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Protein

Solute carrier family 2, facilitated glucose transporter member 1

Gene

Slc2a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei317 – 3171MonosaccharideBy similarity
Binding sitei388 – 3881MonosaccharideBy similarity

GO - Molecular functioni

  • dehydroascorbic acid transporter activity Source: UniProtKB
  • D-glucose transmembrane transporter activity Source: UniProtKB
  • glucose transmembrane transporter activity Source: RGD
  • kinase binding Source: RGD
  • protein self-association Source: UniProtKB
  • sugar:proton symporter activity Source: RGD
  • xenobiotic transporter activity Source: RGD

GO - Biological processi

  • cellular response to glucose starvation Source: Ensembl
  • dehydroascorbic acid transport Source: UniProtKB
  • glucose transport Source: UniProtKB
  • protein complex assembly Source: UniProtKB
  • proton transport Source: GOC
  • response to osmotic stress Source: RGD
  • xenobiotic transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-196836. Vitamin C (ascorbate) metabolism.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-428790. Facilitative Na+-independent glucose transporters.
R-RNO-5653890. Lactose synthesis.
R-RNO-70153. Glucose transport.
SABIO-RKP11167.

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 2, facilitated glucose transporter member 1
Alternative name(s):
Glucose transporter type 1, erythrocyte/brain
Short name:
GLUT-1
Gene namesi
Name:Slc2a1
Synonyms:Glut-1, Glut1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi3704. Slc2a1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicBy similarityAdd
BLAST
Transmembranei12 – 3322Helical; Name=1By similarityAdd
BLAST
Topological domaini34 – 6633ExtracellularBy similarityAdd
BLAST
Transmembranei67 – 8721Helical; Name=2By similarityAdd
BLAST
Topological domaini88 – 903CytoplasmicBy similarity
Transmembranei91 – 11222Helical; Name=3By similarityAdd
BLAST
Topological domaini113 – 1208ExtracellularBy similarity
Transmembranei121 – 14424Helical; Name=4By similarityAdd
BLAST
Topological domaini145 – 15511CytoplasmicBy similarityAdd
BLAST
Transmembranei156 – 17621Helical; Name=5By similarityAdd
BLAST
Topological domaini177 – 1859ExtracellularBy similarity
Transmembranei186 – 20621Helical; Name=6By similarityAdd
BLAST
Topological domaini207 – 27165CytoplasmicBy similarityAdd
BLAST
Transmembranei272 – 29322Helical; Name=7By similarityAdd
BLAST
Topological domaini294 – 30613ExtracellularBy similarityAdd
BLAST
Transmembranei307 – 32822Helical; Name=8By similarityAdd
BLAST
Topological domaini329 – 3346CytoplasmicBy similarity
Transmembranei335 – 35521Helical; Name=9By similarityAdd
BLAST
Topological domaini356 – 36510ExtracellularBy similarity
Transmembranei366 – 38823Helical; Name=10By similarityAdd
BLAST
Topological domaini389 – 40113CytoplasmicBy similarityAdd
BLAST
Transmembranei402 – 42221Helical; Name=11By similarityAdd
BLAST
Topological domaini423 – 4297ExtracellularBy similarity
Transmembranei430 – 45021Helical; Name=12By similarityAdd
BLAST
Topological domaini451 – 49242CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • blood microparticle Source: Ensembl
  • caveola Source: RGD
  • cell-cell junction Source: RGD
  • cortical actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • extracellular exosome Source: Ensembl
  • female pronucleus Source: Ensembl
  • integral component of membrane Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • midbody Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5214.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Solute carrier family 2, facilitated glucose transporter member 1PRO_0000050342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence analysis
Modified residuei478 – 4781PhosphothreonineCombined sources
Modified residuei490 – 4901PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP11167.
PRIDEiP11167.

PTM databases

iPTMnetiP11167.
PhosphoSiteiP11167.
SwissPalmiP11167.

Expressioni

Tissue specificityi

Detected in osteoblastic cells (at protein level). Detected in brain, and at lower levels in kidney, heart and lung.4 Publications

Gene expression databases

ExpressionAtlasiP11167. baseline and differential.
GenevisibleiP11167. RN.

Interactioni

Subunit structurei

Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via C-terminus cytoplasmic region) with DMTN. Interacts with SNX27; the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with STOM (By similarity). Interacts with GIPC (via PDZ domain).By similarity1 Publication

GO - Molecular functioni

  • kinase binding Source: RGD
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi246902. 1 interaction.
STRINGi10116.ENSRNOP00000061340.

Chemistry

BindingDBiP11167.

