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 08-NOV-2023, entry version 153. 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}. 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; 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 GlyCosmos; P12336; 1 site, No reported glycans. DR GlyGen; P12336; 1 site. DR iPTMnet; P12336; -. DR PhosphoSitePlus; P12336; -. DR PaxDb; 10116-ENSRNOP00000015866; -. DR UCSC; RGD:3705; rat. DR AGR; RGD:3705; -. 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:0005768; C:endosome; IDA:RGD. 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: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:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD. DR GO; GO:0009749; P:response to glucose; IEP:RGD. DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD. DR CDD; cd17431; MFS_GLUT_Class1; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 NCBIfam; TIGR00879; SP; 1. DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1. DR PANTHER; PTHR23503:SF27; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 2; 1. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01191; GLUCTRSPORT2. 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 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 //