GTR1_HUMAN
ID GTR1_HUMAN Reviewed; 492 AA.
AC P11166; A8K9S6; B2R620; D3DPX0; O75535; Q0P512; Q147X2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 245.
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:18245775};
DE Short=GLUT-1 {ECO:0000303|PubMed:18245775};
DE AltName: Full=HepG2 glucose transporter {ECO:0000303|PubMed:2834252, ECO:0000303|PubMed:3839598};
GN Name=SLC2A1 {ECO:0000312|HGNC:HGNC:11005};
GN Synonyms=GLUT1 {ECO:0000303|PubMed:18245775};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
RP ASN-45, LACK OF GLYCOSYLATION AT ASN-411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=3839598; DOI=10.1126/science.3839598;
RA Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I., Morris H.R.,
RA Allard W.J., Lienhard G.E., Lodish H.F.;
RT "Sequence and structure of a human glucose transporter.";
RL Science 229:941-945(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=2834252; DOI=10.2337/diab.37.5.657;
RA Fukumoto H., Seino S., Imura H., Seino Y., Bell G.I.;
RT "Characterization and expression of human HepG2/erythrocyte glucose-
RT transporter gene.";
RL Diabetes 37:657-661(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-492.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-423.
RC TISSUE=Articular cartilage;
RA Neama G., Richardson S., Bell S., Carter S., Mobasheri A.;
RT "Molecular characterization and cloning of glucose transporters in human
RT articular chondrocytes.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-192; LEU-204 AND
RP PRO-205.
RX PubMed=18245775; DOI=10.1074/jbc.m708896200;
RA Mueckler M., Makepeace C.;
RT "Transmembrane segment 6 of the Glut1 glucose transporter is an outer helix
RT and contains amino acid side chains essential for transport activity.";
RL J. Biol. Chem. 283:11550-11555(2008).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH ADD2 AND DMTN, INTERACTION WITH DMTN, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18347014; DOI=10.1074/jbc.m707818200;
RA Khan A.A., Hanada T., Mohseni M., Jeong J.J., Zeng L., Gaetani M., Li D.,
RA Reed B.C., Speicher D.W., Chishti A.H.;
RT "Dematin and adducin provide a novel link between the spectrin cytoskeleton
RT and human erythrocyte membrane by directly interacting with glucose
RT transporter-1.";
RL J. Biol. Chem. 283:14600-14609(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-340.
RX PubMed=19449892; DOI=10.1021/bi900521n;
RA Mueckler M., Makepeace C.;
RT "Model of the exofacial substrate-binding site and helical folding of the
RT human Glut1 glucose transporter based on scanning mutagenesis.";
RL Biochemistry 48:5934-5942(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45.
RC TISSUE=Leukemic T-cell;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH STOM, AND
RP SUBUNIT.
RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in
RT human erythrocyte membrane domains.";
RL Biochim. Biophys. Acta 1828:956-966(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND SER-490, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP INTERACTION WITH SNX27.
RX PubMed=23563491; DOI=10.1038/ncb2721;
RA Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J.,
RA Tavare J.M., Cullen P.J.;
RT "A global analysis of SNX27-retromer assembly and cargo specificity reveals
RT a function in glucose and metal ion transport.";
RL Nat. Cell Biol. 15:461-471(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INTERACTION WITH BSG.
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 [23]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT SER-226, MUTAGENESIS OF SER-226,
RP CHARACTERIZATION OF VARIANTS EIG12 PRO-223 AND GLN-223, AND
RP CHARACTERIZATION OF VARIANT GLUT1DS1 TRP-223.
RX PubMed=25982116; DOI=10.1016/j.molcel.2015.04.015;
RA Lee E.E., Ma J., Sacharidou A., Mi W., Salato V.K., Nguyen N., Jiang Y.,
RA Pascual J.M., North P.E., Shaul P.W., Mettlen M., Wang R.C.;
RT "A protein kinase C phosphorylation motif in GLUT1 affects glucose
RT transport and is mutated in GLUT1 deficiency syndrome.";
RL Mol. Cell 58:845-853(2015).
RN [24] {ECO:0007744|PDB:4PYP}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF VARIANT GLUT1DS1 GLN-329 IN
RP COMPLEX WITH NONYL-BETA-D-GLUCOSIDE, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF ASN-45.
RX PubMed=24847886; DOI=10.1038/nature13306;
RA Deng D., Xu C., Sun P., Wu J., Yan C., Hu M., Yan N.;
RT "Crystal structure of the human glucose transporter GLUT1.";
RL Nature 510:121-125(2014).
RN [25] {ECO:0007744|PDB:5EQG, ECO:0007744|PDB:5EQH, ECO:0007744|PDB:5EQI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH CYTOCHALASIN B,
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=27078104; DOI=10.1073/pnas.1603735113;
RA Kapoor K., Finer-Moore J.S., Pedersen B.P., Caboni L., Waight A.,
RA Hillig R.C., Bringmann P., Heisler I., Muller T., Siebeneicher H.,
RA Stroud R.M.;
RT "Mechanism of inhibition of human glucose transporter GLUT1 is conserved
RT between cytochalasin B and phenylalanine amides.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:4711-4716(2016).
RN [26]
RP VARIANT GLUT1DS1 ILE-310, FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=10227690; DOI=10.1023/a:1022544131826;
RA Klepper J., Wang D., Fischbarg J., Vera J.C., Jarjour I.T.,
RA O'Driscoll K.R., De Vivo D.C.;
RT "Defective glucose transport across brain tissue barriers: a newly
RT recognized neurological syndrome.";
RL Neurochem. Res. 24:587-594(1999).
RN [27]
RP VARIANTS GLUT1DS1 PHE-66; LEU-126; LYS-146; GLU-256 AND TRP-333.
RX PubMed=10980529;
RX DOI=10.1002/1098-1004(200009)16:3<224::aid-humu5>3.0.co;2-p;
RA Wang D., Kranz-Eble P., De Vivo D.C.;
RT "Mutational analysis of GLUT1 (SLC2A1) in Glut-1 deficiency syndrome.";
RL Hum. Mutat. 16:224-231(2000).
RN [28]
RP ERRATUM OF PUBMED:10980529.
RA Wang D., Kranz-Eble P., De Vivo D.C.;
RL Hum. Mutat. 16:527-527(2000).
