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Protein

Low-affinity glucose transporter HXT1

Gene

HXT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Low-affinity glucose transporter. HXT1 is as well involved in the transport of mannose.

GO - Molecular functioni

  1. fructose transmembrane transporter activity Source: SGD
  2. galactose transmembrane transporter activity Source: SGD
  3. glucose transmembrane transporter activity Source: SGD
  4. mannose transmembrane transporter activity Source: SGD
  5. pentose transmembrane transporter activity Source: SGD

GO - Biological processi

  1. fructose transport Source: GOC
  2. galactose transport Source: GOC
  3. glucose transport Source: SGD
  4. mannose transport Source: SGD
  5. pentose transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31140-MONOMER.

Protein family/group databases

TCDBi2.A.1.1.108. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Low-affinity glucose transporter HXT1
Gene namesi
Name:HXT1
Synonyms:HOR4
Ordered Locus Names:YHR094C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR094c.
SGDiS000001136. HXT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6060CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei61 – 8121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini82 – 11635ExtracellularSequence AnalysisAdd
BLAST
Transmembranei117 – 13721Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini138 – 1436CytoplasmicSequence Analysis
Transmembranei144 – 16421Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini165 – 17410ExtracellularSequence Analysis
Transmembranei175 – 19521Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini196 – 2016CytoplasmicSequence Analysis
Transmembranei202 – 22221Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini223 – 23614ExtracellularSequence AnalysisAdd
BLAST
Transmembranei237 – 25721Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini258 – 34083CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei341 – 35717Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini358 – 3636ExtracellularSequence Analysis
Transmembranei364 – 38118Helical; Name=8Sequence AnalysisAdd
BLAST
Topological domaini382 – 3887CytoplasmicSequence Analysis
Transmembranei389 – 40921Helical; Name=9Sequence AnalysisAdd
BLAST
Topological domaini410 – 43122ExtracellularSequence AnalysisAdd
BLAST
Transmembranei432 – 45221Helical; Name=10Sequence AnalysisAdd
BLAST
Topological domaini453 – 46917CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei470 – 49021Helical; Name=11Sequence AnalysisAdd
BLAST
Topological domaini491 – 4911ExtracellularSequence Analysis
Transmembranei492 – 51221Helical; Name=12Sequence AnalysisAdd
BLAST
Topological domaini513 – 57058CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Low-affinity glucose transporter HXT1PRO_0000050391Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei38 – 381Phosphoserine2 Publications
Modified residuei44 – 441Phosphoserine2 Publications
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP32465.
PaxDbiP32465.
PeptideAtlasiP32465.

Expressioni

Developmental stagei

Expression is maximal during lag and early exponential phases of growth, decreasing upon further entry into exponential growth.

Inductioni

Repressed at high glucose concentrations.

Gene expression databases

ExpressionAtlasiP32465. differential.
GenevestigatoriP32465.

Interactioni

Protein-protein interaction databases

BioGridi36528. 100 interactions.
DIPiDIP-5593N.
IntActiP32465. 38 interactions.
MINTiMINT-547595.
STRINGi4932.YHR094C.

