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Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1) (HepG2 glucose transporter)

 GTR1_HUMAN              Reviewed;         492 AA.
P11166; A8K9S6; B2R620; D3DPX0; O75535; Q147X2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
30-AUG-2017, entry version 210.
RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1;
AltName: Full=Glucose transporter type 1, erythrocyte/brain;
Short=GLUT-1;
AltName: Full=HepG2 glucose transporter;
Name=SLC2A1; Synonyms=GLUT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
ASN-45, LACK OF GLYCOSYLATION AT ASN-411, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=3839598; DOI=10.1126/science.3839598;
Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I.,
Morris H.R., Allard W.J., Lienhard G.E., Lodish H.F.;
"Sequence and structure of a human glucose transporter.";
Science 229:941-945(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
PubMed=2834252; DOI=10.2337/diab.37.5.657;
Fukumoto H., Seino S., Imura H., Seino Y., Bell G.I.;
"Characterization and expression of human HepG2/erythrocyte glucose-
transporter gene.";
Diabetes 37:657-661(1988).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-492.
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 294-423.
TISSUE=Articular cartilage;
Neama G., Richardson S., Bell S., Carter S., Mobasheri A.;
"Molecular characterization and cloning of glucose transporters in
human articular chondrocytes.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-192; LEU-204
AND PRO-205.
PubMed=18245775; DOI=10.1074/jbc.M708896200;
Mueckler M., Makepeace C.;
"Transmembrane segment 6 of the Glut1 glucose transporter is an outer
helix and contains amino acid side chains essential for transport
activity.";
J. Biol. Chem. 283:11550-11555(2008).
[10]
IDENTIFICATION IN A COMPLEX WITH ADD2 AND DMTN, INTERACTION WITH DMTN,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18347014; DOI=10.1074/jbc.M707818200;
Khan A.A., Hanada T., Mohseni M., Jeong J.J., Zeng L., Gaetani M.,
Li D., Reed B.C., Speicher D.W., Chishti A.H.;
"Dematin and adducin provide a novel link between the spectrin
cytoskeleton and human erythrocyte membrane by directly interacting
with glucose transporter-1.";
J. Biol. Chem. 283:14600-14609(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-340.
PubMed=19449892; DOI=10.1021/bi900521n;
Mueckler M., Makepeace C.;
"Model of the exofacial substrate-binding site and helical folding of
the human Glut1 glucose transporter based on scanning mutagenesis.";
Biochemistry 48:5934-5942(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH STOM, AND
SUBUNIT.
PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
"Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1
in human erythrocyte membrane domains.";
Biochim. Biophys. Acta 1828:956-966(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND SER-490, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INTERACTION WITH SNX27.
PubMed=23563491; DOI=10.1038/ncb2721;
Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J.,
Heesom K.J., Tavare J.M., Cullen P.J.;
"A global analysis of SNX27-retromer assembly and cargo specificity
reveals a function in glucose and metal ion transport.";
Nat. Cell Biol. 15:461-471(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF VARIANT GLUT1DS1 GLN-329 IN
COMPLEX WITH NONYL-BETA-D-GLUCOSIDE, SUBCELLULAR LOCATION, TOPOLOGY,
AND MUTAGENESIS OF ASN-45.
PubMed=24847886; DOI=10.1038/nature13306;
Deng D., Xu C., Sun P., Wu J., Yan C., Hu M., Yan N.;
"Crystal structure of the human glucose transporter GLUT1.";
Nature 510:121-125(2014).
[23]
VARIANT GLUT1DS1 ILE-310.
PubMed=10227690; DOI=10.1023/A:1022544131826;
Klepper J., Wang D., Fischbarg J., Vera J.C., Jarjour I.T.,
O'Driscoll K.R., De Vivo D.C.;
"Defective glucose transport across brain tissue barriers: a newly
recognized neurological syndrome.";
Neurochem. Res. 24:587-594(1999).
[24]
VARIANTS GLUT1DS1 PHE-66; LEU-126; LYS-146; GLU-256 AND TRP-333.
PubMed=10980529;
DOI=10.1002/1098-1004(200009)16:3<224::AID-HUMU5>3.3.CO;2-G;
Wang D., Kranz-Eble P., De Vivo D.C.;
"Mutational analysis of GLUT1 (SLC2A1) in Glut-1 deficiency
syndrome.";
Hum. Mutat. 16:224-231(2000).
[25]
ERRATUM.
Wang D., Kranz-Eble P., De Vivo D.C.;
Hum. Mutat. 16:527-527(2000).
[26]
VARIANT GLUT1DS1 HIS-126.
PubMed=11603379; DOI=10.1002/ana.1222;
Brockmann K., Wang D., Korenke C.G., von Moers A., Ho Y.-Y.,
Pascual J.M., Kuang K., Yang H., Ma L., Kranz-Eble P., Fischbarg J.,
Hanefeld F., De Vivo D.C.;
"Autosomal dominant Glut-1 deficiency syndrome and familial
epilepsy.";
Ann. Neurol. 50:476-485(2001).
[27]
VARIANT GLUT1DS1 ASP-91.
PubMed=11136715; DOI=10.1093/hmg/10.1.63;
Klepper J., Willemsen M., Verrips A., Guertsen E., Herrmann R.,
Kutzick C., Floercken A., Voit T.;
"Autosomal dominant transmission of GLUT1 deficiency.";
Hum. Mol. Genet. 10:63-68(2001).
