GTR3_RAT
ID GTR3_RAT Reviewed; 493 AA.
AC Q07647; Q62729;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
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:8243635};
DE Short=GLUT-3 {ECO:0000303|PubMed:8243635};
GN Name=Slc2a3 {ECO:0000250|UniProtKB:P11169};
GN Synonyms=Glut3 {ECO:0000303|PubMed:8243635};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8243635; DOI=10.1016/0014-5793(93)80697-s;
RA Nagamatsu S., Sawa H., Kamada K., Nakamichi Y., Yoshimoto K., Hoshino T.;
RT "Neuron-specific glucose transporter (NSGT): CNS distribution of GLUT3 rat
RT glucose transporter (RGT3) in rat central neurons.";
RL FEBS Lett. 334:289-295(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7475896; DOI=10.1016/0024-3205(95)00058-e;
RA Krishnan S.N., Haddad G.G.;
RT "Cloning of glucose transporter-3 (GLUT3) cDNA from rat brain.";
RL Life Sci. 56:1193-1197(1995).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=21076856; DOI=10.1007/s11010-010-0634-z;
RA Zoidis E., Ghirlanda-Keller C., Schmid C.;
RT "Stimulation of glucose transport in osteoblastic cells by parathyroid
RT hormone and insulin-like growth factor I.";
RL Mol. Cell. Biochem. 348:33-42(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475; SER-482 AND THR-489, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
RT "Glucose regulates mitochondrial motility via Milton modification by O-
RT GlcNAc transferase.";
RL Cell 158:54-68(2014).
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:0000250|UniProtKB:P11169};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. Perikaryon
CC {ECO:0000269|PubMed:24995978}. Cell projection
CC {ECO:0000269|PubMed:24995978}. Note=Localized to densely spaced patches
CC along neuronal processes. {ECO:0000269|PubMed:24995978}.
CC -!- TISSUE SPECIFICITY: Brain and osteoblastic cells (at protein level)
CC (PubMed:21076856). Highly expressed in brain (PubMed:7475896,
CC PubMed:21076856). {ECO:0000269|PubMed:21076856,
CC ECO:0000269|PubMed:7475896}.
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; D13962; BAA03065.1; -; mRNA.
DR EMBL; U17978; AAA62503.1; -; mRNA.
DR PIR; S38981; S38981.
DR RefSeq; NP_058798.2; NM_017102.2.
DR RefSeq; XP_003749881.1; XM_003749833.4.
DR RefSeq; XP_017458346.1; XM_017602857.1.
DR AlphaFoldDB; Q07647; -.
DR SMR; Q07647; -.
DR BioGRID; 247582; 1.
DR IntAct; Q07647; 1.
DR STRING; 10116.ENSRNOP00000066684; -.
DR TCDB; 2.A.1.1.12; the major facilitator superfamily (mfs).
DR GlyGen; Q07647; 1 site.
DR iPTMnet; Q07647; -.
DR PhosphoSitePlus; Q07647; -.
DR jPOST; Q07647; -.
DR PaxDb; Q07647; -.
DR PRIDE; Q07647; -.
DR GeneID; 25551; -.
DR KEGG; rno:25551; -.
DR UCSC; RGD:3706; rat.
DR CTD; 6515; -.
DR RGD; 3706; Slc2a3.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; Q07647; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; Q07647; -.
DR TreeFam; TF313762; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q07647; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
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; IDA:SynGO.
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:0099699; C:integral component of synaptic membrane; IDA:SynGO.
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:0030672; C:synaptic vesicle membrane; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005536; F:glucose binding; IDA:RGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IDA:RGD.
DR GO; GO:0033222; F:xylose binding; IDA:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
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; IDA:RGD.
DR GO; GO:0098708; P:glucose import across plasma membrane; ISO:RGD.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:RGD.
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; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..493
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 3"
FT /id="PRO_0000050358"
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, ECO:0000255"
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 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:0000250|UniProtKB:P32037"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32037"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 489
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 55
FT /note="R -> S (in Ref. 2; AAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="S -> F (in Ref. 2; AAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="H -> Q (in Ref. 2; AAA62503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 53581 MW; 745446B59BDF4399 CRC64;
MGTAKVTPSL VFAVTVATIG SFQFGYNTGV INAPETIIKD FLNYTLEERL EDLPREGLLT
TLWSLCVAIF SVGGMIGSFS VGLFVNRFGR RNSMLLVNLI AILGGCLMGF AKIAESVEML
ILGRLIIGIF CGLCTGFVPM YIGEVSPTAL RGAFGTLNQL GIVVGILVAQ VFGLDFILGS
EELWPGLLGL TIIPAILQSA ALPFCPESPR FLLINRKEED QATEILQRLW GTPDVIQEIQ
EMKDESIRMS QEKQVTVLEL FKSPSYFQPL LISVVLQLSQ QFSGINAVFY YSTGIFQDAG
VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAVCSVFMT ISLLLKDEYE
AMSFVCIVAI LVYVAFFEIG PGPIPWFIVA ELFSQGPRPA AMAVAGCSNW TSNFLVGMFF
PSAAAYLGAY VFIIFAAFLV FFLIFTSFKV PETKGRTFED ITRAFEGQAH SGKGSAGVEL
NSMQPVKETP GNA
