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Protein

Low-affinity glucose transporter HXT3

Gene

HXT3

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.

GO - Molecular functioni

  • fructose transmembrane transporter activity Source: SGD
  • glucose transmembrane transporter activity Source: SGD
  • mannose transmembrane transporter activity Source: SGD

GO - Biological processi

  • fructose transport Source: GOC
  • glucose transmembrane transport Source: GOC
  • hexose transport Source: SGD
  • mannose transport Source: GOC
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29899-MONOMER.
ReactomeiR-SCE-428790. Facilitative Na+-independent glucose transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-affinity glucose transporter HXT3
Gene namesi
Name:HXT3
Ordered Locus Names:YDR345C
ORF Names:D9651.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR345C.
SGDiS000002753. HXT3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757CytoplasmicSequence analysisAdd
BLAST
Transmembranei58 – 7821Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini79 – 11335ExtracellularSequence analysisAdd
BLAST
Transmembranei114 – 13421Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini135 – 1406CytoplasmicSequence analysis
Transmembranei141 – 16121Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini162 – 17110ExtracellularSequence analysis
Transmembranei172 – 19221Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini193 – 1986CytoplasmicSequence analysis
Transmembranei199 – 21921Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini220 – 23314ExtracellularSequence analysisAdd
BLAST
Transmembranei234 – 25421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini255 – 33783CytoplasmicSequence analysisAdd
BLAST
Transmembranei338 – 35417Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini355 – 3606ExtracellularSequence analysis
Transmembranei361 – 37818Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini379 – 3857CytoplasmicSequence analysis
Transmembranei386 – 40621Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini407 – 42822ExtracellularSequence analysisAdd
BLAST
Transmembranei429 – 44921Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini450 – 46617CytoplasmicSequence analysisAdd
BLAST
Transmembranei467 – 48721Helical; Name=11Sequence analysisAdd
BLAST
Topological domaini488 – 4881ExtracellularSequence analysis
Transmembranei489 – 50921Helical; Name=12Sequence analysisAdd
BLAST
Topological domaini510 – 56758CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Low-affinity glucose transporter HXT3PRO_0000050393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei26 – 261PhosphoserineBy similarity
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP32466.
PeptideAtlasiP32466.

PTM databases

iPTMnetiP32466.

Expressioni

Inductioni

Repressed at high glucose concentrations.

Interactioni

Protein-protein interaction databases

BioGridi32401. 49 interactions.
DIPiDIP-4178N.
IntActiP32466. 4 interactions.
MINTiMINT-492422.

Structurei

3D structure databases

ProteinModelPortaliP32466.
SMRiP32466. Positions 67-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00720000108754.
HOGENOMiHOG000202870.
InParanoidiP32466.
KOiK08139.
OMAiIGMVCCY.
OrthoDBiEOG73JM4H.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
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.

P32466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSTPDLISP QKSSENSNAD LPSNSSQVMN MPEEKGVQDD FQAEADQVLT
60 70 80 90 100
NPNTGKGAYV TVSICCVMVA FGGFVFGWDT GTISGFVAQT DFLRRFGMKH
110 120 130 140 150
KDGSYYLSKV RTGLIVSIFN IGCAIGGIIL AKLGDMYGRK MGLIVVVVIY
160 170 180 190 200
IIGIIIQIAS INKWYQYFIG RIISGLGVGG IAVLSPMLIS EVAPKEMRGT
210 220 230 240 250
LVSCYQLMIT LGIFLGYCTN FGTKNYSNSV QWRVPLGLCF AWALFMIGGM
260 270 280 290 300
TFVPESPRYL VEAGQIDEAR ASLSKVNKVA PDHPFIQQEL EVIEASVEEA
310 320 330 340 350
RAAGSASWGE LFTGKPAMFK RTMMGIMIQS LQQLTGDNYF FYYGTTVFNA
360 370 380 390 400
VGMSDSFETS IVFGVVNFFS TCCSLYTVDR FGRRNCLLYG AIGMVCCYVV
410 420 430 440 450
YASVGVTRLW PNGEGNGSSK GAGNCMIVFA CFYIFCFATT WAPIAYVVIS
460 470 480 490 500
ETFPLRVKSK AMSIATAANW LWGFLIGFFT PFITGAINFY YGYVFMGCMV
510 520 530 540 550
FAYFYVFFFV PETKGLTLEE VNDMYAEGVL PWKSASWVPT SQRGANYDAD
560
ALMHDDQPFY KKMFGKK
Length:567
Mass (Da):62,558
Last modified:October 1, 1993 - v1
Checksum:iF6CA1F7B70204526
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07080 Genomic DNA. Translation: AAA34672.1.
U51032 Genomic DNA. Translation: AAB64781.1.
BK006938 Genomic DNA. Translation: DAA12185.1.
PIRiS31294.
RefSeqiNP_010632.1. NM_001180653.1.

Genome annotation databases

EnsemblFungiiYDR345C; YDR345C; YDR345C.
GeneIDi851946.
KEGGisce:YDR345C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07080 Genomic DNA. Translation: AAA34672.1.
U51032 Genomic DNA. Translation: AAB64781.1.
BK006938 Genomic DNA. Translation: DAA12185.1.
PIRiS31294.
RefSeqiNP_010632.1. NM_001180653.1.

3D structure databases

ProteinModelPortaliP32466.
SMRiP32466. Positions 67-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32401. 49 interactions.
DIPiDIP-4178N.
IntActiP32466. 4 interactions.
MINTiMINT-492422.

PTM databases

iPTMnetiP32466.

Proteomic databases

MaxQBiP32466.
PeptideAtlasiP32466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR345C; YDR345C; YDR345C.
GeneIDi851946.
KEGGisce:YDR345C.

Organism-specific databases

EuPathDBiFungiDB:YDR345C.
SGDiS000002753. HXT3.

Phylogenomic databases

GeneTreeiENSGT00720000108754.
HOGENOMiHOG000202870.
InParanoidiP32466.
KOiK08139.
OMAiIGMVCCY.
OrthoDBiEOG73JM4H.

Enzyme and pathway databases

BioCyciYEAST:G3O-29899-MONOMER.
ReactomeiR-SCE-428790. Facilitative Na+-independent glucose transporters.

Miscellaneous databases

NextBioi970030.
PROiP32466.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
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. "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].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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.
  6. "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-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.

Entry informationi

Entry nameiHXT3_YEAST
AccessioniPrimary (citable) accession number: P32466
Secondary accession number(s): D6VSX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 142 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 37200 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.