GTR2_RAT
ID GTR2_RAT Reviewed; 522 AA.
AC P12336; Q6LE98;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 2 {ECO:0000305};
DE AltName: Full=Glucose transporter type 2, liver {ECO:0000303|PubMed:3048704};
DE Short=GLUT-2 {ECO:0000303|PubMed:7487103};
GN Name=Slc2a2 {ECO:0000312|RGD:3705};
GN Synonyms=Glut2 {ECO:0000303|PubMed:7487103};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND TRANSPORTER ACTIVITY.
RX PubMed=3048704; DOI=10.1016/0092-8674(88)90051-7;
RA Thorens B., Sarkar H.K., Kaback H.R., Lodish H.F.;
RT "Cloning and functional expression in bacteria of a novel glucose
RT transporter present in liver, intestine, kidney, and beta-pancreatic islet
RT cells.";
RL Cell 55:281-290(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 389-456.
RC STRAIN=Holtzman; TISSUE=Liver;
RX PubMed=7487103; DOI=10.1006/abbi.1995.0059;
RA Ahn Y.H., Kim J.W., Han G.S., Lee B.G., Kim Y.S.;
RT "Cloning and characterization of rat pancreatic beta-cell/liver type
RT glucose transporter gene: a unique exon/intron organization.";
RL Arch. Biochem. Biophys. 323:387-396(1995).
CC -!- FUNCTION: Facilitative hexose transporter that mediates the transport
CC of glucose, fructose and galactose (PubMed:3048704). Likely mediates
CC the bidirectional transfer of glucose across the plasma membrane of
CC hepatocytes and is responsible for uptake of glucose by the beta cells;
CC may comprise part of the glucose-sensing mechanism of the beta cell
CC (PubMed:3048704). May also participate with the Na(+)/glucose
CC cotransporter in the transcellular transport of glucose in the small
CC intestine and kidney (By similarity). Also able to mediate the
CC transport of dehydroascorbate (By similarity).
CC {ECO:0000250|UniProtKB:P11168, ECO:0000269|PubMed:3048704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:3048704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915,
CC ChEBI:CHEBI:4139; Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- ACTIVITY REGULATION: D-glucose and maltose competitively inhibit
CC fructose transport. D-glucose, D-fructose and maltose inhibit
CC deoxyglucose transport. {ECO:0000250|UniProtKB:P11168}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3048704};
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Present in liver, intestine, kidney and beta-
CC pancreatic islet cells. {ECO:0000269|PubMed:3048704}.
CC -!- PTM: N-glycosylated; required for stability and retention at the cell
CC surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}.
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; J03145; AAA41298.1; -; mRNA.
DR EMBL; L28134; AAA99958.1; -; Genomic_DNA.
DR PIR; A31556; A31556.
DR AlphaFoldDB; P12336; -.
DR SMR; P12336; -.
DR STRING; 10116.ENSRNOP00000015866; -.
DR ChEMBL; CHEMBL4295714; -.
DR GlyGen; P12336; 1 site.
DR iPTMnet; P12336; -.
DR PhosphoSitePlus; P12336; -.
DR PaxDb; P12336; -.
DR PRIDE; P12336; -.
DR UCSC; RGD:3705; rat.
DR RGD; 3705; Slc2a2.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P12336; -.
DR PhylomeDB; P12336; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR Reactome; R-RNO-8981373; Intestinal hexose absorption.
DR PRO; PR:P12336; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0005353; F:fructose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005158; F:insulin receptor binding; IPI:RGD.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IEP:RGD.
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 GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002440; Glc_transpt_2.
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; PR01191; GLUCTRSPORT2.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050348"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 191
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 312..313
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 318
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 347
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 410
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 418
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11168"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 57086 MW; 075AB81E56CF33F7 CRC64;
MSEDKITGTL AFTVFTAVLG SFQFGYDIGV INAPQEVIIS HYRHVLGVPL DDRRATINYD
INGTDTPLIV TPAHTTPDAW EEETEGSAHI VTMLWSLSVS SFAVGGMVAS FFGGWLGDKL
GRIKAMLAAN SLSLTGALLM GCSKFGPAHA LIIAGRSVSG LYCGLISGLV PMYIGEIAPT
TLRGALGTLH QLALVTGILI SQIAGLSFIL GNQDYWHILL GLSAVPALLQ CLLLLFCPES
PRYLYLNLEE EVRAKKSLKR LRGTEDITKD INEMRKEKEE ASTEQKVSVI QLFTDPNYRQ
PIVVALMLHL AQQFSGINGI FYYSTSIFQT AGISQPVYAT IGVGAINMIF TAVSVLLVEK
AGRRTLFLAG MIGMFFCAVF MSLGLVLLDK FTWMSYVSMT AIFLFVSFFE IGPGPIPWFM
VAEFFSQGPR PTALALAAFS NWVCNFIIAL CFQYIADFLG PYVFFLFAGV VLVFTLFTFF
KVPETKGKSF DEIAAEFRKK SGSAPPRKAT VQMEFLGSSE TV
