA.
DR EMBL; AY692794; AAT92813.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07413.1; -; Genomic_DNA.
DR PIR; S46182; S46182.
DR RefSeq; NP_009857.1; NM_001178646.1.
DR AlphaFoldDB; P38156; -.
DR SMR; P38156; -.
DR BioGRID; 32991; 84.
DR DIP; DIP-7544N; -.
DR IntAct; P38156; 16.
DR MINT; P38156; -.
DR STRING; 4932.YBR298C; -.
DR PaxDb; P38156; -.
DR PRIDE; P38156; -.
DR EnsemblFungi; YBR298C_mRNA; YBR298C; YBR298C.
DR GeneID; 852601; -.
DR KEGG; sce:YBR298C; -.
DR SGD; S000000502; MAL31.
DR VEuPathDB; FungiDB:YBR298C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176341; -.
DR HOGENOM; CLU_001265_11_5_1; -.
DR InParanoid; P38156; -.
DR OMA; FMTYFGR; -.
DR BioCyc; YEAST:G3O-29216-MON; -.
DR PRO; PR:P38156; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38156; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005352; F:alpha-glucoside:proton symporter activity; ISS:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0000017; P:alpha-glucoside transport; ISS:SGD.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Maltose metabolism; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..614
FT /note="Maltose permease MAL31"
FT /id="PRO_0000050422"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 68263 MW; 897FD1DE9AC995CE CRC64;
MKGLSSLINR KKDRNDSHLD EIENGVNATE FNSIEMEEQG KKSDFDLSHL EYGPGSLIPN
DNNEEVPDLL DEAMQDAKEA DESERGMPLM TALKTYPKAA AWSLLVSTTL IQEGYDTAIL
GAFYALPVFQ KKYGSLNSNT GDYEISVSWQ IGLCLCYMAG EIVGLQMTGP SVDYMGNRYT
LIMALFFLAA FIFILYFCKS LGMIAVGQAL CGMPWGCFQC LTVSYASEIC PLALRYYLTT
YSNLCWAFGQ LFAAGIMKNS QNKYANSELG YKLPFALQWI WPLPLAVGIF FAPESPWWLV
KKGRIDQARR SLERTLSGKG PEKELLVSME LDKIKTTIEK EQKMSDEGTY WDCVKDGINR
RRTRIACLCW IGQCSCGASL IGYSTYFYEK AGVSTDTAFT FSIIQYCLGI AATFISWWAS
KYCGRFDLYA FGLAFQAIMF FIIGGLGCSD THGAKMGSGA LLMVVAFFYN LGIAPVVFCL
VSEIPSSRLR TKTIILARNA YNVIQVVVTV LIMYQLNSEK WNWGAKSGFF WGGFCLATLA
WAVVDLPETA GRTFIEINEL FRLGVPARKF KSTKVDPFAA AKAAAAEINV KDPKEDLETS
VVDEGRNTSS VVNK
