GTR2_HUMAN
ID GTR2_HUMAN Reviewed; 524 AA.
AC P11168; A8K481; B2R936; B7Z547; F8W8V8; Q9UCW9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 2 {ECO:0000305};
DE AltName: Full=Glucose transporter type 2, liver {ECO:0000303|PubMed:7593414};
DE Short=GLUT-2 {ECO:0000303|PubMed:7593414};
GN Name=SLC2A2 {ECO:0000312|HGNC:HGNC:11006};
GN Synonyms=GLUT2 {ECO:0000303|PubMed:7593414};
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT LEU-68.
RC TISSUE=Kidney, and Liver;
RX PubMed=3399500; DOI=10.1073/pnas.85.15.5434;
RA Fukumoto H., Seino S., Imura H., Sieno Y., Eddy R.L., Fukushima Y.,
RA Byers M.G., Shows T.B., Bell G.I.;
RT "Sequence, tissue distribution, and chromosomal localization of mRNA
RT encoding a human glucose transporter-like protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5434-5438(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
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].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-100 (ISOFORM 1), AND VARIANTS
RP LEU-68 AND ILE-110.
RC TISSUE=Peripheral blood;
RX PubMed=7593414; DOI=10.1210/jcem.80.11.7593414;
RA Matsubara A., Tanizawa Y., Matsutani A., Kaneko T., Kaku K.;
RT "Sequence variations of the pancreatic islet/liver glucose transporter
RT (GLUT2) gene in Japanese subjects with noninsulin dependent diabetes
RT mellitus.";
RL J. Clin. Endocrinol. Metab. 80:3131-3135(1995).
RN [6]
RP SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TRANSPORTER
RP ACTIVITY, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=8457197; DOI=10.1042/bj2900701;
RA Colville C.A., Seatter M.J., Jess T.J., Gould G.W., Thomas H.M.;
RT "Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3) glucose
RT transporters in Xenopus oocytes: substrate specificities and effects of
RT transport inhibitors.";
RL Biochem. J. 290:701-706(1993).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ILE-322.
RX PubMed=16186102; DOI=10.1074/jbc.m508678200;
RA Manolescu A., Salas-Burgos A.M., Fischbarg J., Cheeseman C.I.;
RT "Identification of a hydrophobic residue as a key determinant of fructose
RT transport by the facilitative hexose transporter SLC2A7 (GLUT7).";
RL J. Biol. Chem. 280:42978-42983(2005).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23396969; DOI=10.1074/jbc.m112.436790;
RA Corpe C.P., Eck P., Wang J., Al-Hasani H., Levine M.;
RT "Intestinal dehydroascorbic acid (DHA) transport mediated by the
RT facilitative sugar transporters, GLUT2 and GLUT8.";
RL J. Biol. Chem. 288:9092-9101(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523, 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 [10]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ILE-322.
RX PubMed=28083649; DOI=10.1007/s00232-016-9945-7;
RA Ebert K., Ludwig M., Geillinger K.E., Schoberth G.C., Essenwanger J.,
RA Stolz J., Daniel H., Witt H.;
RT "Reassessment of GLUT7 and GLUT9 as putative fructose and glucose
RT transporters.";
RL J. Membr. Biol. 250:171-182(2017).
RN [11]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=29548810; DOI=10.1016/j.bcp.2018.03.011;
RA Gauer J.S., Tumova S., Lippiat J.D., Kerimi A., Williamson G.;
RT "Differential patterns of inhibition of the sugar transporters GLUT2, GLUT5
RT and GLUT7 by flavonoids.";
RL Biochem. Pharmacol. 152:11-20(2018).
RN [12]
RP VARIANT NIDDM ILE-197, AND VARIANT ILE-110.
RX PubMed=8063045; DOI=10.1007/bf00408481;
RA Tanizawa Y., Riggs A.C., Chiu K.C., Janssen R.C., Bell D.S.H., Go R.P.C.,
RA Roseman J.M., Acton R.T., Permutt M.A.;
RT "Variability of the pancreatic islet beta cell/liver (GLUT 2) glucose
RT transporter gene in NIDDM patients.";
RL Diabetologia 37:420-427(1994).