Structurei

3D structure databases

ProteinModelPortaliP32465.
SMRiP32465. Positions 70-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00720000108754.
HOGENOMiHOG000202870.
InParanoidiP32465.
KOiK08139.
OrthoDBiEOG73JM4H.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32465-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSTPDLISP QKSNSSNSYE LESGRSKAMN TPEGKNESFH DNLSESQVQP
60 70 80 90 100
AVAPPNTGKG VYVTVSICCV MVAFGGFIFG WDTGTISGFV AQTDFLRRFG
110 120 130 140 150
MKHHDGSHYL SKVRTGLIVS IFNIGCAIGG IVLAKLGDMY GRRIGLIVVV
160 170 180 190 200
VIYTIGIIIQ IASINKWYQY FIGRIISGLG VGGITVLSPM LISEVAPSEM
210 220 230 240 250
RGTLVSCYQV MITLGIFLGY CTNFGTKNYS NSVQWRVPLG LCFAWALFMI
260 270 280 290 300
GGMMFVPESP RYLVEAGRID EARASLAKVN KCPPDHPYIQ YELETIEASV
310 320 330 340 350
EEMRAAGTAS WGELFTGKPA MFQRTMMGIM IQSLQQLTGD NYFFYYGTIV
360 370 380 390 400
FQAVGLSDSF ETSIVFGVVN FFSTCCSLYT VDRFGRRNCL MWGAVGMVCC
410 420 430 440 450
YVVYASVGVT RLWPNGQDQP SSKGAGNCMI VFACFYIFCF ATTWAPIAYV
460 470 480 490 500
VISECFPLRV KSKCMSIASA ANWIWGFLIS FFTPFITGAI NFYYGYVFMG
510 520 530 540 550
CMVFAYFYVF FFVPETKGLS LEEVNDMYAE GVLPWKSASW VPVSKRGADY
560 570
NADDLMHDDQ PFYKSLFSRK
Length:570
Mass (Da):63,261
Last modified:October 1, 1993 - v1
Checksum:i311CBB35AE80D19E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701Missing in AAA34700. (PubMed:2046678)Curated
Sequence conflicti469 – 4691S → T in AAA34700. (PubMed:2046678)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07079 Genomic DNA. Translation: AAB59311.1.
M82963 Genomic DNA. Translation: AAA34700.1.
U00060 Genomic DNA. Translation: AAB68933.1.
BK006934 Genomic DNA. Translation: DAA06789.1.
PIRiS38798.
RefSeqiNP_011962.1. NM_001179224.1.

Genome annotation databases

EnsemblFungiiYHR094C; YHR094C; YHR094C.
GeneIDi856494.
KEGGisce:YHR094C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07079 Genomic DNA. Translation: AAB59311.1.
M82963 Genomic DNA. Translation: AAA34700.1.
U00060 Genomic DNA. Translation: AAB68933.1.
BK006934 Genomic DNA. Translation: DAA06789.1.
PIRiS38798.
RefSeqiNP_011962.1. NM_001179224.1.

3D structure databases

ProteinModelPortaliP32465.
SMRiP32465. Positions 70-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36528. 100 interactions.
DIPiDIP-5593N.
IntActiP32465. 38 interactions.
MINTiMINT-547595.
STRINGi4932.YHR094C.

Protein family/group databases

TCDBi2.A.1.1.108. the major facilitator superfamily (mfs).

Proteomic databases

MaxQBiP32465.
PaxDbiP32465.
PeptideAtlasiP32465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR094C; YHR094C; YHR094C.
GeneIDi856494.
KEGGisce:YHR094C.

Organism-specific databases

CYGDiYHR094c.
SGDiS000001136. HXT1.

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00720000108754.
HOGENOMiHOG000202870.
InParanoidiP32465.
KOiK08139.
OrthoDBiEOG73JM4H.

Enzyme and pathway databases

BioCyciYEAST:G3O-31140-MONOMER.

Miscellaneous databases

NextBioi982203.

Gene expression databases

ExpressionAtlasiP32465. differential.
GenevestigatoriP32465.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The HXT1 gene product of Saccharomyces cerevisiae is a new member of the family of hexose transporters."
    Lewis D.A., Bisson L.F.
    Mol. Cell. Biol. 11:3804-3813(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Roles of multiple glucose transporters in Saccharomyces cerevisiae."
    Ko C.H., Liang H., Gaber R.F.
    Mol. Cell. Biol. 13:638-648(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHXT1_YEAST
AccessioniPrimary (citable) accession number: P32465
Secondary accession number(s): D3DL45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Glucose transport is thought to be mediated by two kinetically distinct systems, a glucose-repressible high-affinity system and a constitutive low-affinity system.
Present with 23300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.