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P32465 (HXT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low-affinity glucose transporter HXT1
Gene names
Name:HXT1
Synonyms:HOR4
Ordered Locus Names:YHR094C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Membrane; Multi-pass membrane protein.

Developmental stage

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

Induction

Repressed at high glucose concentrations.

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.

Sequence similarities

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Low-affinity glucose transporter HXT1
PRO_0000050391

Regions

Topological domain1 – 6060Cytoplasmic Potential
Transmembrane61 – 8121Helical; Name=1; Potential
Topological domain82 – 11635Extracellular Potential
Transmembrane117 – 13721Helical; Name=2; Potential
Topological domain138 – 1436Cytoplasmic Potential
Transmembrane144 – 16421Helical; Name=3; Potential
Topological domain165 – 17410Extracellular Potential
Transmembrane175 – 19521Helical; Name=4; Potential
Topological domain196 – 2016Cytoplasmic Potential
Transmembrane202 – 22221Helical; Name=5; Potential
Topological domain223 – 23614Extracellular Potential
Transmembrane237 – 25721Helical; Name=6; Potential
Topological domain258 – 34083Cytoplasmic Potential
Transmembrane341 – 35717Helical; Name=7; Potential
Topological domain358 – 3636Extracellular Potential
Transmembrane364 – 38118Helical; Name=8; Potential
Topological domain382 – 3887Cytoplasmic Potential
Transmembrane389 – 40921Helical; Name=9; Potential
Topological domain410 – 43122Extracellular Potential
Transmembrane432 – 45221Helical; Name=10; Potential
Topological domain453 – 46917Cytoplasmic Potential
Transmembrane470 – 49021Helical; Name=11; Potential
Topological domain4911Extracellular Potential
Transmembrane492 – 51221Helical; Name=12; Potential
Topological domain513 – 57058Cytoplasmic Potential

Amino acid modifications

Modified residue231Phosphoserine Ref.9
Modified residue381Phosphoserine Ref.7 Ref.10
Modified residue441Phosphoserine Ref.7 Ref.10
Glycosylation2281N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict701Missing in AAA34700. Ref.1
Sequence conflict4691S → T in AAA34700. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32465 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 311CBB35AE80D19E

FASTA57063,261
        10         20         30         40         50         60 
MNSTPDLISP QKSNSSNSYE LESGRSKAMN TPEGKNESFH DNLSESQVQP AVAPPNTGKG 

        70         80         90        100        110        120 
VYVTVSICCV MVAFGGFIFG WDTGTISGFV AQTDFLRRFG MKHHDGSHYL SKVRTGLIVS 

       130        140        150        160        170        180 
IFNIGCAIGG IVLAKLGDMY GRRIGLIVVV VIYTIGIIIQ IASINKWYQY FIGRIISGLG 

       190        200        210        220        230        240 
VGGITVLSPM LISEVAPSEM RGTLVSCYQV MITLGIFLGY CTNFGTKNYS NSVQWRVPLG 

       250        260        270        280        290        300 
LCFAWALFMI GGMMFVPESP RYLVEAGRID EARASLAKVN KCPPDHPYIQ YELETIEASV 

       310        320        330        340        350        360 
EEMRAAGTAS WGELFTGKPA MFQRTMMGIM IQSLQQLTGD NYFFYYGTIV FQAVGLSDSF 

       370        380        390        400        410        420 
ETSIVFGVVN FFSTCCSLYT VDRFGRRNCL MWGAVGMVCC YVVYASVGVT RLWPNGQDQP 

       430        440        450        460        470        480 
SSKGAGNCMI VFACFYIFCF ATTWAPIAYV VISECFPLRV KSKCMSIASA ANWIWGFLIS 

       490        500        510        520        530        540 
FFTPFITGAI NFYYGYVFMG CMVFAYFYVF FFVPETKGLS LEEVNDMYAE GVLPWKSASW 

       550        560        570 
VPVSKRGADY NADDLMHDDQ PFYKSLFSRK 

« Hide

References

« Hide 'large scale' references
[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]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07079 Genomic DNA. Translation: AAB59311.1.
M82963 Genomic DNA. Translation: AAA34700.1.
U00060 Genomic DNA. Translation: AAB68933.1.
BK006934 Genomic DNA. Translation: DAA06789.1.
PIRS38798.
RefSeqNP_011962.1. NM_001179224.1.

3D structure databases

ProteinModelPortalP32465.
SMRP32465. Positions 70-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36528. 100 interactions.
DIPDIP-5593N.
IntActP32465. 38 interactions.
MINTMINT-547595.
STRING4932.YHR094C.

Protein family/group databases

TCDB2.A.1.1.108. the major facilitator superfamily (mfs).

Proteomic databases

MaxQBP32465.
PaxDbP32465.
PeptideAtlasP32465.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR094C; YHR094C; YHR094C.
GeneID856494.
KEGGsce:YHR094C.

Organism-specific databases

CYGDYHR094c.
SGDS000001136. HXT1.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00720000108754.
HOGENOMHOG000202870.
KOK08139.
OMACMSIASA.
OrthoDBEOG73JM4H.

Enzyme and pathway databases

BioCycYEAST:G3O-31140-MONOMER.

Gene expression databases

GenevestigatorP32465.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSPR00171. SUGRTRNSPORT.
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00879. SP. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982203.

Entry information

Entry nameHXT1_YEAST
AccessionPrimary (citable) accession number: P32465
Secondary accession number(s): D3DL45
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 14, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families