GTR3_HUMAN
ID GTR3_HUMAN Reviewed; 496 AA.
AC P11169; B2R606; D3DUU6; Q6I9U2; Q9UG15;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3 {ECO:0000305};
DE AltName: Full=Glucose transporter type 3, brain {ECO:0000303|PubMed:9477959};
DE Short=GLUT-3 {ECO:0000303|PubMed:9477959};
GN Name=SLC2A3 {ECO:0000312|HGNC:HGNC:11007};
GN Synonyms=GLUT3 {ECO:0000303|PubMed:9477959};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal skeletal muscle;
RX PubMed=3170580; DOI=10.1016/s0021-9258(19)37577-5;
RA Kayano T., Fukumoto H., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B.,
RA Bell G.I.;
RT "Evidence for a family of human glucose transporter-like proteins. Sequence
RT and gene localization of a protein expressed in fetal skeletal muscle and
RT other tissues.";
RL J. Biol. Chem. 263:15245-15248(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stuart C.A., Wen K.G., Acosta M., Wood T.G.;
RT "Resistance and expression of glucose transporters in human skeletal
RT muscle.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-453.
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 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 [9]
RP SUBSTRATE SPECIFICITY, REGION, FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 277-GLN--SER-279, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=9477959; DOI=10.1021/bi972322u;
RA Seatter M.J., de la Rue S.A., Porter L.M., Gould G.W.;
RT "QLS motif in transmembrane helix VII of the glucose transporter family
RT interacts with the C-1 (position) of D-glucose and is involved in substrate
RT selection at the exofacial binding site.";
RL Biochemistry 37:1322-1326(1998).
RN [10] {ECO:0007744|PDB:4ZW9, ECO:0007744|PDB:4ZWB, ECO:0007744|PDB:4ZWC}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH D-GLUCOSE,
RP SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, TRANSPORTER ACTIVITY, AND DOMAIN.
RX PubMed=26176916; DOI=10.1038/nature14655;
RA Deng D., Sun P., Yan C., Ke M., Jiang X., Xiong L., Ren W., Hirata K.,
RA Yamamoto M., Fan S., Yan N.;
RT "Molecular basis of ligand recognition and transport by glucose
RT transporters.";
RL Nature 526:391-396(2015).
CC -!- FUNCTION: Facilitative glucose transporter that can also mediate the
CC uptake of various other monosaccharides across the cell membrane
CC (PubMed:9477959, PubMed:26176916). Mediates the uptake of glucose, 2-
CC deoxyglucose, galactose, mannose, xylose and fucose, and probably also
CC dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate
CC fructose transport (PubMed:9477959, PubMed:26176916).
CC {ECO:0000269|PubMed:26176916, ECO:0000269|PubMed:8457197,
CC ECO:0000269|PubMed:9477959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:26176916,
CC ECO:0000269|PubMed:8457197, ECO:0000269|PubMed:9477959};
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: Deoxyglucose transport is inhibit by D-glucose, D-
CC galactose and maltose (PubMed:8457197). Galactose transport is
CC inhibited by D-glucose and maltose (PubMed:8457197).
CC {ECO:0000269|PubMed:8457197}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for deoxyglucose {ECO:0000269|PubMed:8457197,
CC ECO:0000269|PubMed:9477959};
CC KM=8.5 mM for D-galactose {ECO:0000269|PubMed:8457197};
CC -!- INTERACTION:
CC P11169; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-725116, EBI-6942903;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9477959,
CC ECO:0000305|PubMed:26176916}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26176916}. Perikaryon
CC {ECO:0000250|UniProtKB:Q07647}. Cell projection
CC {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced
CC patches along neuronal processes. {ECO:0000250|UniProtKB:Q07647}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:8457197).
CC Expressed in many tissues. {ECO:0000269|PubMed:3170580,
CC ECO:0000269|PubMed:8457197}.
CC -!- DOMAIN: Transport is mediated via a series of conformation changes,
CC switching between a conformation where the substrate-binding cavity is
CC accessible from the outside, and a another conformation where it is
CC accessible from the cytoplasm. {ECO:0000305|PubMed:26176916}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; M20681; AAB61083.1; -; mRNA.
DR EMBL; AF274892; AAF82116.1; -; Genomic_DNA.
DR EMBL; AF274889; AAF82116.1; JOINED; Genomic_DNA.
DR EMBL; AF274890; AAF82116.1; JOINED; Genomic_DNA.
DR EMBL; AF274891; AAF82116.1; JOINED; Genomic_DNA.
DR EMBL; CR457413; CAG33694.1; -; mRNA.
DR EMBL; AK312386; BAG35303.1; -; mRNA.
DR EMBL; CH471116; EAW88644.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88645.1; -; Genomic_DNA.
DR EMBL; BC039196; AAH39196.1; -; mRNA.
DR EMBL; AY034634; AAK56796.1; -; mRNA.
DR CCDS; CCDS8586.1; -.
DR PIR; A31986; A31986.
DR PIR; T14798; T14798.
DR RefSeq; NP_008862.1; NM_006931.2.
DR PDB; 4ZW9; X-ray; 1.50 A; A=1-496.
DR PDB; 4ZWB; X-ray; 2.40 A; A=1-496.
DR PDB; 4ZWC; X-ray; 2.60 A; A/B=1-496.
DR PDB; 5C65; X-ray; 2.65 A; A/B=1-474.
DR PDB; 7CRZ; X-ray; 2.30 A; A=1-496.
DR PDBsum; 4ZW9; -.
DR PDBsum; 4ZWB; -.