RN [29]
RP VARIANT GLUT1DS1 HIS-126.
RX PubMed=11603379; DOI=10.1002/ana.1222;
RA Brockmann K., Wang D., Korenke C.G., von Moers A., Ho Y.-Y., Pascual J.M.,
RA Kuang K., Yang H., Ma L., Kranz-Eble P., Fischbarg J., Hanefeld F.,
RA De Vivo D.C.;
RT "Autosomal dominant Glut-1 deficiency syndrome and familial epilepsy.";
RL Ann. Neurol. 50:476-485(2001).
RN [30]
RP VARIANT GLUT1DS1 ASP-91.
RX PubMed=11136715; DOI=10.1093/hmg/10.1.63;
RA Klepper J., Willemsen M., Verrips A., Guertsen E., Herrmann R., Kutzick C.,
RA Floercken A., Voit T.;
RT "Autosomal dominant transmission of GLUT1 deficiency.";
RL Hum. Mol. Genet. 10:63-68(2001).
RN [31]
RP VARIANTS GLUT1DS1 CYS-126; HIS-126; LYS-146; CYS-153 AND TRP-333.
RX PubMed=12325075; DOI=10.1002/ana.10311;
RA Pascual J.M., van Heertum R.L., Wang D., Engelstad K., De Vivo D.C.;
RT "Imaging the metabolic footprint of Glut1 deficiency on the brain.";
RL Ann. Neurol. 52:458-464(2002).
RN [32]
RP VARIANT GLUT1DS2 ILE-34.
RX PubMed=14605501; DOI=10.1023/a:1025999914822;
RA Overweg-Plandsoen W.C.G., Groener J.E.M., Wang D., Onkenhout W.,
RA Brouwer O.F., Bakker H.D., De Vivo D.C.;
RT "GLUT-1 deficiency without epilepsy -- an exceptional case.";
RL J. Inherit. Metab. Dis. 26:559-563(2003).
RN [33]
RP VARIANTS GLUT1DS1 SER-34; HIS-126; SER-130; CYS-153; LEU-169 DEL; MET-295
RP AND TRP-333, AND CHARACTERIZATION OF VARIANTS GLUT1 DEFICIENCY SER-34;
RP HIS-126; SER-130; CYS-153; LEU-169 DEL; MET-295 AND TRP-333.
RX PubMed=15622525; DOI=10.1002/ana.20331;
RA Wang D., Pascual J.M., Yang H., Engelstad K., Jhung S., Sun R.P.,
RA De Vivo D.C.;
RT "Glut-1 deficiency syndrome: clinical, genetic, and therapeutic aspects.";
RL Ann. Neurol. 57:111-118(2005).
RN [34]
RP VARIANTS GLUT1DS2 THR-275; 282-GLN--SER-285 DEL AND SER-314.
RX PubMed=18451999; DOI=10.1172/jci34438;
RA Weber Y.G., Storch A., Wuttke T.V., Brockmann K., Kempfle J., Maljevic S.,
RA Margari L., Kamm C., Schneider S.A., Huber S.M., Pekrun A., Roebling R.,
RA Seebohm G., Koka S., Lang C., Kraft E., Blazevic D., Salvo-Vargas A.,
RA Fauler M., Mottaghy F.M., Muenchau A., Edwards M.J., Presicci A.,
RA Margari F., Gasser T., Lang F., Bhatia K.P., Lehmann-Horn F., Lerche H.;
RT "GLUT1 mutations are a cause of paroxysmal exertion-induced dyskinesias and
RT induce hemolytic anemia by a cation leak.";
RL J. Clin. Invest. 118:2157-2168(2008).
RN [35]
RP VARIANT EIG12 PRO-223, VARIANTS GLUT1DS2 CYS-126 AND LEU-324,
RP CHARACTERIZATION OF VARIANT EIG12 PRO-223, AND CHARACTERIZATION OF VARIANTS
RP GLUT1DS2 CYS-126 AND LEU-324.
RX PubMed=19798636; DOI=10.1002/ana.21724;
RA Suls A., Mullen S.A., Weber Y.G., Verhaert K., Ceulemans B., Guerrini R.,
RA Wuttke T.V., Salvo-Vargas A., Deprez L., Claes L.R., Jordanova A.,
RA Berkovic S.F., Lerche H., De Jonghe P., Scheffer I.E.;
RT "Early-onset absence epilepsy caused by mutations in the glucose
RT transporter GLUT1.";
RL Ann. Neurol. 66:415-419(2009).
RN [36]
RP VARIANT GLUT1DS1 TYR-292 INS.
RX PubMed=19901175; DOI=10.1001/archneurol.2009.236;
RA Perez-Duenas B., Prior C., Ma Q., Fernandez-Alvarez E., Setoain X.,
RA Artuch R., Pascual J.M.;
RT "Childhood chorea with cerebral hypotrophy: a treatable GLUT1 energy
RT failure syndrome.";
RL Arch. Neurol. 66:1410-1414(2009).
RN [37]
RP VARIANTS GLUT1DS2 TRP-92 AND GLN-333.
RX PubMed=19630075; DOI=10.1002/mds.22507;
RA Schneider S.A., Paisan-Ruiz C., Garcia-Gorostiaga I., Quinn N.P.,
RA Weber Y.G., Lerche H., Hardy J., Bhatia K.P.;
RT "GLUT1 gene mutations cause sporadic paroxysmal exercise-induced
RT dyskinesias.";
RL Mov. Disord. 24:1684-1688(2009).
RN [38]
RP VARIANT GLUT1DS1 TRP-468.
RX PubMed=20221955; DOI=10.1055/s-0030-1248264;
RA Klepper J., Scheffer H., Elsaid M.F., Kamsteeg E.J., Leferink M.,
RA Ben-Omran T.;
RT "Autosomal recessive inheritance of GLUT1 deficiency syndrome.";
RL Neuropediatrics 40:207-210(2009).
RN [39]
RP VARIANTS GLUT1DS1 TYR-34; VAL-96; SER-130; VAL-155; CYS-212; HIS-212;
RP TRP-223; MET-295; GLN-329; GLN-333; ASP-382; ASP-405 AND LEU-485, VARIANTS
RP GLUT1DS2 TRP-93 AND HIS-153, AND VARIANT LEU-303.
