GTR3_MOUSE
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 03-AUG-2022, entry version 179.
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}.
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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; 7.
DR IntAct; P32037; 1.
DR STRING; 10090.ENSMUSP00000032476; -.
DR GlyGen; P32037; 1 site.
DR iPTMnet; P32037; -.
DR PhosphoSitePlus; P32037; -.
DR EPD; P32037; -.
DR PaxDb; P32037; -.
DR PeptideAtlas; P32037; -.
DR PRIDE; 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 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; WIDFALF; -.
DR OrthoDB; 749998at2759; -.
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 70 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:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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:0005354; F:galactose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
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; 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; 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 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