RN [13]
RP CHARACTERIZATION OF VARIANT NIDDM ILE-197, AND CHARACTERIZATION OF VARIANT
RP ILE-110.
RX PubMed=8027028; DOI=10.1016/s0021-9258(17)32372-4;
RA Mueckler M., Kruse M., Strube M., Riggs A.C., Chiu K.C., Permutt M.A.;
RT "A mutation in the Glut2 glucose transporter gene of a diabetic patient
RT abolishes transport activity.";
RL J. Biol. Chem. 269:17765-17767(1994).
RN [14]
RP VARIANT FBS LEU-417.
RX PubMed=10987651; DOI=10.1007/s004390051095;
RA Burwinkel B., Sanjad S.A., Al-Sabban E., Al-Abbad A., Kilimann M.W.;
RT "A mutation in GLUT2, not in phosphorylase kinase subunits, in hepato-renal
RT glycogenosis with Fanconi syndrome and low phosphorylase kinase activity.";
RL Hum. Genet. 105:240-243(1999).
RN [15]
RP VARIANTS FBS PRO-389 AND GLU-423.
RX PubMed=11044475; DOI=10.1203/00006450-200011000-00005;
RA Sakamoto O., Ogawa E., Ohura T., Igarashi Y., Matsubara Y., Narisawa K.,
RA Iinuma K.;
RT "Mutation analysis of the GLUT2 gene in patients with Fanconi-Bickel
RT syndrome.";
RL Pediatr. Res. 48:586-589(2000).
CC -!- FUNCTION: Facilitative hexose transporter that mediates the transport
CC of glucose, fructose and galactose (PubMed:8027028, PubMed:16186102,
CC PubMed:23396969, PubMed:28083649, PubMed:8457197). Likely mediates the
CC bidirectional transfer of glucose across the plasma membrane of
CC hepatocytes and is responsible for uptake of glucose by the beta cells;
CC may comprise part of the glucose-sensing mechanism of the beta cell
CC (PubMed:8027028). May also participate with the Na(+)/glucose
CC cotransporter in the transcellular transport of glucose in the small
CC intestine and kidney (PubMed:3399500). Also able to mediate the
CC transport of dehydroascorbate (PubMed:23396969).
CC {ECO:0000269|PubMed:16186102, ECO:0000269|PubMed:23396969,
CC ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:3399500,
CC ECO:0000269|PubMed:8027028, ECO:0000269|PubMed:8457197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:23396969,
CC ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:29548810,
CC ECO:0000269|PubMed:8457197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:23396969,
CC ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:8457197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000269|PubMed:23396969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915,
CC ChEBI:CHEBI:4139; Evidence={ECO:0000269|PubMed:8457197};
CC -!- ACTIVITY REGULATION: D-glucose and maltose competitively inhibit
CC fructose transport (PubMed:8457197). D-glucose, D-fructose and maltose
CC inhibit deoxyglucose transport (PubMed:8457197). Glucose and fructose
CC transport are inhibited by flavonoids such as epigallocatechin gallate,
CC apigenin and quercetin (PubMed:29548810). {ECO:0000269|PubMed:29548810,
CC ECO:0000269|PubMed:8457197}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.23 mM for dehydroascorbate {ECO:0000269|PubMed:23396969};
CC KM=11.2 mM for deoxyglucose {ECO:0000269|PubMed:8457197};
CC KM=85.5 mM for D-galactose {ECO:0000269|PubMed:8457197};
CC KM=66.7 mM for D-fructose {ECO:0000269|PubMed:8457197};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28083649};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11168-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11168-2; Sequence=VSP_054835;
CC -!- TISSUE SPECIFICITY: Liver, insulin-producing beta cell, small intestine
CC and kidney. {ECO:0000269|PubMed:3399500, ECO:0000269|PubMed:8457197}.
CC -!- PTM: N-glycosylated; required for stability and retention at the cell
CC surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}.
CC -!- DISEASE: Fanconi-Bickel syndrome (FBS) [MIM:227810]: Rare, well-defined
CC clinical entity, inherited in an autosomal recessive mode and
CC characterized by hepatorenal glycogen accumulation, proximal renal
CC tubular dysfunction, and impaired utilization of glucose and galactose.