RX PubMed=20129935; DOI=10.1093/brain/awp336;
RA Leen W.G., Klepper J., Verbeek M.M., Leferink M., Hofste T.,
RA van Engelen B.G., Wevers R.A., Arthur T., Bahi-Buisson N., Ballhausen D.,
RA Bekhof J., van Bogaert P., Carrilho I., Chabrol B., Champion M.P.,
RA Coldwell J., Clayton P., Donner E., Evangeliou A., Ebinger F., Farrell K.,
RA Forsyth R.J., de Goede C.G., Gross S., Grunewald S., Holthausen H.,
RA Jayawant S., Lachlan K., Laugel V., Leppig K., Lim M.J., Mancini G.,
RA Marina A.D., Martorell L., McMenamin J., Meuwissen M.E., Mundy H.,
RA Nilsson N.O., Panzer A., Poll-The B.T., Rauscher C., Rouselle C.M.,
RA Sandvig I., Scheffner T., Sheridan E., Simpson N., Sykora P., Tomlinson R.,
RA Trounce J., Webb D., Weschke B., Scheffer H., Willemsen M.A.;
RT "Glucose transporter-1 deficiency syndrome: the expanding clinical and
RT genetic spectrum of a treatable disorder.";
RL Brain 133:655-670(2010).
RN [40]
RP VARIANT GLUT1DS2 THR-317.
RX PubMed=21204808; DOI=10.1111/j.1528-1167.2010.02726.x;
RA Afawi Z., Suls A., Ekstein D., Kivity S., Neufeld M.Y., Oliver K.,
RA De Jonghe P., Korczyn A.D., Berkovic S.F.;
RT "Mild adolescent/adult onset epilepsy and paroxysmal exercise-induced
RT dyskinesia due to GLUT1 deficiency.";
RL Epilepsia 51:2466-2469(2010).
RN [41]
RP VARIANT GLUT1DS2 ILE-165.
RX PubMed=20621801; DOI=10.1016/j.jns.2010.05.017;
RA Urbizu A., Cuenca-Leon E., Raspall-Chaure M., Gratacos M., Conill J.,
RA Redecillas S., Roig-Quilis M., Macaya A.;
RT "Paroxysmal exercise-induced dyskinesia, writer's cramp, migraine with aura
RT and absence epilepsy in twin brothers with a novel SLC2A1 missense
RT mutation.";
RL J. Neurol. Sci. 295:110-113(2010).
RN [42]
RP VARIANTS GLUT1DS2 ILE-95; PRO-223; SER-314 AND LEU-324, AND VARIANTS
RP GLUT1DS1 ASP-91 AND HIS-126.
RX PubMed=20574033; DOI=10.1212/wnl.0b013e3181eb58b4;
RA Mullen S.A., Suls A., De Jonghe P., Berkovic S.F., Scheffer I.E.;
RT "Absence epilepsies with widely variable onset are a key feature of
RT familial GLUT1 deficiency.";
RL Neurology 75:432-440(2010).
RN [43]
RP INVOLVEMENT IN SDCHCN, VARIANTS SDCHCN ASP-286 AND ILE-435 DEL, AND
RP CHARACTERIZATION OF VARIANTS SDCHCN ASP-286 AND ILE-435 DEL.
RX PubMed=21791420; DOI=10.1182/blood-2010-12-326645;
RA Flatt J.F., Guizouarn H., Burton N.M., Borgese F., Tomlinson R.J.,
RA Forsyth R.J., Baldwin S.A., Levinson B.E., Quittet P., Aguilar-Martinez P.,
RA Delaunay J., Stewart G.W., Bruce L.J.;
RT "Stomatin-deficient cryohydrocytosis results from mutations in SLC2A1: a
RT novel form of GLUT1 deficiency syndrome.";
RL Blood 118:5267-5277(2011).
RN [44]
RP VARIANT GLUT1DS2 PRO-294.
RX PubMed=20830593; DOI=10.1007/s00415-010-5702-5;
RA Anheim M., Maillart E., Vuillaumier-Barrot S., Flamand-Rouviere C.,
RA Pineau F., Ewenczyk C., Riant F., Apartis E., Roze E.;
RT "Excellent response to acetazolamide in a case of paroxysmal dyskinesias
RT due to GLUT1-deficiency.";
RL J. Neurol. 258:316-317(2011).
RN [45]
RP VARIANTS DYT9 CYS-126 AND CYS-212.
RX PubMed=21832227; DOI=10.1212/wnl.0b013e31822e0479;
RA Weber Y.G., Kamm C., Suls A., Kempfle J., Kotschet K., Schule R.,
RA Wuttke T.V., Maljevic S., Liebrich J., Gasser T., Ludolph A.C.,
RA Van Paesschen W., Schols L., De Jonghe P., Auburger G., Lerche H.;
RT "Paroxysmal choreoathetosis/spasticity (DYT9) is caused by a GLUT1
RT defect.";
RL Neurology 77:959-964(2011).
RN [46]
RP VARIANTS EIG12 HIS-51; MET-60; THR-77; ALA-149; SER-218; GLN-223; VAL-243;
RP SER-411 AND TRP-458, AND CHARACTERIZATION OF VARIANTS EIG12 MET-60; THR-77;
RP SER-218; GLN-223; VAL-243; SER-411 AND TRP-458.
RX PubMed=23280796; DOI=10.1002/ana.23702;
RA Arsov T., Mullen S.A., Rogers S., Phillips A.M., Lawrence K.M.,
RA Damiano J.A., Goldberg-Stern H., Afawi Z., Kivity S., Trager C., Petrou S.,
RA Berkovic S.F., Scheffer I.E.;
RT "Glucose transporter 1 deficiency in the idiopathic generalized
RT epilepsies.";
RL Ann. Neurol. 72:807-815(2012).
RN [47]
RP INVOLVEMENT IN SDCHCN, VARIANT SDCHCN ILE-435 DEL, AND CHARACTERIZATION OF
RP VARIANT SDCHCN ILE-435 DEL.
RX PubMed=22492876; DOI=10.1210/jc.2012-1399;
RA Bawazir W.M., Gevers E.F., Flatt J.F., Ang A.L., Jacobs B., Oren C.,
RA Grunewald S., Dattani M., Bruce L.J., Stewart G.W.;
RT "An infant with pseudohyperkalemia, hemolysis, and seizures: cation-leaky
RT GLUT1-deficiency syndrome due to a SLC2A1 mutation.";
RL J. Clin. Endocrinol. Metab. 97:E987-E993(2012).