[28]
VARIANTS GLUT1DS1 CYS-126; HIS-126; LYS-146; CYS-153 AND TRP-333.
PubMed=12325075; DOI=10.1002/ana.10311;
Pascual J.M., van Heertum R.L., Wang D., Engelstad K., De Vivo D.C.;
"Imaging the metabolic footprint of Glut1 deficiency on the brain.";
Ann. Neurol. 52:458-464(2002).
[29]
VARIANT GLUT1DS2 ILE-34.
PubMed=14605501; DOI=10.1023/A:1025999914822;
Overweg-Plandsoen W.C.G., Groener J.E.M., Wang D., Onkenhout W.,
Brouwer O.F., Bakker H.D., De Vivo D.C.;
"GLUT-1 deficiency without epilepsy -- an exceptional case.";
J. Inherit. Metab. Dis. 26:559-563(2003).
[30]
VARIANTS GLUT1DS1 SER-34; HIS-126; SER-130; CYS-153; LEU-169 DEL;
MET-295 AND TRP-333, AND CHARACTERIZATION OF VARIANTS GLUT1 DEFICIENCY
SER-34; HIS-126; SER-130; CYS-153; LEU-169 DEL; MET-295 AND TRP-333.
PubMed=15622525; DOI=10.1002/ana.20331;
Wang D., Pascual J.M., Yang H., Engelstad K., Jhung S., Sun R.P.,
De Vivo D.C.;
"Glut-1 deficiency syndrome: clinical, genetic, and therapeutic
aspects.";
Ann. Neurol. 57:111-118(2005).
[31]
VARIANTS GLUT1DS2 THR-275; 282-GLN--SER-285 DEL AND SER-314.
PubMed=18451999; DOI=10.1172/JCI34438;
Weber Y.G., Storch A., Wuttke T.V., Brockmann K., Kempfle J.,
Maljevic S., Margari L., Kamm C., Schneider S.A., Huber S.M.,
Pekrun A., Roebling R., Seebohm G., Koka S., Lang C., Kraft E.,
Blazevic D., Salvo-Vargas A., Fauler M., Mottaghy F.M., Muenchau A.,
Edwards M.J., Presicci A., Margari F., Gasser T., Lang F.,
Bhatia K.P., Lehmann-Horn F., Lerche H.;
"GLUT1 mutations are a cause of paroxysmal exertion-induced
dyskinesias and induce hemolytic anemia by a cation leak.";
J. Clin. Invest. 118:2157-2168(2008).
[32]
VARIANT EIG12 PRO-223, VARIANTS GLUT1DS2 CYS-126 AND LEU-324,
CHARACTERIZATION OF VARIANT EIG12 PRO-223, AND CHARACTERIZATION OF
VARIANTS GLUT1DS2 CYS-126 AND LEU-324.
PubMed=19798636; DOI=10.1002/ana.21724;
Suls A., Mullen S.A., Weber Y.G., Verhaert K., Ceulemans B.,
Guerrini R., Wuttke T.V., Salvo-Vargas A., Deprez L., Claes L.R.,
Jordanova A., Berkovic S.F., Lerche H., De Jonghe P., Scheffer I.E.;
"Early-onset absence epilepsy caused by mutations in the glucose
transporter GLUT1.";
Ann. Neurol. 66:415-419(2009).
[33]
VARIANT GLUT1DS1 TYR-292 INS.
PubMed=19901175; DOI=10.1001/archneurol.2009.236;
Perez-Duenas B., Prior C., Ma Q., Fernandez-Alvarez E., Setoain X.,
Artuch R., Pascual J.M.;
"Childhood chorea with cerebral hypotrophy: a treatable GLUT1 energy
failure syndrome.";
Arch. Neurol. 66:1410-1414(2009).
[34]
VARIANTS GLUT1DS2 TRP-92 AND GLN-333.
PubMed=19630075; DOI=10.1002/mds.22507;
Schneider S.A., Paisan-Ruiz C., Garcia-Gorostiaga I., Quinn N.P.,
Weber Y.G., Lerche H., Hardy J., Bhatia K.P.;
"GLUT1 gene mutations cause sporadic paroxysmal exercise-induced
dyskinesias.";
Mov. Disord. 24:1684-1688(2009).
[35]
VARIANT GLUT1DS1 TRP-468.
PubMed=20221955; DOI=10.1055/s-0030-1248264;
Klepper J., Scheffer H., Elsaid M.F., Kamsteeg E.J., Leferink M.,
Ben-Omran T.;
"Autosomal recessive inheritance of GLUT1 deficiency syndrome.";
Neuropediatrics 40:207-210(2009).
[36]
VARIANTS GLUT1DS1 TYR-34; VAL-96; SER-130; VAL-155; CYS-212; HIS-212;
TRP-223; MET-295; GLN-329; GLN-333; ASP-382; ASP-405 AND LEU-485,
VARIANTS GLUT1DS2 TRP-93 AND HIS-153, AND VARIANT LEU-303.
