HXT4_YEAST
ID HXT4_YEAST Reviewed; 576 AA.
AC P32467; D3DL44;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Low-affinity glucose transporter HXT4;
DE AltName: Full=Low-affinity glucose transporter LGT1;
GN Name=HXT4; Synonyms=LGT1, RAG1; OrderedLocusNames=YHR092C;
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=7982576; DOI=10.1093/genetics/137.4.957;
RA Theodoris G., Fong N.M., Coons D.M., Bisson L.F.;
RT "High-copy suppression of glucose transport defects by HXT4 and regulatory
RT elements in the promoters of the HXT genes in Saccharomyces cerevisiae.";
RL Genetics 137:957-966(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154188; DOI=10.1002/yea.320091211;
RA Prior C., Fukuhara H., Blaisonneau J., Wesolowski-Louvel M.;
RT "Low-affinity glucose carrier gene LGT1 of Saccharomyces cerevisiae, a
RT homologue of the Kluyveromyces lactis RAG1 gene.";
RL Yeast 9:1373-1377(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 547; 565 AND 567.
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-45, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND IDENTIFICATION OF FRAMESHIFT.
RX PubMed=17180689; DOI=10.1007/s00253-006-0747-1;
RA Saloheimo A., Rauta J., Stasyk O.V., Sibirny A.A., Penttila M.,
RA Ruohonen L.;
RT "Xylose transport studies with xylose-utilizing Saccharomyces cerevisiae
RT strains expressing heterologous and homologous permeases.";
RL Appl. Microbiol. Biotechnol. 74:1041-1052(2007).
CC -!- FUNCTION: Low-affinity glucose transporter. Can also transport xylose.
CC {ECO:0000269|PubMed:17180689}.
CC -!- ACTIVITY REGULATION: Xylose uptake is strongly inhibited by glucose.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 mM for xylose uptake {ECO:0000269|PubMed:17180689};
CC Vmax=190 nmol/min/mg enzyme for xylose uptake
CC {ECO:0000269|PubMed:17180689};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68932.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M81960; AAA20997.1; -; Genomic_DNA.
DR EMBL; X67321; CAA47735.1; -; Genomic_DNA.
DR EMBL; U00060; AAB68932.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006934; DAA06788.2; -; Genomic_DNA.
DR PIR; S46724; S46724.
DR RefSeq; NP_011960.2; NM_001179222.2.
DR AlphaFoldDB; P32467; -.
DR SMR; P32467; -.
DR BioGRID; 36527; 69.
DR DIP; DIP-7908N; -.
DR IntAct; P32467; 11.
DR STRING; 4932.YHR092C; -.
DR TCDB; 2.A.1.1.30; the major facilitator superfamily (mfs).
DR iPTMnet; P32467; -.
DR MaxQB; P32467; -.
DR PaxDb; P32467; -.
DR PRIDE; P32467; -.
DR EnsemblFungi; YHR092C_mRNA; YHR092C; YHR092C.
DR GeneID; 856492; -.
DR KEGG; sce:YHR092C; -.
DR SGD; S000001134; HXT4.
DR VEuPathDB; FungiDB:YHR092C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P32467; -.
DR OMA; HIGWTSP; -.
DR BioCyc; YEAST:G3O-31139-MON; -.
DR PRO; PR:P32467; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32467; 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:0005353; F:fructose transmembrane transporter activity; TAS:SGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015578; F:mannose transmembrane transporter activity; TAS:SGD.
DR GO; GO:0015146; F:pentose transmembrane transporter activity; IMP:SGD.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0008645; P:hexose transmembrane transport; TAS: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; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Isopeptide bond; Membrane; Reference proteome;
KW Repeat; Sugar transport; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..576
FT /note="Low-affinity glucose transporter HXT4"
FT /id="PRO_0000050394"
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:0000269|PubMed:14557538"
SQ SEQUENCE 576 AA; 63910 MW; F58E0060721E9EC7 CRC64;
MSEEAAYQED TAVQNTPADA LSPVESDSNS ALSTPSNKAE RDDMKDFDEN HEESNNYVEI
PKKPASAYVT VSICCLMVAF GGFVFGWDTG TISGFVAQTD FIRRFGMKHH DGTYYLSKVR
TGLIVSIFNI GCAIGGIILA KLGDMYGRKM 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