RN [48]
RP VARIANT EIG12 CYS-232, AND CHARACTERIZATION OF VARIANT EIG12 CYS-232.
RX PubMed=22282645; DOI=10.1212/wnl.0b013e318247ff54;
RA Striano P., Weber Y.G., Toliat M.R., Schubert J., Leu C., Chaimana R.,
RA Baulac S., Guerrero R., LeGuern E., Lehesjoki A.E., Polvi A., Robbiano A.,
RA Serratosa J.M., Guerrini R., Nurnberg P., Sander T., Zara F., Lerche H.,
RA Marini C.;
RT "GLUT1 mutations are a rare cause of familial idiopathic generalized
RT epilepsy.";
RL Neurology 78:557-562(2012).
RN [49]
RP CHARACTERIZATION OF VARIANT GLUT1DS1 LEU-485, AND SUBCELLULAR LOCATION.
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:18245775, PubMed:19449892,
CC PubMed:25982116, PubMed:27078104, PubMed:10227690). Has a very broad
CC substrate specificity; can transport a wide range of aldoses including
CC both pentoses and hexoses (PubMed:18245775, PubMed:19449892). Most
CC important energy carrier of the brain: present at the blood-brain
CC barrier and assures the energy-independent, facilitative transport of
CC glucose into the brain (PubMed:10227690). In association with BSG and
CC NXNL1, promotes retinal cone survival by increasing glucose uptake into
CC photoreceptors (By similarity). {ECO:0000250|UniProtKB:P46896,
CC ECO:0000269|PubMed:10227690, ECO:0000269|PubMed:18245775,
CC ECO:0000269|PubMed:19449892, ECO:0000269|PubMed:25982116,
CC ECO:0000269|PubMed:27078104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:10227690,
CC ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:27078104};
CC -!- ACTIVITY REGULATION: The uptake of glucose is inhibited by cytochalasin
CC B and Phe-amide core-scaffold inhibitors GLUT-i1 and GLUT-i2
CC (PubMed:27078104). These inhibitors bind in the central cavity of the
CC inward-open state and overlap the glucose-binding site
CC (PubMed:27078104). Glucose uptake is increased in response to phorbol
CC ester 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment: TPA-induced
CC glucose uptake requires phosphorylation at Ser-226 (PubMed:25982116).
CC {ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:27078104}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.6 mM for glucose {ECO:0000269|PubMed:25982116};
CC KM=50.1 mM for glucose (in presence of TPA)
CC {ECO:0000269|PubMed:25982116};
CC -!- PATHWAY: Carbohydrate degradation.
CC -!- SUBUNIT: Interacts with GIPC (via PDZ domain) (By similarity). Found in
CC a complex with ADD2, DMTN and SLC2A1. Interacts (via C-terminus
CC cytoplasmic region) with DMTN isoform 2 (PubMed:18347014). Interacts
CC with SNX27; the interaction is required when endocytosed to prevent
CC degradation in lysosomes and promote recycling to the plasma membrane
CC (PubMed:23563491). Interacts with STOM (PubMed:23219802). Interacts
CC with SGTA (via Gln-rich region) (By similarity). Interacts with isoform
CC 1 of BSG (PubMed:25957687). {ECO:0000250|UniProtKB:P11167,
CC ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:23219802,
CC ECO:0000269|PubMed:23563491, ECO:0000269|PubMed:25957687}.
CC -!- INTERACTION:
CC P11166; O43889-2: CREB3; NbExp=3; IntAct=EBI-717153, EBI-625022;
CC P11166; P11166: SLC2A1; NbExp=3; IntAct=EBI-717153, EBI-717153;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18245775,
CC ECO:0000269|PubMed:19449892, ECO:0000269|PubMed:23219802,
CC ECO:0000269|PubMed:24847886, ECO:0000269|PubMed:25982116,
CC ECO:0000269|PubMed:30197081}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Photoreceptor
CC inner segment {ECO:0000250|UniProtKB:P17809}. Note=Localizes primarily
CC at the cell surface (PubMed:18245775, PubMed:19449892, PubMed:23219802,
CC PubMed:25982116, PubMed:24847886). Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (PubMed:17081065).
CC {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:18245775,
CC ECO:0000269|PubMed:19449892, ECO:0000269|PubMed:23219802,
CC ECO:0000269|PubMed:24847886, ECO:0000269|PubMed:25982116}.
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC Expressed at variable levels in many human tissues.
CC {ECO:0000269|PubMed:23219802}.
CC -!- PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by
CC increasing cell membrane localization. {ECO:0000269|PubMed:25982116}.