PubMed=20129935; DOI=10.1093/brain/awp336;
Leen W.G., Klepper J., Verbeek M.M., Leferink M., Hofste T.,
van Engelen B.G., Wevers R.A., Arthur T., Bahi-Buisson N.,
Ballhausen D., Bekhof J., van Bogaert P., Carrilho I., Chabrol B.,
Champion M.P., Coldwell J., Clayton P., Donner E., Evangeliou A.,
Ebinger F., Farrell K., Forsyth R.J., de Goede C.G., Gross S.,
Grunewald S., Holthausen H., Jayawant S., Lachlan K., Laugel V.,
Leppig K., Lim M.J., Mancini G., Marina A.D., Martorell L.,
McMenamin J., Meuwissen M.E., Mundy H., Nilsson N.O., Panzer A.,
Poll-The B.T., Rauscher C., Rouselle C.M., Sandvig I., Scheffner T.,
Sheridan E., Simpson N., Sykora P., Tomlinson R., Trounce J., Webb D.,
Weschke B., Scheffer H., Willemsen M.A.;
"Glucose transporter-1 deficiency syndrome: the expanding clinical and
genetic spectrum of a treatable disorder.";
Brain 133:655-670(2010).
[37]
VARIANT GLUT1DS2 THR-317.
PubMed=21204808; DOI=10.1111/j.1528-1167.2010.02726.x;
Afawi Z., Suls A., Ekstein D., Kivity S., Neufeld M.Y., Oliver K.,
De Jonghe P., Korczyn A.D., Berkovic S.F.;
"Mild adolescent/adult onset epilepsy and paroxysmal exercise-induced
dyskinesia due to GLUT1 deficiency.";
Epilepsia 51:2466-2469(2010).
[38]
VARIANT GLUT1DS2 ILE-165.
PubMed=20621801; DOI=10.1016/j.jns.2010.05.017;
Urbizu A., Cuenca-Leon E., Raspall-Chaure M., Gratacos M., Conill J.,
Redecillas S., Roig-Quilis M., Macaya A.;
"Paroxysmal exercise-induced dyskinesia, writer's cramp, migraine with
aura and absence epilepsy in twin brothers with a novel SLC2A1
missense mutation.";
J. Neurol. Sci. 295:110-113(2010).
[39]
VARIANTS GLUT1DS2 ILE-95; PRO-223; SER-314 AND LEU-324, AND VARIANTS
GLUT1DS1 ASP-91 AND HIS-126.
PubMed=20574033; DOI=10.1212/WNL.0b013e3181eb58b4;
Mullen S.A., Suls A., De Jonghe P., Berkovic S.F., Scheffer I.E.;
"Absence epilepsies with widely variable onset are a key feature of
familial GLUT1 deficiency.";
Neurology 75:432-440(2010).
[40]
INVOLVEMENT IN SDCHCN, VARIANTS SDCHCN ASP-286 AND ILE-435 DEL, AND
CHARACTERIZATION OF VARIANTS SDCHCN ASP-286 AND ILE-435 DEL.
PubMed=21791420; DOI=10.1182/blood-2010-12-326645;
Flatt J.F., Guizouarn H., Burton N.M., Borgese F., Tomlinson R.J.,
Forsyth R.J., Baldwin S.A., Levinson B.E., Quittet P.,
Aguilar-Martinez P., Delaunay J., Stewart G.W., Bruce L.J.;
"Stomatin-deficient cryohydrocytosis results from mutations in SLC2A1:
a novel form of GLUT1 deficiency syndrome.";
Blood 118:5267-5277(2011).
[41]
VARIANT GLUT1DS2 PRO-294.
PubMed=20830593; DOI=10.1007/s00415-010-5702-5;
Anheim M., Maillart E., Vuillaumier-Barrot S., Flamand-Rouviere C.,
Pineau F., Ewenczyk C., Riant F., Apartis E., Roze E.;
"Excellent response to acetazolamide in a case of paroxysmal
dyskinesias due to GLUT1-deficiency.";
J. Neurol. 258:316-317(2011).
[42]
VARIANTS DYT9 CYS-126 AND CYS-212.
PubMed=21832227; DOI=10.1212/WNL.0b013e31822e0479;
Weber Y.G., Kamm C., Suls A., Kempfle J., Kotschet K., Schule R.,
Wuttke T.V., Maljevic S., Liebrich J., Gasser T., Ludolph A.C.,
Van Paesschen W., Schols L., De Jonghe P., Auburger G., Lerche H.;
"Paroxysmal choreoathetosis/spasticity (DYT9) is caused by a GLUT1
defect.";
Neurology 77:959-964(2011).
[43]
VARIANTS EIG12 HIS-51; MET-60; THR-77; ALA-149; SER-218; GLN-223;
VAL-243; SER-411 AND TRP-458, AND CHARACTERIZATION OF VARIANTS EIG12
MET-60; THR-77; SER-218; GLN-223; VAL-243; SER-411 AND TRP-458.
PubMed=23280796; DOI=10.1002/ana.23702;
Arsov T., Mullen S.A., Rogers S., Phillips A.M., Lawrence K.M.,
Damiano J.A., Goldberg-Stern H., Afawi Z., Kivity S., Trager C.,
Petrou S., Berkovic S.F., Scheffer I.E.;
"Glucose transporter 1 deficiency in the idiopathic generalized
epilepsies.";
Ann. Neurol. 72:807-815(2012).
