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 27-MAR-2024, entry version 215. 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). RN [17] RP FUNCTION, INTERACTION WITH SMIM43, AND SUBCELLULAR LOCATION. RX PubMed=35810171; DOI=10.1038/s41467-022-31762-x; RA Fu H., Wang T., Kong X., Yan K., Yang Y., Cao J., Yuan Y., Wang N., Kee K., RA Lu Z.J., Xi Q.; RT "A Nodal enhanced micropeptide NEMEP regulates glucose uptake during RT mesendoderm differentiation of embryonic stem cells."; RL Nat. Commun. 13:3984-3984(2022). CC -!- FUNCTION: Facilitative glucose transporter, which is responsible for CC constitutive or basal glucose uptake (PubMed:17320047, CC PubMed:35810171). Has a very broad substrate specificity; can transport CC a wide range of aldoses including both pentoses and hexoses (By CC similarity). Most important energy carrier of the brain: present at the CC blood-brain barrier and assures the energy-independent, facilitative CC transport of glucose into the brain (By similarity). In association CC with BSG and NXNL1, promotes retinal cone survival by increasing CC glucose uptake into photoreceptors (By similarity). Required for CC mesendoderm differentiation (PubMed:35810171). CC {ECO:0000250|UniProtKB:P11166, ECO:0000250|UniProtKB:P46896, CC ECO:0000269|PubMed:17320047, ECO:0000269|PubMed:25957687, CC ECO:0000269|PubMed:35810171}. 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). Interacts with SMIM43; the interaction may CC promote SLC2A1-mediated glucose transport to meet the energy needs of CC mesendoderm differentiation (PubMed:35810171). CC {ECO:0000250|UniProtKB:P11166, ECO:0000250|UniProtKB:P11167, CC ECO:0000269|PubMed:35810171}. CC -!- INTERACTION: CC P17809; A0A286YD83: Smim43; NbExp=5; IntAct=EBI-646060, EBI-46438951; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17320047, CC ECO:0000269|PubMed:30197081, ECO:0000269|PubMed:35810171}; Multi-pass CC membrane protein {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 12. DR ComplexPortal; CPX-3112; Glucose transporter complex 1. DR IntAct; P17809; 3. DR MINT; P17809; -. DR STRING; 10090.ENSMUSP00000030398; -. DR GlyCosmos; P17809; 1 site, No reported glycans. DR GlyGen; P17809; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P17809; -. DR MetOSite; P17809; -. DR PhosphoSitePlus; P17809; -. DR SwissPalm; P17809; -. DR EPD; P17809; -. DR jPOST; P17809; -. DR MaxQB; P17809; -. DR PaxDb; 10090-ENSMUSP00000030398; -. DR PeptideAtlas; P17809; -. DR ProteomicsDB; 271185; -. DR Pumba; P17809; -. DR Antibodypedia; 3451; 858 antibodies from 46 providers. DR DNASU; 20525; -. DR Ensembl; ENSMUST00000030398.10; ENSMUSP00000030398.4; ENSMUSG00000028645.12. DR GeneID; 20525; -. DR KEGG; mmu:20525; -. DR UCSC; uc008ule.2; mouse. DR AGR; MGI:95755; -. 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; WAITASF; -. DR OrthoDB; 1899001at2759; -. 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 80 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 281 other cell types or tissues. DR ExpressionAtlas; P17809; baseline and differential. 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:1990350; C:glucose transporter complex; ISO:MGI. DR GO; GO:0000139; C:Golgi membrane; IDA:MGI. 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: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; ISO:MGI. 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: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 CDD; cd17431; MFS_GLUT_Class1; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 NCBIfam; TIGR00879; SP; 1. DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1. DR PANTHER; PTHR23503:SF51; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 1; 1. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01190; GLUCTRSPORT1. DR PRINTS; PR00171; SUGRTRNSPORT. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1. DR Genevisible; P17809; MM. 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 //