GTR1_MOUSE
ID GTR1_MOUSE Reviewed; 492 AA.
AC P17809; Q61608; Q6GTI3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 206.
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:17320047};
DE Short=GLUT-1 {ECO:0000303|PubMed:17320047};
DE Short=GT1 {ECO:0000303|PubMed:17320047};
GN Name=Slc2a1 {ECO:0000312|MGI:MGI:95755};
GN Synonyms=Glut1 {ECO:0000303|PubMed:17320047};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2654938; DOI=10.1073/pnas.86.9.3150;
RA Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T.,
RA Cornelius P., Pekala P.H., Lane M.D.;
RT "Sequence, tissue distribution, and differential expression of mRNA for a
RT putative insulin-responsive glucose transporter in mouse 3T3-L1
RT adipocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2190533; DOI=10.1016/0003-9861(90)90490-p;
RA Reed B.C., Shade D., Alperovich F., Vang M.;
RT "3T3-L1 adipocyte glucose transporter (HepG2 class): sequence and
RT regulation of protein and mRNA expression by insulin, differentiation, and
RT glucose starvation.";
RL Arch. Biochem. Biophys. 279:261-274(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
RX PubMed=1339457; DOI=10.1016/s0021-9258(19)50423-9;
RA Murakami T., Nishiyama T., Shirotani T., Shinohara Y., Kan M., Ishii K.,
RA Kanai F., Nakazuru S., Ebina Y.;
RT "Identification of two enhancer elements in the gene encoding the type 1
RT glucose transporter from the mouse which are responsive to serum, growth
RT factor, and oncogenes.";
RL J. Biol. Chem. 267:9300-9306(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 151-237, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=1289053; DOI=10.1242/dev.116.3.555;
RA Smith D.E., Gridley T.;
RT "Differential screening of a PCR-generated mouse embryo cDNA library:
RT glucose transporters are differentially expressed in early postimplantation
RT mouse embryos.";
RL Development 116:555-561(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 357-463, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=1765007; DOI=10.1242/dev.113.1.363;
RA Hogan A., Heyner S., Charron M.J., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Thorens B., Schultz G.A.;
RT "Glucose transporter gene expression in early mouse embryos.";
RL Development 113:363-372(1991).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=14578187; DOI=10.1016/s0002-9440(10)63546-8;
RA Heilig C., Brosius F., Siu B., Concepcion L., Mortensen R., Heilig K.,
RA Zhu M., Weldon R., Wu G., Conner D.;
RT "Implications of glucose transporter protein type 1 (GLUT1)-haplodeficiency
RT in embryonic stem cells for their survival in response to hypoxic stress.";
RL Am. J. Pathol. 163:1873-1885(2003).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17320047; DOI=10.1016/j.bbrc.2007.02.025;
RA Roach W., Plomann M.;
RT "PACSIN3 overexpression increases adipocyte glucose transport through
RT GLUT1.";
RL Biochem. Biophys. Res. Commun. 355:745-750(2007).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25957687; DOI=10.1016/j.cell.2015.03.023;
RA Ait-Ali N., Fridlich R., Millet-Puel G., Clerin E., Delalande F.,
RA Jaillard C., Blond F., Perrocheau L., Reichman S., Byrne L.C.,
RA Olivier-Bandini A., Bellalou J., Moyse E., Bouillaud F., Nicol X.,
RA Dalkara D., van Dorsselaer A., Sahel J.A., Leveillard T.;
RT "Rod-derived cone viability factor promotes cone survival by stimulating
RT aerobic glycolysis.";
RL Cell 161:817-832(2015).
RN [16]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-485.
RX PubMed=30197081; DOI=10.1016/j.cell.2018.08.019;
RA Meyer K., Kirchner M., Uyar B., Cheng J.Y., Russo G.,
RA Hernandez-Miranda L.R., Szymborska A., Zauber H., Rudolph I.M.,
RA Willnow T.E., Akalin A., Haucke V., Gerhardt H., Birchmeier C., Kuehn R.,
RA Krauss M., Diecke S., Pascual J.M., Selbach M.;
RT "Mutations in disordered regions can cause disease by creating dileucine
RT motifs.";
RL Cell 175:239-253(2018).
CC -!- FUNCTION: Facilitative glucose transporter, which is responsible for
CC constitutive or basal glucose uptake (PubMed:17320047). Has a very
CC broad substrate specificity; can transport a wide range of aldoses
CC including both pentoses and hexoses (By similarity). Most important
CC energy carrier of the brain: present at the blood-brain barrier and
CC assures the energy-independent, facilitative transport of glucose into
CC the 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:17320047,
CC ECO:0000269|PubMed:25957687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11166};
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 isoform 2. Interacts with
CC SNX27; the interaction is required when endocytosed to prevent
CC degradation in lysosomes and promote recycling to the plasma membrane.