Structurei

3D structure databases

ProteinModelPortaliP11167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 2887Monosaccharide bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0569. Eukaryota.
COG0477. LUCA.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP11167.
KOiK07299.
OMAiMLMMNLL.
OrthoDBiEOG7QVM2R.
PhylomeDBiP11167.
TreeFamiTF313762.

Family and domain databases

InterProiIPR002439. Glu_transpt_1.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR01190. GLUCTRSPORT1.
PR00171. 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.

P11167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH
60 70 80 90 100
RYGESIPSTT LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN
110 120 130 140 150
LLAFVSAVLM GFSKLGKSFE MLILGRFIIG VYCGLTTGFV PMYVGEVSPT
160 170 180 190 200
ALRGALGTLH QLGIVVGILI AQVFGLDSIM GNADLWPLLL SVIFIPALLQ
210 220 230 240 250
CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD LQEMKEEGRQ
260 270 280 290 300
MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
310 320 330 340 350
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL
360 370 380 390 400
MTIALALLEQ LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR
410 420 430 440 450
PAAVAVAGFS NWTSNFIVGM CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF
460 470 480 490
KVPETKGRTF DEIASGFRQG GASQSDKTPE ELFHPLGADS QV
Length:492
Mass (Da):53,963
Last modified:July 1, 1989 - v1
Checksum:i05719AB061D0F67C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13979 mRNA. Translation: AAA41248.1.
M22063, M22061, M22062 Genomic DNA. Translation: AAA41297.1.
BC061873 mRNA. Translation: AAH61873.1.
PIRiA25949.
RefSeqiNP_620182.1. NM_138827.1.
UniGeneiRn.3205.

Genome annotation databases

EnsembliENSRNOT00000064452; ENSRNOP00000061340; ENSRNOG00000007284.
GeneIDi24778.
KEGGirno:24778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13979 mRNA. Translation: AAA41248.1.
M22063, M22061, M22062 Genomic DNA. Translation: AAA41297.1.
BC061873 mRNA. Translation: AAH61873.1.
PIRiA25949.
RefSeqiNP_620182.1. NM_138827.1.
UniGeneiRn.3205.

3D structure databases

ProteinModelPortaliP11167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246902. 1 interaction.
STRINGi10116.ENSRNOP00000061340.

Chemistry

BindingDBiP11167.
ChEMBLiCHEMBL5214.

PTM databases

iPTMnetiP11167.
PhosphoSiteiP11167.
SwissPalmiP11167.

Proteomic databases

PaxDbiP11167.
PRIDEiP11167.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000064452; ENSRNOP00000061340; ENSRNOG00000007284.
GeneIDi24778.
KEGGirno:24778.

Organism-specific databases

CTDi6513.
RGDi3704. Slc2a1.

Phylogenomic databases

eggNOGiKOG0569. Eukaryota.
COG0477. LUCA.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP11167.
KOiK07299.
OMAiMLMMNLL.
OrthoDBiEOG7QVM2R.
PhylomeDBiP11167.
TreeFamiTF313762.

Enzyme and pathway databases

ReactomeiR-RNO-196836. Vitamin C (ascorbate) metabolism.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-428790. Facilitative Na+-independent glucose transporters.
R-RNO-5653890. Lactose synthesis.
R-RNO-70153. Glucose transport.
SABIO-RKP11167.

Miscellaneous databases

PROiP11167.

Gene expression databases

ExpressionAtlasiP11167. baseline and differential.
GenevisibleiP11167. RN.

Family and domain databases

InterProiIPR002439. Glu_transpt_1.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR01190. GLUCTRSPORT1.
PR00171. 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. "Cloning and characterization of a cDNA encoding the rat brain glucose-transporter protein."
    Birnbaum M.J., Haspel H.C., Rosen O.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:5784-5788(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "The rat facilitated glucose transporter gene. Transformation and serum-stimulated transcription initiate from identical sites."
    Williams S.A., Birnbaum M.J.
    J. Biol. Chem. 263:19513-19518(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton."
    Bunn R.C., Jensen M.A., Reed B.C.
    Mol. Biol. Cell 10:819-832(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GIPC, TISSUE SPECIFICITY.
    Strain: Fischer 344.
    Tissue: Brain.
  5. "Stimulation of glucose transport in osteoblastic cells by parathyroid hormone and insulin-like growth factor I."
    Zoidis E., Ghirlanda-Keller C., Schmid C.
    Mol. Cell. Biochem. 348:33-42(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGTR1_RAT
AccessioniPrimary (citable) accession number: P11167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.