[44]
INVOLVEMENT IN SDCHCN, VARIANT SDCHCN ILE-435 DEL, AND
CHARACTERIZATION OF VARIANT SDCHCN ILE-435 DEL.
PubMed=22492876; DOI=10.1210/jc.2012-1399;
Bawazir W.M., Gevers E.F., Flatt J.F., Ang A.L., Jacobs B., Oren C.,
Grunewald S., Dattani M., Bruce L.J., Stewart G.W.;
"An infant with pseudohyperkalemia, hemolysis, and seizures: cation-
leaky GLUT1-deficiency syndrome due to a SLC2A1 mutation.";
J. Clin. Endocrinol. Metab. 97:E987-E993(2012).
[45]
VARIANT EIG12 CYS-232, AND CHARACTERIZATION OF VARIANT EIG12 CYS-232.
PubMed=22282645; DOI=10.1212/WNL.0b013e318247ff54;
Striano P., Weber Y.G., Toliat M.R., Schubert J., Leu C., Chaimana R.,
Baulac S., Guerrero R., LeGuern E., Lehesjoki A.E., Polvi A.,
Robbiano A., Serratosa J.M., Guerrini R., Nurnberg P., Sander T.,
Zara F., Lerche H., Marini C.;
"GLUT1 mutations are a rare cause of familial idiopathic generalized
epilepsy.";
Neurology 78:557-562(2012).
-!- FUNCTION: Facilitative glucose transporter. This isoform may be
responsible for constitutive or basal glucose uptake. Has a very
broad substrate specificity; can transport a wide range of aldoses
including both pentoses and hexoses. {ECO:0000269|PubMed:18245775,
ECO:0000269|PubMed:19449892}.
-!- SUBUNIT: Interacts with GIPC (via PDZ domain) (By similarity).
Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via C-
terminus cytoplasmic region) with DMTN isoform 2
(PubMed:18347014). Interacts with SNX27; the interaction is
required when endocytosed to prevent degradation in lysosomes and
promote recycling to the plasma membrane (PubMed:23563491).
Interacts with STOM (PubMed:23219802). Interacts with SGTA (via
Gln-rich region) (By similarity). {ECO:0000250|UniProtKB:P11167,
ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:23219802,
ECO:0000269|PubMed:23563491}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-717153, EBI-717153;
O43889-2:CREB3; NbExp=3; IntAct=EBI-717153, EBI-625022;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Melanosome. Note=Localizes primarily at the cell surface.
Identified by mass spectrometry in melanosome fractions from stage
I to stage IV.
-!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
Expressed at variable levels in many human tissues.
{ECO:0000269|PubMed:23219802}.
-!- DISEASE: GLUT1 deficiency syndrome 1 (GLUT1DS1) [MIM:606777]: A
neurologic disorder showing wide phenotypic variability. The most
severe 'classic' phenotype comprises infantile-onset epileptic
encephalopathy associated with delayed development, acquired
microcephaly, motor incoordination, and spasticity. Onset of
seizures, usually characterized by apneic episodes, staring
spells, and episodic eye movements, occurs within the first 4
months of life. Other paroxysmal findings include intermittent
ataxia, confusion, lethargy, sleep disturbance, and headache.
Varying degrees of cognitive impairment can occur, ranging from
learning disabilities to severe mental retardation.
{ECO:0000269|PubMed:10227690, ECO:0000269|PubMed:10980529,
ECO:0000269|PubMed:11136715, ECO:0000269|PubMed:11603379,
ECO:0000269|PubMed:12325075, ECO:0000269|PubMed:15622525,
ECO:0000269|PubMed:19901175, ECO:0000269|PubMed:20129935,
ECO:0000269|PubMed:20221955, ECO:0000269|PubMed:20574033,
ECO:0000269|PubMed:24847886}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: GLUT1 deficiency syndrome 2 (GLUT1DS2) [MIM:612126]: A
clinically variable disorder characterized primarily by onset in
childhood of paroxysmal exercise-induced dyskinesia. The
dyskinesia involves transient abnormal involuntary movements, such
as dystonia and choreoathetosis, induced by exercise or exertion,
and affecting the exercised limbs. Some patients may also have
epilepsy, most commonly childhood absence epilepsy. Mild mental
retardation may also occur. In some patients involuntary exertion-
induced dystonic, choreoathetotic, and ballistic movements may be
associated with macrocytic hemolytic anemia.
{ECO:0000269|PubMed:14605501, ECO:0000269|PubMed:18451999,
ECO:0000269|PubMed:19630075, ECO:0000269|PubMed:19798636,
ECO:0000269|PubMed:20129935, ECO:0000269|PubMed:20574033,
ECO:0000269|PubMed:20621801, ECO:0000269|PubMed:20830593,
ECO:0000269|PubMed:21204808}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epilepsy, idiopathic generalized 12 (EIG12) [MIM:614847]:
A disorder characterized by recurring generalized seizures in the
absence of detectable brain lesions and/or metabolic
abnormalities. Generalized seizures arise diffusely and
simultaneously from both hemispheres of the brain. Seizure types
include juvenile myoclonic seizures, absence seizures, and
generalized tonic-clonic seizures. In some EIG12 patients seizures
may remit with age. {ECO:0000269|PubMed:19798636,
ECO:0000269|PubMed:22282645, ECO:0000269|PubMed:23280796}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Dystonia 9 (DYT9) [MIM:601042]: An autosomal dominant
neurologic disorder characterized by childhood onset of paroxysmal
choreoathetosis and progressive spastic paraplegia. Most patients
show some degree of cognitive impairment. Other variable features
may include seizures, migraine headaches, and ataxia.