CC Interacts with GIPC (via PDZ domain). Interacts with STOM. Interacts
CC with SGTA (via Gln-rich region) (By similarity). Interacts with isoform
CC 1 of BSG (By similarity). {ECO:0000250|UniProtKB:P11166,
CC ECO:0000250|UniProtKB:P11167}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17320047,
CC ECO:0000269|PubMed:30197081}; Multi-pass membrane protein
CC {ECO:0000255}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:25957687}.
CC -!- TISSUE SPECIFICITY: Retina (at protein level).
CC {ECO:0000269|PubMed:25957687}.
CC -!- DEVELOPMENTAL STAGE: Levels decline 3-fold between days 7.5 and 12.5 of
CC gestation. At 7.5 dpc, expressed more strongly in extraembryonic
CC tissues than in the embryo proper. Expressed in amnion, chorion, and
CC ectoplacental cone. In the yolk sac, expressed more strongly in the
CC mesoderm layer than the ectoderm. Expression fairly widespread in the
CC embryo at 8.5 dpc, but by 10.5 dpc, expression is down-regulated and
CC observed in the eye and the spinal cord. {ECO:0000269|PubMed:1289053,
CC ECO:0000269|PubMed:1765007}.
CC -!- PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by
CC increasing cell membrane localization. {ECO:0000250|UniProtKB:P11166}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality.
CC {ECO:0000269|PubMed:14578187}.
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; M23384; AAA37752.1; -; mRNA.
DR EMBL; M22998; AAA37707.1; -; mRNA.
DR EMBL; AK170873; BAE42084.1; -; mRNA.
DR EMBL; AL606975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30474.1; -; Genomic_DNA.
DR EMBL; BC055340; AAH55340.1; -; mRNA.
DR EMBL; X69697; CAA49367.1; -; mRNA.
DR EMBL; S77924; AAB20846.2; -; mRNA.
DR CCDS; CCDS18569.1; -.
DR PIR; A44887; A44887.
DR PIR; S09705; S09705.
DR RefSeq; NP_035530.2; NM_011400.3.
DR AlphaFoldDB; P17809; -.
DR SMR; P17809; -.
DR BioGRID; 203304; 9.
DR ComplexPortal; CPX-3112; Glucose transporter complex 1.
DR IntAct; P17809; 2.
DR MINT; P17809; -.
DR STRING; 10090.ENSMUSP00000030398; -.
DR GlyGen; P17809; 1 site.
DR iPTMnet; P17809; -.
DR PhosphoSitePlus; P17809; -.
DR SwissPalm; P17809; -.
DR EPD; P17809; -.
DR jPOST; P17809; -.
DR MaxQB; P17809; -.
DR PaxDb; P17809; -.
DR PeptideAtlas; P17809; -.
DR PRIDE; P17809; -.
DR ProteomicsDB; 271185; -.
DR Antibodypedia; 3451; 734 antibodies from 46 providers.
DR DNASU; 20525; -.
DR Ensembl; ENSMUST00000030398; ENSMUSP00000030398; ENSMUSG00000028645.
DR GeneID; 20525; -.
DR KEGG; mmu:20525; -.
DR UCSC; uc008ule.2; mouse.
DR CTD; 6513; -.
DR MGI; MGI:95755; Slc2a1.
DR VEuPathDB; HostDB:ENSMUSG00000028645; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156792; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P17809; -.
DR OMA; LNATWTV; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P17809; -.
DR TreeFam; TF313762; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR Reactome; R-MMU-5653890; Lactose synthesis.
DR BioGRID-ORCS; 20525; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Slc2a1; mouse.
DR PRO; PR:P17809; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P17809; protein.
DR Bgee; ENSMUSG00000028645; Expressed in iris and 278 other tissues.
DR ExpressionAtlas; P17809; baseline and differential.
DR Genevisible; P17809; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
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:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0001939; C:female pronucleus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
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:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:0098708; P:glucose import across plasma membrane; ISO:MGI.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:MGI.
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; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IBA:GO_Central.
DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:MGI.
DR GO; GO:0042908; P:xenobiotic transport; ISO:MGI.
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_0000050339"
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:0000250|UniProtKB:P11166"
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:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT MUTAGEN 485
FT /note="P->L: Lethality immediately after birth in knockin
FT mice; caused by creation of a dileucine internalization
FT motif that promotes mislocalization of the protein."
FT /evidence="ECO:0000269|PubMed:30197081"
FT CONFLICT 52
FT /note="Y -> I (in Ref. 1; AAA37752)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..195
FT /note="IFI -> VFV (in Ref. 1; AAA37752)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..360
FT /note="LLER -> MQEQ (in Ref. 9; AAB20846)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> R (in Ref. 1; AAA37752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 53985 MW; 464B668853D7636E CRC64;
MDPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH RYGEPIPSTT
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVAAVLM GFSKLGKSFE
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
GNADLWPLLL SVIFIPALLQ CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD
LQEMKEEGRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL MTIALALLER
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAIAVAGFS NWTSNFIVGM
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
ELFHPLGADS QV
