GAL2_YEAST
ID GAL2_YEAST Reviewed; 574 AA.
AC P13181; D6VY81; Q12521;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Galactose transporter;
DE AltName: Full=Galactose permease;
GN Name=GAL2; Synonyms=IMP1; OrderedLocusNames=YLR081W; ORFNames=L9449.6;
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].
RX PubMed=2666404; DOI=10.1128/jb.171.8.4486-4493.1989;
RA Szkutnicka K., Tschopp J.F., Andrews L., Cirillo V.P.;
RT "Sequence and structure of the yeast galactose transporter.";
RL J. Bacteriol. 171:4486-4493(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2697639; DOI=10.1016/0378-1119(89)90423-x;
RA Nehlin J.O., Carlberg M., Ronne H.;
RT "Yeast galactose permease is related to yeast and mammalian glucose
RT transporters.";
RL Gene 85:313-319(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-35; SER-39; SER-48;
RP SER-50; SER-53 AND SER-55, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GAL2 is a facilitated diffusion transporter required for both
CC the high-affinity galactokinase-dependent and low-affinity
CC galactokinase-independent galactose transport processes.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; M68547; AAA34623.1; -; Genomic_DNA.
DR EMBL; M81879; AAA34624.1; -; Genomic_DNA.
DR EMBL; Z73253; CAA97640.1; -; Genomic_DNA.
DR EMBL; Z73254; CAA97642.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67585.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09397.1; -; Genomic_DNA.
DR PIR; S64913; S64913.
DR RefSeq; NP_013182.1; NM_001181968.1.
DR AlphaFoldDB; P13181; -.
DR SMR; P13181; -.
DR BioGRID; 31354; 74.
DR DIP; DIP-4773N; -.
DR IntAct; P13181; 2.
DR MINT; P13181; -.
DR STRING; 4932.YLR081W; -.
DR TCDB; 2.A.1.1.6; the major facilitator superfamily (mfs).
DR iPTMnet; P13181; -.
DR MaxQB; P13181; -.
DR PaxDb; P13181; -.
DR PRIDE; P13181; -.
DR EnsemblFungi; YLR081W_mRNA; YLR081W; YLR081W.
DR GeneID; 850770; -.
DR KEGG; sce:YLR081W; -.
DR SGD; S000004071; GAL2.
DR VEuPathDB; FungiDB:YLR081W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P13181; -.
DR OMA; MACMVIY; -.
DR BioCyc; YEAST:G3O-32232-MON; -.
DR PRO; PR:P13181; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P13181; 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; IDA:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0006012; P:galactose metabolic process; IMP:SGD.
DR GO; GO:0015757; P:galactose transmembrane transport; IMP: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 PRINTS; PR00171; SUGRTRNSPORT.
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 Membrane; Phosphoprotein; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..574
FT /note="Galactose transporter"
FT /id="PRO_0000050416"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..362
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 50
FT /note="S -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="A -> R (in Ref. 1; AAA34623)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="G -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="H -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63626 MW; 5ACB68A4094F01A5 CRC64;
MAVEENNMPV VSQQPQAGED VISSLSKDSH LSAQSQKYSN DELKAGESGS EGSQSVPIEI
PKKPMSEYVT VSLLCLCVAF GGFMFGWDTG TISGFVVQTD FLRRFGMKHK DGTHYLSNVR
TGLIVAIFNI GCAFGGIILS KGGDMYGRKK GLSIVVSVYI VGIIIQIASI NKWYQYFIGR
IISGLGVGGI AVLCPMLISE IAPKHLRGTL VSCYQLMITA GIFLGYCTNY GTKSYSNSVQ
WRVPLGLCFA WSLFMIGALT LVPESPRYLC EVNKVEDAKR SIAKSNKVSP EDPAVQAELD
LIMAGIEAEK LAGNASWGEL FSTKTKVFQR LLMGVFVQMF QQLTGNNYFF YYGTVIFKSV
GLDDSFETSI VIGVVNFAST FFSLWTVENL GHRKCLLLGA ATMMACMVIY ASVGVTRLYP
HGKSQPSSKG AGNCMIVFTC FYIFCYATTW APVAWVITAE SFPLRVKSKC MALASASNWV
WGFLIAFFTP FITSAINFYY GYVFMGCLVA MFFYVFFFVP ETKGLSLEEI QELWEEGVLP
WKSEGWIPSS RRGNNYDLED LQHDDKPWYK AMLE