DR PDBsum; 4ZWC; -.
DR PDBsum; 5C65; -.
DR PDBsum; 7CRZ; -.
DR AlphaFoldDB; P11169; -.
DR SMR; P11169; -.
DR BioGRID; 112406; 21.
DR IntAct; P11169; 13.
DR MINT; P11169; -.
DR STRING; 9606.ENSP00000075120; -.
DR BindingDB; P11169; -.
DR ChEMBL; CHEMBL5215; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR DrugBank; DB01296; Glucosamine.
DR TCDB; 2.A.1.1.91; the major facilitator superfamily (mfs).
DR GlyGen; P11169; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P11169; -.
DR PhosphoSitePlus; P11169; -.
DR SwissPalm; P11169; -.
DR BioMuta; SLC2A3; -.
DR DMDM; 121760; -.
DR EPD; P11169; -.
DR jPOST; P11169; -.
DR MassIVE; P11169; -.
DR MaxQB; P11169; -.
DR PaxDb; P11169; -.
DR PeptideAtlas; P11169; -.
DR PRIDE; P11169; -.
DR ProteomicsDB; 52705; -.
DR Antibodypedia; 1472; 354 antibodies from 39 providers.
DR DNASU; 6515; -.
DR Ensembl; ENST00000075120.12; ENSP00000075120.7; ENSG00000059804.16.
DR GeneID; 6515; -.
DR KEGG; hsa:6515; -.
DR MANE-Select; ENST00000075120.12; ENSP00000075120.7; NM_006931.3; NP_008862.1.
DR UCSC; uc001qtr.4; human.
DR CTD; 6515; -.
DR DisGeNET; 6515; -.
DR GeneCards; SLC2A3; -.
DR HGNC; HGNC:11007; SLC2A3.
DR HPA; ENSG00000059804; Tissue enhanced (bone).
DR MalaCards; SLC2A3; -.
DR MIM; 138170; gene.
DR neXtProt; NX_P11169; -.
DR OpenTargets; ENSG00000059804; -.
DR Orphanet; 399; Huntington disease.
DR PharmGKB; PA35877; -.
DR VEuPathDB; HostDB:ENSG00000059804; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000162491; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P11169; -.
DR OMA; WIDFALF; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P11169; -.
DR TreeFam; TF313762; -.
DR PathwayCommons; P11169; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR SignaLink; P11169; -.
DR SIGNOR; P11169; -.
DR BioGRID-ORCS; 6515; 16 hits in 1007 CRISPR screens.
DR ChiTaRS; SLC2A3; human.
DR GenomeRNAi; 6515; -.
DR Pharos; P11169; Tchem.
DR PRO; PR:P11169; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P11169; protein.
DR Bgee; ENSG00000059804; Expressed in endothelial cell and 196 other tissues.
DR ExpressionAtlas; P11169; baseline and differential.
DR Genevisible; P11169; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; 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; NAS:ProtInc.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central.
DR GO; GO:0015757; P:galactose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:0098708; P:glucose import across plasma membrane; IGI: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:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; IGI:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002945; Glc_transpt_3.
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; PR01192; GLUCTRSPORT3.
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; Cell membrane; Cell projection; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..496
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 3"
FT /id="PRO_0000050353"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 33..64
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 86..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 112..118
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 143..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 175..183
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 205..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 291..304
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..325
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 326..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..352
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 353..363
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 364..389
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 390..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 400..420
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 421..429
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26176916"
FT TOPO_DOM 451..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 277..279
FT /note="Important for selectivity against fructose"
FT /evidence="ECO:0000269|PubMed:26176916"
FT BINDING 159
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT BINDING 280..281
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT BINDING 286
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT BINDING 315
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT BINDING 378
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT BINDING 386
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:26176916,
FT ECO:0007744|PDB:4ZW9"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32037"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32037"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 85
FT /note="V -> L (in dbSNP:rs17728193)"
FT /id="VAR_052502"
FT MUTAGEN 277..279
FT /note="QLS->HVA: Confers moderate fructose transport
FT activity."
FT /evidence="ECO:0000269|PubMed:26176916"
FT HELIX 8..29
FT /evidence="ECO:0007829|PDB:4ZW9"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4ZWC"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:4ZW9"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5C65"
FT HELIX 56..79
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 111..115
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 117..145
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 151..173
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 304..355
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 362..379
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:4ZW9"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 398..427
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 431..449
FT /evidence="ECO:0007829|PDB:4ZW9"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:4ZW9"
SQ SEQUENCE 496 AA; 53924 MW; F601CD6892F16516 CRC64;
MGTQKVTPAL IFAITVATIG SFQFGYNTGV INAPEKIIKE FINKTLTDKG NAPPSEVLLT
SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLIVNLL AVTGGCFMGL CKVAKSVEML
ILGRLVIGLF CGLCTGFVPM YIGEISPTAL RGAFGTLNQL GIVVGILVAQ IFGLEFILGS
EELWPLLLGF TILPAILQSA ALPFCPESPR FLLINRKEEE NAKQILQRLW GTQDVSQDIQ
EMKDESARMS QEKQVTVLEL FRVSSYRQPI IISIVLQLSQ QLSGINAVFY YSTGIFKDAG
VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAFCSTLMT VSLLLKDNYN
GMSFVCIGAI LVFVAFFEIG PGPIPWFIVA ELFSQGPRPA AMAVAGCSNW TSNFLVGLLF
PSAAHYLGAY VFIIFTGFLI TFLAFTFFKV PETRGRTFED ITRAFEGQAH GADRSGKDGV
MEMNSIEPAK ETTTNV