CC {ECO:0000269|PubMed:10987651, ECO:0000269|PubMed:11044475}. 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=GLUT2 entry;
CC URL="https://en.wikipedia.org/wiki/GLUT2";
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DR EMBL; J03810; AAA59514.1; -; mRNA.
DR EMBL; AK290846; BAF83535.1; -; mRNA.
DR EMBL; AK298418; BAH12783.1; -; mRNA.
DR EMBL; AK313622; BAG36383.1; -; mRNA.
DR EMBL; AC061708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78499.1; -; Genomic_DNA.
DR CCDS; CCDS3215.1; -. [P11168-1]
DR PIR; A31318; A31318.
DR RefSeq; NP_000331.1; NM_000340.1. [P11168-1]
DR RefSeq; NP_001265587.1; NM_001278658.1. [P11168-2]
DR RefSeq; NP_001265588.1; NM_001278659.1.
DR AlphaFoldDB; P11168; -.
DR SMR; P11168; -.
DR BioGRID; 112405; 11.
DR IntAct; P11168; 3.
DR STRING; 9606.ENSP00000323568; -.
DR BindingDB; P11168; -.
DR ChEMBL; CHEMBL5873; -.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR DrugBank; DB01296; Glucosamine.
DR DrugBank; DB09344; Invert sugar.
DR DrugBank; DB00428; Streptozocin.
DR TCDB; 2.A.1.1.29; the major facilitator superfamily (mfs).
DR GlyGen; P11168; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P11168; -.
DR PhosphoSitePlus; P11168; -.
DR BioMuta; SLC2A2; -.
DR DMDM; 121756; -.
DR MassIVE; P11168; -.
DR MaxQB; P11168; -.
DR PaxDb; P11168; -.
DR PeptideAtlas; P11168; -.
DR PRIDE; P11168; -.
DR ProteomicsDB; 30213; -.
DR ProteomicsDB; 52704; -. [P11168-1]
DR Antibodypedia; 4178; 552 antibodies from 42 providers.
DR DNASU; 6514; -.
DR Ensembl; ENST00000314251.8; ENSP00000323568.3; ENSG00000163581.14. [P11168-1]
DR GeneID; 6514; -.
DR KEGG; hsa:6514; -.
DR MANE-Select; ENST00000314251.8; ENSP00000323568.3; NM_000340.2; NP_000331.1.
DR UCSC; uc003fhe.2; human. [P11168-1]
DR CTD; 6514; -.
DR DisGeNET; 6514; -.
DR GeneCards; SLC2A2; -.
DR HGNC; HGNC:11006; SLC2A2.
DR HPA; ENSG00000163581; Tissue enriched (liver).
DR MalaCards; SLC2A2; -.
DR MIM; 138160; gene.
DR MIM; 227810; phenotype.
DR neXtProt; NX_P11168; -.
DR OpenTargets; ENSG00000163581; -.
DR Orphanet; 2088; Fanconi-Bickel syndrome.
DR PharmGKB; PA35876; -.
DR VEuPathDB; HostDB:ENSG00000163581; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000155708; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P11168; -.
DR OMA; PQCIPMN; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; P11168; -.
DR TreeFam; TF313762; -.
DR BioCyc; MetaCyc:ENSG00000163581-MON; -.
DR PathwayCommons; P11168; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR Reactome; R-HSA-5619098; Defective SLC2A2 causes Fanconi-Bickel syndrome (FBS).
DR Reactome; R-HSA-8981373; Intestinal hexose absorption.
DR SignaLink; P11168; -.
DR SIGNOR; P11168; -.
DR BioGRID-ORCS; 6514; 10 hits in 1070 CRISPR screens.
DR GenomeRNAi; 6514; -.
DR Pharos; P11168; Tchem.
DR PRO; PR:P11168; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P11168; protein.
DR Bgee; ENSG00000163581; Expressed in right lobe of liver and 62 other tissues.
DR ExpressionAtlas; P11168; baseline and differential.
DR Genevisible; P11168; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; IDA:UniProtKB.