{ECO:0000269|PubMed:21832227}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Stomatin-deficient cryohydrocytosis with neurologic
defects (SDCHCN) [MIM:608885]: A rare form of stomatocytosis
characterized by episodic hemolytic anemia, cold-induced red cells
cation leak, erratic hyperkalemia, neonatal hyperbilirubinemia,
hepatosplenomegaly, cataracts, seizures, mental retardation, and
movement disorder. {ECO:0000269|PubMed:21791420,
ECO:0000269|PubMed:22492876}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=GLUT1 entry;
URL="https://en.wikipedia.org/wiki/GLUT1";
-----------------------------------------------------------------------
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EMBL; K03195; AAA52571.1; -; mRNA.
EMBL; AK292791; BAF85480.1; -; mRNA.
EMBL; AK312403; BAG35317.1; -; mRNA.
EMBL; CH471059; EAX07124.1; -; Genomic_DNA.
EMBL; BC118590; AAI18591.1; -; mRNA.
EMBL; M20653; AAB61084.1; -; Genomic_DNA.
EMBL; AF070544; AAC28635.1; -; mRNA.
EMBL; AY034633; AAK56795.1; -; mRNA.
CCDS; CCDS477.1; -.
PIR; A27217; A27217.
RefSeq; NP_006507.2; NM_006516.2.
UniGene; Hs.473721; -.
PDB; 1SUK; Model; -; A=1-492.
PDB; 4PYP; X-ray; 3.17 A; A=1-492.
PDB; 5EQG; X-ray; 2.90 A; A=1-492.
PDB; 5EQH; X-ray; 2.99 A; A=1-492.
PDB; 5EQI; X-ray; 3.00 A; A=1-492.
PDBsum; 1SUK; -.
PDBsum; 4PYP; -.
PDBsum; 5EQG; -.
PDBsum; 5EQH; -.
PDBsum; 5EQI; -.
ProteinModelPortal; P11166; -.
SMR; P11166; -.
BioGrid; 112404; 29.
DIP; DIP-23N; -.
IntAct; P11166; 26.
MINT; MINT-1386229; -.
STRING; 9606.ENSP00000416293; -.
BindingDB; P11166; -.
ChEMBL; CHEMBL2535; -.
DrugBank; DB08831; 2-deoxyglucose.
DrugBank; DB08830; Dehydroascorbic Acid.
DrugBank; DB00292; Etomidate.
DrugBank; DB09502; Fludeoxyglucose F-18.
GuidetoPHARMACOLOGY; 875; -.
TCDB; 2.A.1.1.28; the major facilitator superfamily (mfs).
iPTMnet; P11166; -.
PhosphoSitePlus; P11166; -.
SwissPalm; P11166; -.
UniCarbKB; P11166; -.
BioMuta; SLC2A1; -.
DMDM; 115502394; -.
EPD; P11166; -.
MaxQB; P11166; -.
PaxDb; P11166; -.
PeptideAtlas; P11166; -.
PRIDE; P11166; -.
Ensembl; ENST00000426263; ENSP00000416293; ENSG00000117394.
GeneID; 6513; -.
KEGG; hsa:6513; -.
UCSC; uc001cik.3; human.
CTD; 6513; -.
DisGeNET; 6513; -.
GeneCards; SLC2A1; -.
GeneReviews; SLC2A1; -.
HGNC; HGNC:11005; SLC2A1.
HPA; CAB002759; -.
HPA; HPA031345; -.
HPA; HPA058494; -.
MalaCards; SLC2A1; -.
MIM; 138140; gene.
MIM; 601042; phenotype.
MIM; 606777; phenotype.
MIM; 608885; phenotype.
MIM; 612126; phenotype.
MIM; 614847; phenotype.
neXtProt; NX_P11166; -.
OpenTargets; ENSG00000117394; -.
Orphanet; 64280; Childhood absence epilepsy.
Orphanet; 71277; Encephalopathy due to GLUT1 deficiency.
Orphanet; 168577; Hereditary cryohydrocytosis with reduced stomatin.
Orphanet; 53583; Paroxysmal dystonic choreathetosis with episodic ataxia and spasticity.
Orphanet; 98811; Paroxysmal exertion-induced dyskinesia.
PharmGKB; PA35875; -.
eggNOG; KOG0569; Eukaryota.
eggNOG; COG0477; LUCA.
GeneTree; ENSGT00760000119022; -.
HOVERGEN; HBG014816; -.
InParanoid; P11166; -.
KO; K07299; -.
OMA; LQCIVLP; -.
OrthoDB; EOG091G0A9K; -.
PhylomeDB; P11166; -.
TreeFam; TF313762; -.
Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-428790; Facilitative Na+-independent glucose transporters.
Reactome; R-HSA-5653890; Lactose synthesis.
Reactome; R-HSA-70153; Glucose transport.
SIGNOR; P11166; -.
ChiTaRS; SLC2A1; human.
GeneWiki; GLUT1; -.
GenomeRNAi; 6513; -.
