GTR1_RAT
ID GTR1_RAT Reviewed; 492 AA.
AC P11167;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1 {ECO:0000305};
DE AltName: Full=Glucose transporter type 1, erythrocyte/brain {ECO:0000303|PubMed:10198040};
DE Short=GLUT-1 {ECO:0000303|PubMed:10198040};
GN Name=Slc2a1 {ECO:0000312|RGD:3704};
GN Synonyms=Glut1 {ECO:0000303|PubMed:10198040};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=3016720; DOI=10.1073/pnas.83.16.5784;
RA Birnbaum M.J., Haspel H.C., Rosen O.M.;
RT "Cloning and characterization of a cDNA encoding the rat brain glucose-
RT transporter protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5784-5788(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=3198639; DOI=10.1016/s0021-9258(19)77665-0;
RA Williams S.A., Birnbaum M.J.;
RT "The rat facilitated glucose transporter gene. Transformation and serum-
RT stimulated transcription initiate from identical sites.";
RL J. Biol. Chem. 263:19513-19518(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=2211693; DOI=10.1016/s0021-9258(17)44734-x;
RA Holman G.D., Kozka I.J., Clark A.E., Flower C.J., Saltis J.,
RA Habberfield A.D., Simpson I.A., Cushman S.W.;
RT "Cell surface labeling of glucose transporter isoform GLUT4 by bis-mannose
RT photolabel. Correlation with stimulation of glucose transport in rat
RT adipose cells by insulin and phorbol ester.";
RL J. Biol. Chem. 265:18172-18179(1990).
RN [5]
RP INTERACTION WITH GIPC, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344; TISSUE=Brain;
RX PubMed=10198040; DOI=10.1091/mbc.10.4.819;
RA Bunn R.C., Jensen M.A., Reed B.C.;
RT "Protein interactions with the glucose transporter binding protein GLUT1CBP
RT that provide a link between GLUT1 and the cytoskeleton.";
RL Mol. Biol. Cell 10:819-832(1999).
RN [6]
RP INTERACTION WITH SGTA.
RX PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA Liou S.T., Wang C.;
RT "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT composed of three structural units with distinct functions.";
RL Arch. Biochem. Biophys. 435:253-263(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21076856; DOI=10.1007/s11010-010-0634-z;
RA Zoidis E., Ghirlanda-Keller C., Schmid C.;
RT "Stimulation of glucose transport in osteoblastic cells by parathyroid
RT hormone and insulin-like growth factor I.";
RL Mol. Cell. Biochem. 348:33-42(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Facilitative glucose transporter, which is responsible for
CC constitutive or basal glucose uptake (PubMed:2211693). Has a very broad
CC substrate specificity; can transport a wide range of aldoses including
CC both pentoses and hexoses (By similarity). Most important energy
CC carrier of the brain: present at the blood-brain barrier and assures
CC the energy-independent, facilitative transport of glucose into the
CC brain (By similarity). In association with BSG and NXNL1, promotes
CC retinal cone survival by increasing glucose uptake into photoreceptors
CC (By similarity). {ECO:0000250|UniProtKB:P11166,
CC ECO:0000250|UniProtKB:P46896, ECO:0000269|PubMed:2211693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:2211693};
CC -!- ACTIVITY REGULATION: The uptake of glucose is inhibited by cytochalasin
CC B. Glucose uptake is increased in response to phorbol ester 12-O-
CC tetradecanoylphorbol-13-acetate (TPA) treatment: TPA-induced glucose
CC uptake requires phosphorylation at Ser-226.
CC {ECO:0000250|UniProtKB:P11166}.
CC -!- SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via
CC C-terminus cytoplasmic region) with DMTN. Interacts with SNX27; the
CC interaction is required when endocytosed to prevent degradation in
CC lysosomes and promote recycling to the plasma membrane. Interacts with
CC STOM (By similarity). Interacts with GIPC (via PDZ domain)
CC (PubMed:10198040). Interacts with SGTA (via Gln-rich region)
CC (PubMed:15708368). Interacts with isoform 1 of BSG (By similarity).
CC {ECO:0000250|UniProtKB:P11166, ECO:0000269|PubMed:10198040,
CC ECO:0000269|PubMed:15708368}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2211693};
CC Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P17809}.
CC -!- TISSUE SPECIFICITY: Detected in osteoblastic cells (at protein level).
CC Detected in brain, and at lower levels in kidney, heart and lung.
CC {ECO:0000269|PubMed:10198040, ECO:0000269|PubMed:21076856,
CC ECO:0000269|PubMed:3016720, ECO:0000269|PubMed:3198639}.
CC -!- PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by
CC increasing cell membrane localization. {ECO:0000250|UniProtKB:P11166}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; M13979; AAA41248.1; -; mRNA.
DR EMBL; M22063; AAA41297.1; -; Genomic_DNA.
DR EMBL; M22061; AAA41297.1; JOINED; Genomic_DNA.
DR EMBL; M22062; AAA41297.1; JOINED; Genomic_DNA.
DR EMBL; BC061873; AAH61873.1; -; mRNA.
DR PIR; A25949; A25949.
DR RefSeq; NP_620182.1; NM_138827.1.
DR AlphaFoldDB; P11167; -.
DR SMR; P11167; -.
DR BioGRID; 246902; 3.
DR ComplexPortal; CPX-3113; Glucose transporter complex 1.
DR IntAct; P11167; 1.
DR MINT; P11167; -.
DR STRING; 10116.ENSRNOP00000061340; -.
DR BindingDB; P11167; -.
DR ChEMBL; CHEMBL5214; -.
DR GlyGen; P11167; 1 site.
DR iPTMnet; P11167; -.
DR PhosphoSitePlus; P11167; -.
DR SwissPalm; P11167; -.
DR PaxDb; P11167; -.
DR PRIDE; P11167; -.
DR Ensembl; ENSRNOT00000064452; ENSRNOP00000061340; ENSRNOG00000007284.
DR GeneID; 24778; -.
DR KEGG; rno:24778; -.
DR CTD; 6513; -.
DR RGD; 3704; Slc2a1.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156792; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P11167; -.
DR OMA; LNATWTV; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P11167; -.
DR TreeFam; TF313762; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR Reactome; R-RNO-5653890; Lactose synthesis.
DR SABIO-RK; P11167; -.
DR PRO; PR:P11167; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007284; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; P11167; baseline and differential.
DR Genevisible; P11167; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0001939; C:female pronucleus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:RGD.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEP:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:0098708; P:glucose import across plasma membrane; ISO:RGD.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:RGD.
DR GO; GO:0042908; P:xenobiotic transport; IDA:RGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002439; Glu_transpt_1.
DR InterPro; IPR045263; GLUT.
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 PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01190; GLUCTRSPORT1.
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 Acetylation; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..492
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 1"
FT /id="PRO_0000050342"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 12..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 34..66
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 88..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 91..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 113..120
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 121..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 145..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 177..185
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 186..206
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 207..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 272..293
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 294..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 307..328
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 329..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 335..355
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 356..365
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 366..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 389..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 402..422
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 423..429
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 451..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 282..283
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 288
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 317
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 380
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 388
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 53963 MW; 05719AB061D0F67C CRC64;
MEPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH RYGESIPSTT
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVSAVLM GFSKLGKSFE
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
GNADLWPLLL SVIFIPALLQ CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD
LQEMKEEGRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL MTIALALLEQ
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAVAVAGFS NWTSNFIVGM
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
ELFHPLGADS QV