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:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015757; P:galactose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002440; Glc_transpt_2.
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; PR01191; GLUCTRSPORT2.
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 Alternative splicing; Cell membrane; Disease variant; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..524
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050346"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 314..315
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 320
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 349
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 412
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 420
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..123
FT /note="MTEDKVTGTLVFTVITAVLGSFQFGYDIGVINAPQQVIISHYRHVLGVPLDD
FT RKAINNYVINSTDELPTISYSMNPKPTPWAEEETVAAAQLITMLWSLSVSSFAVGGMTA
FT SFFGGWLGDTLG -> MHLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054835"
FT VARIANT 68
FT /note="P -> L (in dbSNP:rs7637863)"
FT /evidence="ECO:0000269|PubMed:3399500,
FT ECO:0000269|PubMed:7593414"
FT /id="VAR_007169"
FT VARIANT 101
FT /note="V -> I (in dbSNP:rs1800572)"
FT /id="VAR_014718"
FT VARIANT 110
FT /note="T -> I (in dbSNP:rs5400)"
FT /evidence="ECO:0000269|PubMed:7593414,
FT ECO:0000269|PubMed:8027028, ECO:0000269|PubMed:8063045"
FT /id="VAR_014719"
FT VARIANT 197
FT /note="V -> I (in NIDDM; abolishes transport activity of
FT the transporter expressed in Xenopus oocytes;
FT dbSNP:rs121909741)"
FT /evidence="ECO:0000269|PubMed:8027028,
FT ECO:0000269|PubMed:8063045"
FT /id="VAR_018650"
FT VARIANT 389
FT /note="L -> P (in FBS; dbSNP:rs121909747)"
FT /evidence="ECO:0000269|PubMed:11044475"
FT /id="VAR_018651"
FT VARIANT 404
FT /note="I -> T (in dbSNP:rs2229608)"
FT /id="VAR_052501"
FT VARIANT 417
FT /note="P -> L (in FBS; dbSNP:rs121909744)"
FT /evidence="ECO:0000269|PubMed:10987651"
FT /id="VAR_018652"
FT VARIANT 423
FT /note="V -> E (in FBS; dbSNP:rs28928874)"
FT /evidence="ECO:0000269|PubMed:11044475"
FT /id="VAR_018653"
FT VARIANT 478
FT /note="L -> V (in dbSNP:rs5397)"
FT /id="VAR_014720"
FT MUTAGEN 322
FT /note="I->V: Reduced fructose transport."
FT /evidence="ECO:0000269|PubMed:16186102,
FT ECO:0000269|PubMed:28083649"
FT CONFLICT 183
FT /note="A -> S (in Ref. 2; BAF83535)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="V -> I (in Ref. 2; BAH12783)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="S -> N (in Ref. 2; BAF83535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57490 MW; DA600577207EC083 CRC64;
MTEDKVTGTL VFTVITAVLG SFQFGYDIGV INAPQQVIIS HYRHVLGVPL DDRKAINNYV
INSTDELPTI SYSMNPKPTP WAEEETVAAA QLITMLWSLS VSSFAVGGMT ASFFGGWLGD
TLGRIKAMLV ANILSLVGAL LMGFSKLGPS HILIIAGRSI SGLYCGLISG LVPMYIGEIA
PTALRGALGT FHQLAIVTGI LISQIIGLEF ILGNYDLWHI LLGLSGVRAI LQSLLLFFCP
ESPRYLYIKL DEEVKAKQSL KRLRGYDDVT KDINEMRKER EEASSEQKVS IIQLFTNSSY
RQPILVALML HVAQQFSGIN GIFYYSTSIF QTAGISKPVY ATIGVGAVNM VFTAVSVFLV
EKAGRRSLFL IGMSGMFVCA IFMSVGLVLL NKFSWMSYVS MIAIFLFVSF FEIGPGPIPW
FMVAEFFSQG PRPAALAIAA FSNWTCNFIV ALCFQYIADF CGPYVFFLFA GVLLAFTLFT
FFKVPETKGK SFEEIAAEFQ KKSGSAHRPK AAVEMKFLGA TETV