PRO; PR:P11166; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117394; -.
CleanEx; HS_SLC2A1; -.
ExpressionAtlas; P11166; baseline and differential.
Genevisible; P11166; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0055056; F:D-glucose transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0033300; F:dehydroascorbic acid transporter activity; EXP:Reactome.
GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0042910; F:xenobiotic transporter activity; IEA:Ensembl.
GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:1904659; P:glucose transmembrane transport; IMP:UniProtKB.
GO; GO:0015758; P:glucose transport; IDA:UniProtKB.
GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
GO; GO:0005989; P:lactose biosynthetic process; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
CDD; cd06174; MFS; 1.
InterPro; IPR002439; Glu_transpt_1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR003663; Sugar/inositol_transpt.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF00083; Sugar_tr; 1.
PRINTS; PR01190; GLUCTRSPORT1.
PRINTS; PR00171; SUGRTRNSPORT.
SUPFAM; SSF103473; SSF103473; 2.
TIGRFAMs; TIGR00879; SP; 1.
PROSITE; PS50850; MFS; 1.
PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cataract; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Dystonia; Epilepsy;
Glycoprotein; Hereditary hemolytic anemia; Membrane;
Mental retardation; Phosphoprotein; Reference proteome;
Sugar transport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 492 Solute carrier family 2, facilitated
glucose transporter member 1.
/FTId=PRO_0000050338.
TOPO_DOM 1 11 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 12 33 Helical; Name=1.
TOPO_DOM 34 66 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 67 87 Helical; Name=2.
TOPO_DOM 88 90 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 91 112 Helical; Name=3.
TOPO_DOM 113 120 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 121 144 Helical; Name=4.
TOPO_DOM 145 155 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 156 176 Helical; Name=5.
TOPO_DOM 177 185 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 186 206 Helical; Name=6.
TOPO_DOM 207 271 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 272 293 Helical; Name=7.
TOPO_DOM 294 306 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 307 328 Helical; Name=8.
TOPO_DOM 329 334 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 335 355 Helical; Name=9.
TOPO_DOM 356 365 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 366 388 Helical; Name=10.
TOPO_DOM 389 401 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 402 422 Helical; Name=11.
TOPO_DOM 423 429 Extracellular.
{ECO:0000269|PubMed:24847886}.
TRANSMEM 430 450 Helical; Name=12.
TOPO_DOM 451 492 Cytoplasmic.
{ECO:0000269|PubMed:24847886}.
REGION 282 288 Monosaccharide binding.
BINDING 317 317 Monosaccharide.
BINDING 388 388 Monosaccharide.
SITE 411 411 Not glycosylated.
{ECO:0000269|PubMed:3839598}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 478 478 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:3839598}.
VARIANT 34 34 N -> I (in GLUT1DS2; dbSNP:rs80359812).
{ECO:0000269|PubMed:14605501}.
/FTId=VAR_054755.
VARIANT 34 34 N -> S (in GLUT1DS1; 55% of wild-type
glucose uptake activity).
{ECO:0000269|PubMed:15622525}.
/FTId=VAR_054756.
VARIANT 34 34 N -> Y (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065206.
VARIANT 51 51 R -> H (in EIG12; unknown pathological
significance; dbSNP:rs201815571).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076226.
VARIANT 60 60 T -> M (in EIG12; unknown pathological
significance; decreased glucose
transport; dbSNP:rs142986731).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076227.
VARIANT 66 66 S -> F (in GLUT1DS1; dbSNP:rs80359813).
{ECO:0000269|PubMed:10980529}.
/FTId=VAR_013283.
VARIANT 77 77 M -> T (in EIG12; decreased glucose
transport).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076228.
VARIANT 91 91 G -> D (in GLUT1DS1; significantly
decreases the transport of 3-O-methyl-D-
glucose; dbSNP:rs80359814).
{ECO:0000269|PubMed:11136715,
ECO:0000269|PubMed:20574033}.
/FTId=VAR_013182.
VARIANT 92 92 R -> W (in GLUT1DS2; dbSNP:rs202060209).
{ECO:0000269|PubMed:19630075}.
/FTId=VAR_069077.
VARIANT 93 93 R -> W (in GLUT1DS2; dbSNP:rs267607061).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065207.
VARIANT 95 95 S -> I (in GLUT1DS2; dbSNP:rs267607060).
{ECO:0000269|PubMed:20574033}.
/FTId=VAR_065208.
VARIANT 96 96 M -> V (in GLUT1DS1; dbSNP:rs753161833).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065209.
VARIANT 126 126 R -> C (in GLUT1DS1, GLUT1DS2 and DYT9;
reduced transporter activity;
dbSNP:rs80359818).
{ECO:0000269|PubMed:12325075,
ECO:0000269|PubMed:19798636,
ECO:0000269|PubMed:21832227}.
/FTId=VAR_054757.
VARIANT 126 126 R -> H (in GLUT1DS1; significantly
decreases the transport of 3-O-methyl-D-
glucose and dehydroascorbic acid; 57% of
wild-type glucose uptake activity;
dbSNP:rs80359816).
{ECO:0000269|PubMed:11603379,
ECO:0000269|PubMed:12325075,
ECO:0000269|PubMed:15622525,
ECO:0000269|PubMed:20574033}.
/FTId=VAR_013183.