CC -!- DISEASE: GLUT1 deficiency syndrome 1 (GLUT1DS1) [MIM:606777]: A
CC neurologic disorder showing wide phenotypic variability. The most
CC severe 'classic' phenotype comprises infantile-onset epileptic
CC encephalopathy associated with delayed development, acquired
CC microcephaly, motor incoordination, and spasticity. Onset of seizures,
CC usually characterized by apneic episodes, staring spells, and episodic
CC eye movements, occurs within the first 4 months of life. Other
CC paroxysmal findings include intermittent ataxia, confusion, lethargy,
CC sleep disturbance, and headache. Varying degrees of cognitive
CC impairment can occur, ranging from learning disabilities to severe
CC intellectual disability. {ECO:0000269|PubMed:10227690,
CC ECO:0000269|PubMed:10980529, ECO:0000269|PubMed:11136715,
CC ECO:0000269|PubMed:11603379, ECO:0000269|PubMed:12325075,
CC ECO:0000269|PubMed:15622525, ECO:0000269|PubMed:19901175,
CC ECO:0000269|PubMed:20129935, ECO:0000269|PubMed:20221955,
CC ECO:0000269|PubMed:20574033, ECO:0000269|PubMed:24847886,
CC ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:30197081}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: GLUT1 deficiency syndrome 2 (GLUT1DS2) [MIM:612126]: A
CC clinically variable disorder characterized primarily by onset in
CC childhood of paroxysmal exercise-induced dyskinesia. The dyskinesia
CC involves transient abnormal involuntary movements, such as dystonia and
CC choreoathetosis, induced by exercise or exertion, and affecting the
CC exercised limbs. Some patients may also have epilepsy, most commonly
CC childhood absence epilepsy. Mild intellectual disability may also
CC occur. In some patients involuntary exertion-induced dystonic,
CC choreoathetotic, and ballistic movements may be associated with
CC macrocytic hemolytic anemia. {ECO:0000269|PubMed:14605501,
CC ECO:0000269|PubMed:18451999, ECO:0000269|PubMed:19630075,
CC ECO:0000269|PubMed:19798636, ECO:0000269|PubMed:20129935,
CC ECO:0000269|PubMed:20574033, ECO:0000269|PubMed:20621801,
CC ECO:0000269|PubMed:20830593, ECO:0000269|PubMed:21204808}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Epilepsy, idiopathic generalized 12 (EIG12) [MIM:614847]: A
CC disorder characterized by recurring generalized seizures in the absence
CC of detectable brain lesions and/or metabolic abnormalities. Generalized
CC seizures arise diffusely and simultaneously from both hemispheres of
CC the brain. Seizure types include juvenile myoclonic seizures, absence
CC seizures, and generalized tonic-clonic seizures. In some EIG12 patients
CC seizures may remit with age. {ECO:0000269|PubMed:19798636,
CC ECO:0000269|PubMed:22282645, ECO:0000269|PubMed:23280796,
CC ECO:0000269|PubMed:25982116}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Dystonia 9 (DYT9) [MIM:601042]: An autosomal dominant
CC neurologic disorder characterized by childhood onset of paroxysmal
CC choreoathetosis and progressive spastic paraplegia. Most patients show
CC some degree of cognitive impairment. Other variable features may
CC include seizures, migraine headaches, and ataxia.
CC {ECO:0000269|PubMed:21832227}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Stomatin-deficient cryohydrocytosis with neurologic defects
CC (SDCHCN) [MIM:608885]: A rare form of stomatocytosis characterized by
CC episodic hemolytic anemia, cold-induced red cells cation leak, erratic
CC hyperkalemia, neonatal hyperbilirubinemia, hepatosplenomegaly,
CC cataracts, seizures, intellectual disability, and movement disorder.
CC {ECO:0000269|PubMed:21791420, ECO:0000269|PubMed:22492876}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=GLUT1 entry;
CC URL="https://en.wikipedia.org/wiki/GLUT1";
CC ---------------------------------------------------------------------------
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DR EMBL; K03195; AAA52571.1; -; mRNA.
DR EMBL; AK292791; BAF85480.1; -; mRNA.
DR EMBL; AK312403; BAG35317.1; -; mRNA.
DR EMBL; CH471059; EAX07124.1; -; Genomic_DNA.
DR EMBL; BC118590; AAI18591.1; -; mRNA.
DR EMBL; BC121804; AAI21805.1; -; mRNA.
DR EMBL; M20653; AAB61084.1; -; Genomic_DNA.
DR EMBL; AF070544; AAC28635.1; -; mRNA.
DR EMBL; AY034633; AAK56795.1; -; mRNA.
DR CCDS; CCDS477.1; -.
DR PIR; A27217; A27217.
DR RefSeq; NP_006507.2; NM_006516.2.
DR PDB; 4PYP; X-ray; 3.17 A; A=1-492.
DR PDB; 5EQG; X-ray; 2.90 A; A=1-492.
DR PDB; 5EQH; X-ray; 2.99 A; A=1-492.
DR PDB; 5EQI; X-ray; 3.00 A; A=1-492.
DR PDB; 6THA; X-ray; 2.40 A; A=1-492.
DR PDBsum; 4PYP; -.
DR PDBsum; 5EQG; -.
DR PDBsum; 5EQH; -.
DR PDBsum; 5EQI; -.
DR PDBsum; 6THA; -.
DR AlphaFoldDB; P11166; -.
DR SMR; P11166; -.
DR BioGRID; 112404; 229.
DR ComplexPortal; CPX-3111; Glucose transporter complex 1.
DR CORUM; P11166; -.
DR DIP; DIP-23N; -.
DR IntAct; P11166; 58.
DR MINT; P11166; -.
DR STRING; 9606.ENSP00000416293; -.
DR BindingDB; P11166; -.
DR ChEMBL; CHEMBL2535; -.
DR DrugBank; DB08831; 2-deoxyglucose.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB11059; Carboxymethylcellulose.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB08830; Dehydroascorbic acid.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB00292; Etomidate.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR DrugBank; DB01296; Glucosamine.
DR DrugBank; DB02709; Resveratrol.
DR DrugCentral; P11166; -.
DR GuidetoPHARMACOLOGY; 875; -.
DR TCDB; 2.A.1.1.28; the major facilitator superfamily (mfs).
DR GlyConnect; 573; 13 N-Linked glycans, 1 O-Linked glycan (1 site).
DR GlyGen; P11166; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P11166; -.
DR MetOSite; P11166; -.
DR PhosphoSitePlus; P11166; -.
DR SwissPalm; P11166; -.
DR BioMuta; SLC2A1; -.
DR DMDM; 115502394; -.
DR CPTAC; CPTAC-274; -.
DR CPTAC; CPTAC-275; -.
DR EPD; P11166; -.
DR jPOST; P11166; -.
DR MassIVE; P11166; -.
DR MaxQB; P11166; -.
DR PaxDb; P11166; -.
DR PeptideAtlas; P11166; -.
DR PRIDE; P11166; -.
DR ProteomicsDB; 52703; -.
DR Antibodypedia; 3451; 734 antibodies from 46 providers.
DR DNASU; 6513; -.
DR Ensembl; ENST00000426263.10; ENSP00000416293.2; ENSG00000117394.24.
DR GeneID; 6513; -.
DR KEGG; hsa:6513; -.
DR MANE-Select; ENST00000426263.10; ENSP00000416293.2; NM_006516.4; NP_006507.2.
DR UCSC; uc001cik.3; human.
DR CTD; 6513; -.
DR DisGeNET; 6513; -.
DR GeneCards; SLC2A1; -.
DR GeneReviews; SLC2A1; -.
DR HGNC; HGNC:11005; SLC2A1.
DR HPA; ENSG00000117394; Tissue enhanced (placenta, skin).
DR MalaCards; SLC2A1; -.
DR MIM; 138140; gene.
