MPH2_YEAST
ID MPH2_YEAST Reviewed; 609 AA.
AC P0CD99; D6VRB0; P47186; Q07787;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Alpha-glucosides permease MPH2;
DE AltName: Full=Maltose transport protein 2;
GN Name=MPH2; OrderedLocusNames=YDL247W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP FUNCTION.
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 [4]
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).
CC -!- FUNCTION: High-affinity uptake of maltose and maltotriose. Also
CC transports alpha-methylglucoside, glucose and turanose but not
CC melezitose or trehalose. {ECO:0000269|PubMed:10618490,
CC ECO:0000269|PubMed:12210897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC 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; Z74295; CAA98827.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11620.1; -; Genomic_DNA.
DR PIR; S67812; S67812.
DR RefSeq; NP_010034.1; NM_001180307.1.
DR AlphaFoldDB; P0CD99; -.
DR SMR; P0CD99; -.
DR BioGRID; 31865; 3.
DR DIP; DIP-5180N; -.
DR STRING; 4932.YDL247W; -.
DR PaxDb; P0CD99; -.
DR PRIDE; P0CD99; -.
DR EnsemblFungi; YDL247W_mRNA; YDL247W; YDL247W.
DR GeneID; 851350; -.
DR KEGG; sce:YDL247W; -.
DR SGD; S000002406; MPH2.
DR VEuPathDB; FungiDB:YDL247W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176341; -.
DR HOGENOM; CLU_001265_11_5_1; -.
DR InParanoid; P0CD99; -.
DR OMA; ISADWQT; -.
DR BioCyc; YEAST:G3O-29622-MON; -.
DR PRO; PR:P0CD99; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P0CD99; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015151; F:alpha-glucoside transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005363; F:maltose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0000017; P:alpha-glucoside transport; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IDA:SGD.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane 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 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 2: Evidence at transcript level;
KW Cell membrane; Maltose metabolism; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..609
FT /note="Alpha-glucosides permease MPH2"
FT /id="PRO_0000050424"
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..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 609 AA; 68189 MW; FD3A88D5DFB8399C 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 GIAPVVFCLV
SEMPSSRLRT KTIILARNTY NVVSIICSVL ILYQLNSKKW NWGAKSGFFW GVLCFCTLIW
AVVDLPETAG KTFVEINELF KLGVSARKFK STKVDPFVVK TPLKTSLITT PREISKLPLQ
RNSNVSHHL