VARIANT 126 126 R -> L (in GLUT1DS1; compound
heterozygote with V-256;
dbSNP:rs80359816).
{ECO:0000269|PubMed:10980529}.
/FTId=VAR_013184.
VARIANT 130 130 G -> S (in GLUT1DS1; 75% of wild-type
glucose uptake activity;
dbSNP:rs80359819).
{ECO:0000269|PubMed:15622525,
ECO:0000269|PubMed:20129935}.
/FTId=VAR_054758.
VARIANT 146 146 E -> K (in GLUT1DS1; dbSNP:rs80359820).
{ECO:0000269|PubMed:10980529,
ECO:0000269|PubMed:12325075}.
/FTId=VAR_013284.
VARIANT 149 149 P -> A (in EIG12; unknown pathological
significance).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076229.
VARIANT 153 153 R -> C (in GLUT1DS1; 44% of wild-type
glucose uptake activity).
{ECO:0000269|PubMed:12325075,
ECO:0000269|PubMed:15622525}.
/FTId=VAR_054759.
VARIANT 153 153 R -> H (in GLUT1DS2; dbSNP:rs794727642).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065210.
VARIANT 155 155 A -> V (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065211.
VARIANT 165 165 V -> I (in GLUT1DS2).
{ECO:0000269|PubMed:20621801}.
/FTId=VAR_065212.
VARIANT 169 169 Missing (in GLUT1DS1; 48% of wild-type
glucose uptake activity).
{ECO:0000269|PubMed:15622525}.
/FTId=VAR_054760.
VARIANT 212 212 R -> C (in GLUT1DS1 and DYT9;
dbSNP:rs387907312).
{ECO:0000269|PubMed:20129935,
ECO:0000269|PubMed:21832227}.
/FTId=VAR_065213.
VARIANT 212 212 R -> H (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065214.
VARIANT 218 218 R -> S (in EIG12; decreased glucose
transport).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076230.
VARIANT 223 223 R -> P (in EIG12; mild phenotype; reduced
transporter activity; dbSNP:rs397514564).
{ECO:0000269|PubMed:19798636,
ECO:0000269|PubMed:20574033}.
/FTId=VAR_065215.
VARIANT 223 223 R -> Q (in EIG12; unknown pathological
significance; no effect on glucose
transport; dbSNP:rs397514564).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076231.
VARIANT 223 223 R -> W (in GLUT1DS1; dbSNP:rs796053248).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065216.
VARIANT 232 232 R -> C (in EIG12; the mutant protein is
expressed at the cell surface but has
mildly decreased glucose uptake (70%)
compared to wild-type;
dbSNP:rs387907313).
{ECO:0000269|PubMed:22282645}.
/FTId=VAR_069078.
VARIANT 243 243 E -> V (in EIG12; decreased glucose
transport).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076232.
VARIANT 256 256 K -> E (in GLUT1DS1; compound
heterozygote with L-126;
dbSNP:rs121909738).
{ECO:0000269|PubMed:10980529}.
/FTId=VAR_013185.
VARIANT 275 275 A -> T (in GLUT1DS2; the mutation
decreases glucose transport but does not
affect cation permeability;
dbSNP:rs121909740).
{ECO:0000269|PubMed:18451999}.
/FTId=VAR_054761.
VARIANT 282 285 Missing (in GLUT1DS2; accompanied by
hemolytic anemia and altered erythrocyte
ion concentrations; the mutation
decreases glucose transport and causes a
cation leak that alteres intracellular
concentrations of sodium potassium and
calcium). {ECO:0000269|PubMed:18451999}.
/FTId=VAR_054762.
VARIANT 286 286 G -> D (in SDCHCN; no effect on protein
abundance; no effect on localization to
the plasma membrane; loss of D-glucose
transporter activity; increased cation
leakage; dbSNP:rs864309514).
{ECO:0000269|PubMed:21791420,
ECO:0000269|PubMed:22492876}.
/FTId=VAR_076233.
VARIANT 292 292 Y -> YY (in GLUT1DS1).
{ECO:0000269|PubMed:19901175}.
/FTId=VAR_069079.
VARIANT 294 294 S -> P (in GLUT1DS2).
{ECO:0000269|PubMed:20830593}.
/FTId=VAR_065784.
VARIANT 295 295 T -> M (in GLUT1DS1; 75% of wild-type
glucose uptake activity;
dbSNP:rs80359823).
{ECO:0000269|PubMed:15622525,
ECO:0000269|PubMed:20129935}.
/FTId=VAR_054763.
VARIANT 303 303 V -> L (found in a patient with GLUT1
deficiency syndrome).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065217.
VARIANT 310 310 T -> I (in GLUT1DS1; dbSNP:rs80359824).
{ECO:0000269|PubMed:10227690}.
/FTId=VAR_013285.
VARIANT 314 314 G -> S (in GLUT1DS2; the mutation
decreases glucose transport but does not
affect cation permeability;
dbSNP:rs121909739).
{ECO:0000269|PubMed:18451999,
ECO:0000269|PubMed:20574033}.
/FTId=VAR_054764.
VARIANT 317 317 N -> T (in GLUT1DS2).
{ECO:0000269|PubMed:21204808}.
/FTId=VAR_065218.