DR MIM; 601042; phenotype.
DR MIM; 606777; phenotype.
DR MIM; 608885; phenotype.
DR MIM; 612126; phenotype.
DR MIM; 614847; phenotype.
DR neXtProt; NX_P11166; -.
DR OpenTargets; ENSG00000117394; -.
DR Orphanet; 64280; Childhood absence epilepsy.
DR Orphanet; 71277; Classic glucose transporter type 1 deficiency syndrome.
DR Orphanet; 86911; Epilepsy with myoclonic absences.
DR Orphanet; 168577; Hereditary cryohydrocytosis with reduced stomatin.
DR Orphanet; 1942; Myoclonic-astatic epilepsy.
DR Orphanet; 53583; Paroxysmal dystonic choreathetosis with episodic ataxia and spasticity.
DR Orphanet; 98811; Paroxysmal exertion-induced dyskinesia.
DR PharmGKB; PA35875; -.
DR VEuPathDB; HostDB:ENSG00000117394; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156792; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P11166; -.
DR OMA; LNATWTV; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P11166; -.
DR TreeFam; TF313762; -.
DR BioCyc; MetaCyc:ENSG00000117394-MON; -.
DR PathwayCommons; P11166; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR Reactome; R-HSA-5619043; Defective SLC2A1 causes GLUT1 deficiency syndrome 1 (GLUT1DS1).
DR Reactome; R-HSA-5653890; Lactose synthesis.
DR SignaLink; P11166; -.
DR SIGNOR; P11166; -.
DR BioGRID-ORCS; 6513; 201 hits in 1089 CRISPR screens.
DR ChiTaRS; SLC2A1; human.
DR GeneWiki; GLUT1; -.
DR GenomeRNAi; 6513; -.
DR Pharos; P11166; Tchem.
DR PRO; PR:P11166; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P11166; protein.
DR Bgee; ENSG00000117394; Expressed in tibial nerve and 162 other tissues.
DR ExpressionAtlas; P11166; baseline and differential.
DR Genevisible; P11166; HS.
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:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; ISS:ARUK-UCL.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:ARUK-UCL.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IMP:ARUK-UCL.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central.
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; IMP:ARUK-UCL.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IMP:ARUK-UCL.
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; IDA: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; IMP:ARUK-UCL.
DR DisProt; DP02855; -.
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 3D-structure; Acetylation; Cataract; Cell membrane;
KW Direct protein sequencing; Disease variant; Dystonia; Epilepsy;
KW Glycoprotein; Hereditary hemolytic anemia; Intellectual disability;
KW Membrane; Phosphoprotein; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 1"
FT /id="PRO_0000050338"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 12..33
FT /note="Helical; Name=1"
FT TOPO_DOM 34..66
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT TOPO_DOM 88..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 91..112
FT /note="Helical; Name=3"
FT TOPO_DOM 113..120
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 121..144
FT /note="Helical; Name=4"
FT TOPO_DOM 145..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT TOPO_DOM 177..185
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 186..206
FT /note="Helical; Name=6"
FT TOPO_DOM 207..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 272..293
FT /note="Helical; Name=7"
FT TOPO_DOM 294..306
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 307..328
FT /note="Helical; Name=8"
FT TOPO_DOM 329..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 335..355
FT /note="Helical; Name=9"
FT TOPO_DOM 356..365
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 366..388
FT /note="Helical; Name=10"
FT TOPO_DOM 389..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 402..422
FT /note="Helical; Name=11"
FT TOPO_DOM 423..429
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24847886"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT TOPO_DOM 451..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24847886"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000305|PubMed:30197081"
FT BINDING 137
FT /ligand="cytochalasin B"
FT /ligand_id="ChEBI:CHEBI:23527"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:27078104,
FT ECO:0007744|PDB:5EQI"
FT BINDING 282..283
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000305|PubMed:24847886"
FT BINDING 282
FT /ligand="cytochalasin B"
FT /ligand_id="ChEBI:CHEBI:23527"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:27078104,
FT ECO:0007744|PDB:5EQI"
FT BINDING 288
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000305|PubMed:24847886,
FT ECO:0007744|PDB:4PYP"
FT BINDING 317
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000305|PubMed:24847886,
FT ECO:0007744|PDB:4PYP"
FT BINDING 380
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000305|PubMed:24847886,
FT ECO:0007744|PDB:4PYP"
FT BINDING 388
FT /ligand="cytochalasin B"
FT /ligand_id="ChEBI:CHEBI:23527"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:27078104,
FT ECO:0007744|PDB:5EQI"
FT BINDING 411
FT /ligand="cytochalasin B"
FT /ligand_id="ChEBI:CHEBI:23527"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:27078104"
FT SITE 411
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:3839598"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 226
FT /note="Phosphoserine; by PKC/PRKCB"
FT /evidence="ECO:0000269|PubMed:25982116"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:3839598"
FT VARIANT 34
FT /note="N -> I (in GLUT1DS2; dbSNP:rs80359812)"
FT /evidence="ECO:0000269|PubMed:14605501"
FT /id="VAR_054755"
FT VARIANT 34
FT /note="N -> S (in GLUT1DS1; 55% of wild-type glucose uptake
FT activity; dbSNP:rs80359812)"
FT /evidence="ECO:0000269|PubMed:15622525"
FT /id="VAR_054756"
FT VARIANT 34
