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 09-DEC-2015, entry version 134. DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3; DE AltName: Full=Glucose transporter type 3, brain; DE Short=GLUT-3; GN Name=Slc2a3; Synonyms=Glut-3, Glut3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Brain; RX PubMed=1730609; 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 RT GLUT3, the brain facilitative glucose transporter isoform, and RT identification of sites 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: RT Characterization 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 RT project: 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- RT linked 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Facilitative glucose transporter that can also mediate CC the uptake of various other monosaccharides across the cell CC membrane. Mediates the uptake of glucose, 2-deoxyglucose, CC galactose, mannose, xylose and fucose, and probably also CC dehydroascorbate. Does not mediate fructose transport. CC {ECO:0000250|UniProtKB:P11169}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1730609}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. 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 CC changes, switching between a conformation where the substrate- CC binding cavity is accessible from the outside, and a another CC conformation where it is accessible from the cytoplasm. CC {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 UniGene; Mm.395108; -. DR ProteinModelPortal; P32037; -. DR SMR; P32037; 5-469. DR STRING; 10090.ENSMUSP00000032476; -. DR PhosphoSite; P32037; -. DR MaxQB; P32037; -. DR PaxDb; P32037; -. DR PRIDE; P32037; -. DR Ensembl; ENSMUST00000032476; ENSMUSP00000032476; ENSMUSG00000003153. DR GeneID; 20527; -. DR KEGG; mmu:20527; -. DR UCSC; uc009dpq.2; mouse. DR CTD; 6515; -. DR MGI; MGI:95757; Slc2a3. DR eggNOG; KOG0569; Eukaryota. DR eggNOG; COG0477; LUCA. DR HOGENOM; HOG000202871; -. DR HOVERGEN; HBG014816; -. DR InParanoid; P32037; -. DR KO; K08142; -. DR OMA; EDQATEI; -. DR OrthoDB; EOG7QVM2R; -. DR PhylomeDB; P32037; -. DR TreeFam; TF313762; -. DR Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism. DR Reactome; R-MMU-428790; Facilitative Na+-independent glucose transporters. DR Reactome; R-MMU-70153; Glucose transport. DR ChiTaRS; Slc2a3; mouse. DR NextBio; 298771; -. DR PRO; PR:P32037; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; P32037; -. DR ExpressionAtlas; P32037; baseline and differential. DR Genevisible; P32037; MM. DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB. 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 transporter activity; IDA:UniProtKB. DR GO; GO:0005536; F:glucose binding; ISS:UniProtKB. DR GO; GO:0005351; F:sugar:proton symporter activity; IBA:GO_Central. DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB. DR GO; GO:0046323; P:glucose import; IBA:GO_Central. DR GO; GO:1904659; P:glucose transmembrane transport; IDA:GOC. DR GO; GO:0015758; P:glucose transport; IDA:UniProtKB. DR GO; GO:0035428; P:hexose transmembrane transport; IBA:GO_Central. DR GO; GO:0015992; P:proton transport; IBA:GOC. DR InterPro; IPR002945; Glc_transpt_3. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport_like. DR InterPro; IPR003663; Sugar/inositol_transpt. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01192; GLUCTRSPORT3. DR PRINTS; PR00171; SUGRTRNSPORT. DR SUPFAM; SSF103473; SSF103473; 2. 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 Cell membrane; Complete proteome; Direct protein sequencing; KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 493 Solute carrier family 2, facilitated FT glucose transporter member 3. FT /FTId=PRO_0000050354. FT TOPO_DOM 1 10 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 11 32 Helical; Name=1. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 33 64 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 65 85 Helical; Name=2. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 86 90 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 91 111 Helical; Name=3. FT {ECO:0000250|UniProtKB:P11169}. FT TOPO_DOM 112 118 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 119 142 Helical; Name=4. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 143 153 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 154 174 Helical; Name=5. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 175 183 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 184 204 Helical; Name=6. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 205 269 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 270 290 Helical; Name=7. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 291 304 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 305 325 Helical; Name=8. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 326 331 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 332 352 Helical; Name=9. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 353 363 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 364 389 Helical; Name=10. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 390 399 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 400 420 Helical; Name=11. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 421 429 Extracellular. FT {ECO:0000250|UniProtKB:P11169}. FT TRANSMEM 430 450 Helical; Name=12. FT {ECO:0000250|UniProtKB:P11169, FT ECO:0000255}. FT TOPO_DOM 451 493 Cytoplasmic. FT {ECO:0000250|UniProtKB:P11169}. FT REGION 277 279 Important for selectivity against FT fructose. {ECO:0000250|UniProtKB:P11169}. FT REGION 280 286 Monosaccharide binding. FT {ECO:0000250|UniProtKB:P11169}. FT BINDING 315 315 Monosaccharide. FT {ECO:0000250|UniProtKB:P11169}. FT BINDING 378 378 Monosaccharide. FT {ECO:0000250|UniProtKB:P11169}. FT BINDING 386 386 Monosaccharide. FT {ECO:0000250|UniProtKB:P11169}. FT MOD_RES 232 232 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 471 471 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 482 482 Phosphoserine. FT {ECO:0000250|UniProtKB:Q07647}. FT MOD_RES 489 489 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q07647}. FT CARBOHYD 43 43 N-linked (GlcNAc...). FT {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 //