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   27-MAR-2024, entry version 219.
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]
RP   INTERACTION WITH SMIM43.
RX   PubMed=35810171; DOI=10.1038/s41467-022-31762-x;
RA   Fu H., Wang T., Kong X., Yan K., Yang Y., Cao J., Yuan Y., Wang N., Kee K.,
RA   Lu Z.J., Xi Q.;
RT   "A Nodal enhanced micropeptide NEMEP regulates glucose uptake during
RT   mesendoderm differentiation of embryonic stem cells.";
RL   Nat. Commun. 13:3984-3984(2022).
RN   [11] {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 (PubMed:9477959,
CC       PubMed:26176916). Can also mediate the uptake of various other
CC       monosaccharides across the cell membrane (PubMed:9477959,
CC       PubMed:26176916). Mediates the uptake of glucose, 2-deoxyglucose,
CC       galactose, mannose, xylose and fucose, and probably also
CC       dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate
CC       fructose transport (PubMed:9477959, PubMed:26176916). Required for
CC       mesendoderm differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:P32037, ECO:0000269|PubMed:26176916,
CC       ECO:0000269|PubMed:8457197, 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   -!- SUBUNIT: Interacts with SMIM43; the interaction may promote SLC2A3-
CC       mediated glucose transport to meet the energy needs of mesendoderm
CC       differentiation. {ECO:0000269|PubMed:35810171}.
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   PDB; 7SPS; X-ray; 2.30 A; A/B=1-496.
DR   PDB; 7SPT; X-ray; 2.10 A; A=1-496.
DR   PDBsum; 4ZW9; -.
DR   PDBsum; 4ZWB; -.
DR   PDBsum; 4ZWC; -.
DR   PDBsum; 5C65; -.
DR   PDBsum; 7CRZ; -.
DR   PDBsum; 7SPS; -.
DR   PDBsum; 7SPT; -.
DR   AlphaFoldDB; P11169; -.
DR   SMR; P11169; -.
DR   BioGRID; 112406; 26.
DR   IntAct; P11169; 14.
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   GlyCosmos; P11169; 1 site, No reported glycans.
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; 9606-ENSP00000075120; -.
DR   PeptideAtlas; P11169; -.
DR   ProteomicsDB; 52705; -.
DR   Pumba; P11169; -.
DR   Antibodypedia; 1472; 406 antibodies from 39 providers.
DR   DNASU; 6515; -.
DR   Ensembl; ENST00000075120.12; ENSP00000075120.7; ENSG00000059804.17.
DR   Ensembl; ENST00000707174.1; ENSP00000516774.1; ENSG00000059804.17.
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   AGR; HGNC:11007; -.
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; QIGCINA; -.
DR   OrthoDB; 1899001at2759; -.
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 1070 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 198 other cell types or tissues.
DR   ExpressionAtlas; P11169; baseline and differential.
DR   GO; GO:0016235; C:aggresome; IDA:HPA.
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:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
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: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:0150104; P:transport across blood-brain barrier; IGI:ARUK-UCL.
DR   CDD; cd17431; MFS_GLUT_Class1; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1.
DR   PANTHER; PTHR23503:SF99; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 3; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR01192; GLUCTRSPORT3.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
DR   Genevisible; P11169; HS.
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
//