FT /note="N -> Y (in GLUT1DS1)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065206"
FT VARIANT 51
FT /note="R -> H (in EIG12; unknown pathological significance;
FT dbSNP:rs201815571)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076226"
FT VARIANT 60
FT /note="T -> M (in EIG12; unknown pathological significance;
FT decreased glucose transport; dbSNP:rs142986731)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076227"
FT VARIANT 66
FT /note="S -> F (in GLUT1DS1; dbSNP:rs80359813)"
FT /evidence="ECO:0000269|PubMed:10980529"
FT /id="VAR_013283"
FT VARIANT 77
FT /note="M -> T (in EIG12; decreased glucose transport;
FT dbSNP:rs1187210267)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076228"
FT VARIANT 91
FT /note="G -> D (in GLUT1DS1; significantly decreases the
FT transport of 3-O-methyl-D-glucose; dbSNP:rs80359814)"
FT /evidence="ECO:0000269|PubMed:11136715,
FT ECO:0000269|PubMed:20574033"
FT /id="VAR_013182"
FT VARIANT 92
FT /note="R -> W (in GLUT1DS2; dbSNP:rs202060209)"
FT /evidence="ECO:0000269|PubMed:19630075"
FT /id="VAR_069077"
FT VARIANT 93
FT /note="R -> W (in GLUT1DS2; dbSNP:rs267607061)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065207"
FT VARIANT 95
FT /note="S -> I (in GLUT1DS2; dbSNP:rs267607060)"
FT /evidence="ECO:0000269|PubMed:20574033"
FT /id="VAR_065208"
FT VARIANT 96
FT /note="M -> V (in GLUT1DS1; dbSNP:rs753161833)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065209"
FT VARIANT 126
FT /note="R -> C (in GLUT1DS1, GLUT1DS2 and DYT9; reduced
FT transporter activity; dbSNP:rs80359818)"
FT /evidence="ECO:0000269|PubMed:12325075,
FT ECO:0000269|PubMed:19798636, ECO:0000269|PubMed:21832227"
FT /id="VAR_054757"
FT VARIANT 126
FT /note="R -> H (in GLUT1DS1; significantly decreases the
FT transport of 3-O-methyl-D-glucose and dehydroascorbic acid;
FT 57% of wild-type glucose uptake activity;
FT dbSNP:rs80359816)"
FT /evidence="ECO:0000269|PubMed:11603379,
FT ECO:0000269|PubMed:12325075, ECO:0000269|PubMed:15622525,
FT ECO:0000269|PubMed:20574033"
FT /id="VAR_013183"
FT VARIANT 126
FT /note="R -> L (in GLUT1DS1; dbSNP:rs80359816)"
FT /evidence="ECO:0000269|PubMed:10980529"
FT /id="VAR_013184"
FT VARIANT 130
FT /note="G -> S (in GLUT1DS1; 75% of wild-type glucose uptake
FT activity; dbSNP:rs80359819)"
FT /evidence="ECO:0000269|PubMed:15622525,
FT ECO:0000269|PubMed:20129935"
FT /id="VAR_054758"
FT VARIANT 146
FT /note="E -> K (in GLUT1DS1; dbSNP:rs80359820)"
FT /evidence="ECO:0000269|PubMed:10980529,
FT ECO:0000269|PubMed:12325075"
FT /id="VAR_013284"
FT VARIANT 149
FT /note="P -> A (in EIG12; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076229"
FT VARIANT 153
FT /note="R -> C (in GLUT1DS1; 44% of wild-type glucose uptake
FT activity)"
FT /evidence="ECO:0000269|PubMed:12325075,
FT ECO:0000269|PubMed:15622525"
FT /id="VAR_054759"
FT VARIANT 153
FT /note="R -> H (in GLUT1DS2; dbSNP:rs794727642)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065210"
FT VARIANT 155
FT /note="A -> V (in GLUT1DS1)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065211"
FT VARIANT 165
FT /note="V -> I (in GLUT1DS2; dbSNP:rs1057520545)"
FT /evidence="ECO:0000269|PubMed:20621801"
FT /id="VAR_065212"
FT VARIANT 169
FT /note="Missing (in GLUT1DS1; 48% of wild-type glucose
FT uptake activity; dbSNP:rs80359832)"
FT /evidence="ECO:0000269|PubMed:15622525"
FT /id="VAR_054760"
FT VARIANT 212
FT /note="R -> C (in GLUT1DS1 and DYT9; dbSNP:rs387907312)"
FT /evidence="ECO:0000269|PubMed:20129935,
FT ECO:0000269|PubMed:21832227"
FT /id="VAR_065213"
FT VARIANT 212
FT /note="R -> H (in GLUT1DS1; dbSNP:rs886039517)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065214"
FT VARIANT 218
FT /note="R -> S (in EIG12; decreased glucose transport)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076230"
FT VARIANT 223
FT /note="R -> P (in EIG12; mild phenotype; reduced
FT transporter activity; impaired phosphorylation by PKC;
FT dbSNP:rs397514564)"
FT /evidence="ECO:0000269|PubMed:19798636,
FT ECO:0000269|PubMed:20574033, ECO:0000269|PubMed:25982116"
FT /id="VAR_065215"
FT VARIANT 223
FT /note="R -> Q (in EIG12; unknown pathological significance;
FT no effect on glucose transport; impaired phosphorylation by
FT PKC; dbSNP:rs397514564)"
FT /evidence="ECO:0000269|PubMed:23280796,
FT ECO:0000269|PubMed:25982116"
FT /id="VAR_076231"
FT VARIANT 223
FT /note="R -> W (in GLUT1DS1; impaired phosphorylation by
FT PKC; dbSNP:rs796053248)"
FT /evidence="ECO:0000269|PubMed:20129935,
FT ECO:0000269|PubMed:25982116"
FT /id="VAR_065216"
FT VARIANT 232
FT /note="R -> C (in EIG12; the mutant protein is expressed at
FT the cell surface but has mildly decreased glucose uptake
FT (70%) compared to wild-type; dbSNP:rs387907313)"
FT /evidence="ECO:0000269|PubMed:22282645"
FT /id="VAR_069078"
FT VARIANT 243
FT /note="E -> V (in EIG12; decreased glucose transport)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076232"
FT VARIANT 256
FT /note="K -> E (in GLUT1DS1; dbSNP:rs121909738)"
FT /evidence="ECO:0000269|PubMed:10980529"
FT /id="VAR_013185"
FT VARIANT 275
FT /note="A -> T (in GLUT1DS2; the mutation decreases glucose
FT transport but does not affect cation permeability;
FT dbSNP:rs121909740)"
FT /evidence="ECO:0000269|PubMed:18451999"
FT /id="VAR_054761"
FT VARIANT 282..285
FT /note="Missing (in GLUT1DS2; accompanied by hemolytic
FT anemia and altered erythrocyte ion concentrations; the
FT mutation decreases glucose transport and causes a cation
FT leak that alteres intracellular concentrations of sodium
FT potassium and calcium)"
FT /evidence="ECO:0000269|PubMed:18451999"
FT /id="VAR_054762"
FT VARIANT 286
FT /note="G -> D (in SDCHCN; no effect on protein abundance;