VARIANT 324 324 S -> L (in GLUT1DS2; mild phenotype;
reduced transporter activity;
dbSNP:rs796053253).
{ECO:0000269|PubMed:19798636,
ECO:0000269|PubMed:20574033}.
/FTId=VAR_065219.
VARIANT 329 329 E -> Q (in GLUT1DS1; stabilizes the
inward-open conformation).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065220.
VARIANT 333 333 R -> Q (in GLUT1DS1 and GLUT1DS2).
{ECO:0000269|PubMed:19630075,
ECO:0000269|PubMed:20129935}.
/FTId=VAR_065221.
VARIANT 333 333 R -> W (in GLUT1DS1; 43% of wild-type
glucose uptake activity;
dbSNP:rs80359825).
{ECO:0000269|PubMed:10980529,
ECO:0000269|PubMed:12325075,
ECO:0000269|PubMed:15622525}.
/FTId=VAR_013286.
VARIANT 382 382 G -> D (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065222.
VARIANT 405 405 A -> D (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065223.
VARIANT 411 411 N -> S (in EIG12; decreased glucose
transport; dbSNP:rs398123069).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076234.
VARIANT 435 435 Missing (in SDCHCN; no effect on protein
abundance; no effect on localization to
the plasma membrane; loss of D-glucose
transporter activity; increased cation
leakage). {ECO:0000269|PubMed:21791420,
ECO:0000269|PubMed:22492876}.
/FTId=VAR_076235.
VARIANT 458 458 R -> W (in EIG12; decreased glucose
transport; dbSNP:rs13306758).
{ECO:0000269|PubMed:23280796}.
/FTId=VAR_076236.
VARIANT 468 468 R -> W (in GLUT1DS1; dbSNP:rs267607059).
{ECO:0000269|PubMed:20221955}.
/FTId=VAR_069080.
VARIANT 485 485 P -> L (in GLUT1DS1).
{ECO:0000269|PubMed:20129935}.
/FTId=VAR_065224.
MUTAGEN 45 45 N->T: Loss of glycosylation site.
{ECO:0000269|PubMed:24847886}.
MUTAGEN 192 192 I->C: Strongly decreases glucose
transport. {ECO:0000269|PubMed:18245775}.
MUTAGEN 204 204 L->C: Abolishes glucose transport.
{ECO:0000269|PubMed:18245775}.
MUTAGEN 205 205 P->C: Abolishes glucose transport.
{ECO:0000269|PubMed:18245775}.
MUTAGEN 340 340 G->C: Strongly decreases glucose
transport. {ECO:0000269|PubMed:19449892}.
CONFLICT 25 26 Missing (in Ref. 2; BAF85480).
{ECO:0000305}.
CONFLICT 95 95 S -> L (in Ref. 2; BAF85480).
{ECO:0000305}.
CONFLICT 152 152 L -> F (in Ref. 1; AAA52571).
{ECO:0000305}.
HELIX 11 30 {ECO:0000244|PDB:5EQG}.
HELIX 37 52 {ECO:0000244|PDB:5EQG}.
HELIX 58 90 {ECO:0000244|PDB:5EQG}.
HELIX 92 98 {ECO:0000244|PDB:5EQG}.
HELIX 100 111 {ECO:0000244|PDB:5EQG}.
TURN 112 117 {ECO:0000244|PDB:5EQG}.
HELIX 119 145 {ECO:0000244|PDB:5EQG}.
TURN 150 152 {ECO:0000244|PDB:5EQG}.
HELIX 153 156 {ECO:0000244|PDB:5EQG}.
HELIX 159 174 {ECO:0000244|PDB:5EQG}.
TURN 177 180 {ECO:0000244|PDB:5EQG}.
TURN 183 185 {ECO:0000244|PDB:5EQG}.
HELIX 186 191 {ECO:0000244|PDB:5EQG}.
HELIX 194 203 {ECO:0000244|PDB:5EQG}.
HELIX 204 206 {ECO:0000244|PDB:5EQG}.
HELIX 211 215 {ECO:0000244|PDB:5EQG}.
TURN 216 218 {ECO:0000244|PDB:5EQG}.
HELIX 221 232 {ECO:0000244|PDB:5EQG}.
HELIX 238 253 {ECO:0000244|PDB:5EQG}.
HELIX 259 264 {ECO:0000244|PDB:5EQG}.
TURN 266 268 {ECO:0000244|PDB:5EQG}.
HELIX 269 283 {ECO:0000244|PDB:5EQG}.
TURN 284 286 {ECO:0000244|PDB:5EQG}.
HELIX 288 301 {ECO:0000244|PDB:5EQG}.
HELIX 306 328 {ECO:0000244|PDB:5EQG}.
HELIX 333 356 {ECO:0000244|PDB:5EQG}.
TURN 357 360 {ECO:0000244|PDB:5EQG}.
HELIX 364 379 {ECO:0000244|PDB:5EQG}.
TURN 380 385 {ECO:0000244|PDB:5EQG}.
HELIX 386 394 {ECO:0000244|PDB:5EQG}.
TURN 397 399 {ECO:0000244|PDB:5EQG}.
HELIX 400 429 {ECO:0000244|PDB:5EQG}.
HELIX 430 432 {ECO:0000244|PDB:5EQG}.
HELIX 433 451 {ECO:0000244|PDB:5EQG}.
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


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