HXT4_YEAS7
ID HXT4_YEAS7 Reviewed; 576 AA.
AC A6ZT02;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Low-affinity glucose transporter HXT4;
DE AltName: Full=Low-affinity glucose transporter LGT1;
GN Name=HXT4; Synonyms=LGT1, RAG1; ORFNames=SCY_2486;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Low-affinity glucose transporter. Can also transport xylose
CC (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Xylose uptake is strongly inhibited by glucose.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Glucose transport is thought to be mediated by two
CC kinetically distinct systems, a glucose-repressible high-affinity
CC system and a constitutive low-affinity system.
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; AAFW02000082; EDN62333.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZT02; -.
DR SMR; A6ZT02; -.
DR EnsemblFungi; EDN62333; EDN62333; SCY_2486.
DR HOGENOM; CLU_001265_30_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; 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 PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Isopeptide bond; Membrane; Repeat;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..576
FT /note="Low-affinity glucose transporter HXT4"
FT /id="PRO_0000392109"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..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..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..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..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..363
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..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..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P32467"
SQ SEQUENCE 576 AA; 63938 MW; AA753354C6AACE99 CRC64;
MSEEAAYQED TAVQNTPADA LSPVESDSNS ALSTPSNKAE RDDMKDFDEN HEESNNYVEI
PKKPASAYVT VSICCLMVAF GGFVFGWDTG TISGFVAQTD FIRRFGMKHH DGTYYLSKVR
TGLIVSIFNI GCAIGGIILA RLGDMYGRKM GLIVVVVIYI IGIIIQIASI NKWYQYFIGR
IISGLGVGGI AVLSPMLISE VSPKHIRGTL VSCYQLMITL GIFLGYCTNY GTKTYTNSVQ
WRVPLGLGFA WALFMIGGMT FVPESPRYLV EVGKIEEAKR SIALSNKVSA DDPAVMAEVE
VVQATVEAEK LAGNASWGEI FSTKTKVFQR LIMGAMIQSL QQLTGDNYFF YYGTTVFTAV
GLEDSFETSI VLGIVNFAST FVGIFLVERY GRRRCLLWGA ASMTACMVVF ASVGVTRLWP
NGKKNGSSKG AGNCMIVFTC FYLFCFATTW APIPFVVNSE TFPLRVKSKC MAIAQACNWI
WGFLIGFFTP FISGAIDFYY GYVFMGCLVF SYFYVFFFVP ETKGLTLEEV NTLWEEGVLP
WKSPSWVPPN KRGTDYNADD LMHDDQPFYK KMFGKK
