ID GTR3_MOUSE Reviewed; 493 AA. AC P32037; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 13-SEP-2023, entry version 185. 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:1730609}; DE Short=GLUT-3 {ECO:0000303|PubMed:1730609}; GN Name=Slc2a3 {ECO:0000312|MGI:MGI:95757}; GN Synonyms=Glut3 {ECO:0000303|PubMed:1730609}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Brain; RX PubMed=1730609; DOI=10.1016/s0021-9258(18)48518-3; RA Nagamatsu S., Kornhauser J.M., Seino S., Mayo K.E., Steiner D.F., RA Bell G.I.; RT "Glucose transporter expression in brain. cDNA sequence of mouse GLUT3, the RT brain facilitative glucose transporter isoform, and identification of sites RT of expression by in situ hybridization."; RL J. Biol. Chem. 267:467-472(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Takeda J., Minokoshi Y., Yasuda K., Kayano T., Graeme B.I.; RT "Evolution of facilitative sugar transporter gene family: Characterization RT of mouse GLUT3 and human GLUT5 genes."; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; 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 [4] RP PROTEIN SEQUENCE OF 218-228, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232 AND SER-471, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Facilitative glucose transporter that can also mediate the CC uptake of various other monosaccharides across the cell membrane. CC Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, CC xylose and fucose, and probably also dehydroascorbate. Does not mediate CC fructose transport. {ECO:0000250|UniProtKB:P11169}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11169}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915, CC ChEBI:CHEBI:4139; Evidence={ECO:0000250|UniProtKB:P11169}; CC -!- ACTIVITY REGULATION: Deoxyglucose transport is inhibit by D-glucose, D- CC galactose and maltose. Galactose transport is inhibited by D-glucose CC and maltose. {ECO:0000250|UniProtKB:P11169}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1730609}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. 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: Detected in brain (at protein level). Highly CC expressed in brain. {ECO:0000269|PubMed:1730609}. 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:0000250|UniProtKB:P11169}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M75135; AAA37704.1; -; mRNA. DR EMBL; X61093; CAA43406.1; -; mRNA. DR EMBL; U11853; AAB60666.1; -; Genomic_DNA. DR EMBL; U11844; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11845; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11846; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11848; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11849; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11850; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11851; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; U11852; AAB60666.1; JOINED; Genomic_DNA. DR EMBL; BC034122; AAH34122.1; -; mRNA. DR EMBL; BC058811; AAH58811.1; -; mRNA. DR CCDS; CCDS20502.1; -. DR PIR; A41751; A41751. DR RefSeq; NP_035531.3; NM_011401.4. DR AlphaFoldDB; P32037; -. DR SMR; P32037; -. DR BioGRID; 203306; 9. DR IntAct; P32037; 1. DR STRING; 10090.ENSMUSP00000032476; -. DR GlyCosmos; P32037; 1 site, No reported glycans. DR GlyGen; P32037; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P32037; -. DR PhosphoSitePlus; P32037; -. DR SwissPalm; P32037; -. DR EPD; P32037; -. DR PaxDb; P32037; -. DR PeptideAtlas; P32037; -. DR ProteomicsDB; 271348; -. DR DNASU; 20527; -. DR Ensembl; ENSMUST00000032476; ENSMUSP00000032476; ENSMUSG00000003153. DR GeneID; 20527; -. DR KEGG; mmu:20527; -. DR UCSC; uc009dpq.2; mouse. DR AGR; MGI:95757; -. DR CTD; 6515; -. DR MGI; MGI:95757; Slc2a3. DR VEuPathDB; HostDB:ENSMUSG00000003153; -. DR eggNOG; KOG0569; Eukaryota. DR GeneTree; ENSGT00940000160313; -. DR HOGENOM; CLU_001265_30_5_1; -. DR InParanoid; P32037; -. DR OMA; YWIDYGT; -. DR OrthoDB; 1899001at2759; -. DR PhylomeDB; P32037; -. DR TreeFam; TF313762; -. DR Reactome; R-MMU-189200; Cellular hexose transport. DR Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 20527; 2 hits in 75 CRISPR screens. DR ChiTaRS; Slc2a3; mouse. DR PRO; PR:P32037; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P32037; Protein. DR Bgee; ENSMUSG00000003153; Expressed in spermatocyte and 240 other tissues. DR ExpressionAtlas; P32037; baseline and differential. DR Genevisible; P32037; MM. DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI. DR GO; GO:0016235; C:aggresome; ISO:MGI. DR GO; GO:0005901; C:caveola; ISO:MGI. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0097060; C:synaptic membrane; ISO:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI. 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:0005354; F:galactose transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0016936; F:galactoside binding; ISO:MGI. DR GO; GO:0005536; F:glucose binding; ISS:UniProtKB. DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; ISO:MGI. DR GO; GO:0033222; F:xylose binding; ISO:MGI. DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB. DR GO; GO:0015757; P:galactose transmembrane transport; ISS:UniProtKB. DR GO; GO:0046323; P:glucose import; ISO:MGI. DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB. DR GO; GO:0015749; P:monosaccharide transmembrane transport; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. 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. PE 1: Evidence at protein level; KW Cell membrane; Cell projection; Direct protein sequencing; Glycoprotein; KW Membrane; Phosphoprotein; Reference proteome; Sugar transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..493 FT /note="Solute carrier family 2, facilitated glucose FT transporter member 3" FT /id="PRO_0000050354" FT TOPO_DOM 1..10 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 11..32 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 33..64 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 65..85 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 86..90 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 91..111 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TOPO_DOM 112..118 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 119..142 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 143..153 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 154..174 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 175..183 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 184..204 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 205..269 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 270..290 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 291..304 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 305..325 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 326..331 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 332..352 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 353..363 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 364..389 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 390..399 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 400..420 FT /note="Helical; Name=11" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 421..429 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P11169" FT TRANSMEM 430..450 FT /note="Helical; Name=12" FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255" FT TOPO_DOM 451..493 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P11169" FT REGION 277..279 FT /note="Important for selectivity against fructose" FT /evidence="ECO:0000250|UniProtKB:P11169" FT REGION 469..493 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 159 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT BINDING 280..281 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT BINDING 286 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT BINDING 315 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT BINDING 378 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT BINDING 386 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P11169" FT MOD_RES 232 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 482 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q07647" FT MOD_RES 489 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q07647" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" SQ SEQUENCE 493 AA; 53479 MW; 9090B8DCB8780082 CRC64; MGTTKVTPSL VFAVTVATIG SFQFGYNTGV INAPETILKD FLNYTLEERL EDLPSEGLLT ALWSLCVAIF SVGGMIGSFS VGLFVNRFGR RNSMLLVNLL AIIAGCLMGF AKIAESVEML ILGRLLIGIF CGLCTGFVPM YIGEVSPTAL RGAFGTLNQL GIVVGILVAQ IFGLDFILGS EELWPGLLGL TIIPAILQSA ALPFCPESPR FLLINKKEED QATEILQRLW GTSDVVQEIQ EMKDESVRMS QEKQVTVLEL FRSPNYVQPL LISIVLQLSQ QLSGINAVFY YSTGIFKDAG VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAVCSVFMT ISLLLKDDYE AMSFVCIVAI LIYVAFFEIG PGPIPWFIVA ELFSQGPRPA AIAVAGCCNW TSNFLVGMLF PSAAAYLGAY VFIIFAAFLI FFLIFTFFKV PETKGRTFED IARAFEGQAH SGKGPAGVEL NSMQPVKETP GNA //