FT no effect on localization to the plasma membrane; loss of
FT D-glucose transporter activity; increased cation leakage;
FT dbSNP:rs864309514)"
FT /evidence="ECO:0000269|PubMed:21791420,
FT ECO:0000269|PubMed:22492876"
FT /id="VAR_076233"
FT VARIANT 292
FT /note="Y -> YY (in GLUT1DS1)"
FT /evidence="ECO:0000269|PubMed:19901175"
FT /id="VAR_069079"
FT VARIANT 294
FT /note="S -> P (in GLUT1DS2)"
FT /evidence="ECO:0000269|PubMed:20830593"
FT /id="VAR_065784"
FT VARIANT 295
FT /note="T -> M (in GLUT1DS1; 75% of wild-type glucose uptake
FT activity; dbSNP:rs80359823)"
FT /evidence="ECO:0000269|PubMed:15622525,
FT ECO:0000269|PubMed:20129935"
FT /id="VAR_054763"
FT VARIANT 303
FT /note="V -> L (found in a patient with GLUT1 deficiency
FT syndrome; dbSNP:rs1205631854)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065217"
FT VARIANT 310
FT /note="T -> I (in GLUT1DS1; dbSNP:rs80359824)"
FT /evidence="ECO:0000269|PubMed:10227690"
FT /id="VAR_013285"
FT VARIANT 314
FT /note="G -> S (in GLUT1DS2; the mutation decreases glucose
FT transport but does not affect cation permeability;
FT dbSNP:rs121909739)"
FT /evidence="ECO:0000269|PubMed:18451999,
FT ECO:0000269|PubMed:20574033"
FT /id="VAR_054764"
FT VARIANT 317
FT /note="N -> T (in GLUT1DS2)"
FT /evidence="ECO:0000269|PubMed:21204808"
FT /id="VAR_065218"
FT VARIANT 324
FT /note="S -> L (in GLUT1DS2; mild phenotype; reduced
FT transporter activity; dbSNP:rs796053253)"
FT /evidence="ECO:0000269|PubMed:19798636,
FT ECO:0000269|PubMed:20574033"
FT /id="VAR_065219"
FT VARIANT 329
FT /note="E -> Q (in GLUT1DS1; stabilizes the inward-open
FT conformation)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065220"
FT VARIANT 333
FT /note="R -> Q (in GLUT1DS1 and GLUT1DS2;
FT dbSNP:rs1553155986)"
FT /evidence="ECO:0000269|PubMed:19630075,
FT ECO:0000269|PubMed:20129935"
FT /id="VAR_065221"
FT VARIANT 333
FT /note="R -> W (in GLUT1DS1; 43% of wild-type glucose uptake
FT activity; dbSNP:rs80359825)"
FT /evidence="ECO:0000269|PubMed:10980529,
FT ECO:0000269|PubMed:12325075, ECO:0000269|PubMed:15622525"
FT /id="VAR_013286"
FT VARIANT 382
FT /note="G -> D (in GLUT1DS1)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065222"
FT VARIANT 405
FT /note="A -> D (in GLUT1DS1)"
FT /evidence="ECO:0000269|PubMed:20129935"
FT /id="VAR_065223"
FT VARIANT 411
FT /note="N -> S (in EIG12; decreased glucose transport;
FT dbSNP:rs398123069)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076234"
FT VARIANT 435
FT /note="Missing (in SDCHCN; no effect on protein abundance;
FT no effect on localization to the plasma membrane; loss of
FT D-glucose transporter activity; increased cation leakage)"
FT /evidence="ECO:0000269|PubMed:21791420,
FT ECO:0000269|PubMed:22492876"
FT /id="VAR_076235"
FT VARIANT 458
FT /note="R -> W (in EIG12; decreased glucose transport;
FT dbSNP:rs13306758)"
FT /evidence="ECO:0000269|PubMed:23280796"
FT /id="VAR_076236"
FT VARIANT 468
FT /note="R -> W (in GLUT1DS1; dbSNP:rs267607059)"
FT /evidence="ECO:0000269|PubMed:20221955"
FT /id="VAR_069080"
FT VARIANT 485
FT /note="P -> L (in GLUT1DS1; creates a dileucine
FT internalization motif that promotes recruitment of clathrin
FT and mislocalization of the protein to endocytic
FT compartments)"
FT /evidence="ECO:0000269|PubMed:20129935,
FT ECO:0000269|PubMed:30197081"
FT /id="VAR_065224"
FT MUTAGEN 45
FT /note="N->T: Loss of glycosylation site."
FT /evidence="ECO:0000269|PubMed:24847886"
FT MUTAGEN 192
FT /note="I->C: Strongly decreases glucose transport."
FT /evidence="ECO:0000269|PubMed:18245775"
FT MUTAGEN 204
FT /note="L->C: Abolishes glucose transport."
FT /evidence="ECO:0000269|PubMed:18245775"
FT MUTAGEN 205
FT /note="P->C: Abolishes glucose transport."
FT /evidence="ECO:0000269|PubMed:18245775"
FT MUTAGEN 226
FT /note="S->A: Abolishes phosphorylation by PKA, leading to
FT impaired response to TPA."
FT /evidence="ECO:0000269|PubMed:25982116"
FT MUTAGEN 340
FT /note="G->C: Strongly decreases glucose transport."
FT /evidence="ECO:0000269|PubMed:19449892"
FT CONFLICT 25..26
FT /note="Missing (in Ref. 2; BAF85480)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="S -> L (in Ref. 2; BAF85480)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> F (in Ref. 1; AAA52571)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="W -> R (in Ref. 4; AAI21805)"
FT /evidence="ECO:0000305"
FT HELIX 11..31
FT /evidence="ECO:0007829|PDB:6THA"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 58..81
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 92..111
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 119..147
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:5EQG"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 266..283
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 306..327
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 333..356
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:6THA"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 400..429
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:6THA"
FT HELIX 433..450
FT /evidence="ECO:0007829|PDB:6THA"
SQ SEQUENCE 492 AA; 54084 MW; E71E1C6BD1B00B1E CRC64;
MEPSSKKLTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWVH RYGESILPTT
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVSAVLM GFSKLGKSFE
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
GNKDLWPLLL SIIFIPALLQ CIVLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTHD
LQEMKEESRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAIL MTIALALLEQ
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAIAVAGFS NWTSNFIVGM
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
ELFHPLGADS QV
