GTR2_MOUSE
ID GTR2_MOUSE Reviewed; 523 AA.
AC P14246; Q3TNA5; Q9DBA7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 3.
DT 03-AUG-2022, entry version 196.
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:2771649};
DE Short=GLUT-2 {ECO:0000303|PubMed:7929431};
GN Name=Slc2a2 {ECO:0000312|MGI:MGI:1095438};
GN Synonyms=Glut2 {ECO:0000303|PubMed:7929431};
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2602116; DOI=10.1093/nar/17.23.10099;
RA Suzue K., Lodish H.F., Thorens B.;
RT "Sequence of the mouse liver glucose transporter.";
RL Nucleic Acids Res. 17:10099-10099(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=2771649; DOI=10.1093/nar/17.15.6386;
RA Asano T., Shibasaki Y., Lin J.L., Akanuma Y., Takaku F., Oka Y.;
RT "The nucleotide sequence of cDNA for a mouse liver-type glucose transporter
RT protein.";
RL Nucleic Acids Res. 17:6386-6386(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=7929431; DOI=10.1016/s0021-9258(18)47106-2;
RA Waeber G., Thompson N., Haefliger J.-A., Nicod P.;
RT "Characterization of the murine high Km glucose transporter GLUT2 gene and
RT its transcriptional regulation by glucose in a differentiated insulin-
RT secreting cell line.";
RL J. Biol. Chem. 269:26912-26919(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 384-496, AND TISSUE SPECIFICITY.
RX PubMed=1765007; DOI=10.1242/dev.113.1.363;
RA Hogan A., Heyner S., Charron M.J., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Thorens B., Schultz G.A.;
RT "Glucose transporter gene expression in early mouse embryos.";
RL Development 113:363-372(1991).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=1289053; DOI=10.1242/dev.116.3.555;
RA Smith D.E., Gridley T.;
RT "Differential screening of a PCR-generated mouse embryo cDNA library:
RT glucose transporters are differentially expressed in early postimplantation
RT mouse embryos.";
RL Development 116:555-561(1992).
RN [8]
RP GLYCOSYLATION AT ASN-62.
RC STRAIN=129/SvJ;
RX PubMed=16377570; DOI=10.1016/j.cell.2005.09.041;
RA Ohtsubo K., Takamatsu S., Minowa M.T., Yoshida A., Takeuchi M., Marth J.D.;
RT "Dietary and genetic control of glucose transporter 2 glycosylation
RT promotes insulin secretion in suppressing diabetes.";
RL Cell 123:1307-1321(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 hexose transporter that mediates the transport
CC of glucose, fructose and galactose. Likely mediates the bidirectional
CC transfer of glucose across the plasma membrane of hepatocytes and is
CC responsible for uptake of glucose by the beta cells; may comprise part
CC of the glucose-sensing mechanism of the beta cell. May also participate
CC with the Na(+)/glucose cotransporter in the transcellular transport of
CC glucose in the small intestine and kidney. Also able to mediate the
CC transport of dehydroascorbate. {ECO:0000250|UniProtKB:P11168}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11168};
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:0000250|UniProtKB:P11168};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In embryo, expressed in endoderm layer of yolk sac
CC and liver primordium. {ECO:0000269|PubMed:1289053,
CC ECO:0000269|PubMed:1765007}.
CC -!- PTM: N-glycosylated; required for stability and retention at the cell
CC surface of pancreatic beta cells. {ECO:0000269|PubMed:16377570}.
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; X16986; CAA34855.1; -; mRNA.
DR EMBL; X15684; CAA33719.1; -; mRNA.
DR EMBL; S77926; AAB20847.1; -; mRNA.
DR EMBL; AK005068; BAB23792.1; -; mRNA.
DR EMBL; AK165430; BAE38184.1; -; mRNA.
DR EMBL; BC034675; AAH34675.1; -; mRNA.
DR EMBL; X78722; CAA55368.1; -; Genomic_DNA.
DR CCDS; CCDS50880.1; -.
DR PIR; S06920; S06920.
DR RefSeq; NP_112474.2; NM_031197.2.
DR AlphaFoldDB; P14246; -.
DR SMR; P14246; -.
DR BioGRID; 203305; 2.
DR STRING; 10090.ENSMUSP00000029240; -.
DR GlyGen; P14246; 1 site.
DR iPTMnet; P14246; -.
DR PhosphoSitePlus; P14246; -.
DR jPOST; P14246; -.
DR MaxQB; P14246; -.
DR PaxDb; P14246; -.
DR PeptideAtlas; P14246; -.
DR PRIDE; P14246; -.
DR ProteomicsDB; 271186; -.
DR Antibodypedia; 4178; 552 antibodies from 42 providers.
DR DNASU; 20526; -.
DR Ensembl; ENSMUST00000029240; ENSMUSP00000029240; ENSMUSG00000027690.
DR GeneID; 20526; -.
DR KEGG; mmu:20526; -.
DR UCSC; uc008oua.2; mouse.
DR CTD; 6514; -.
DR MGI; MGI:1095438; Slc2a2.
DR VEuPathDB; HostDB:ENSMUSG00000027690; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000155708; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P14246; -.
DR OMA; PQCIPMN; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; P14246; -.
DR TreeFam; TF313762; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR Reactome; R-MMU-8981373; Intestinal hexose absorption.
DR BioGRID-ORCS; 20526; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc2a2; mouse.
DR PRO; PR:P14246; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P14246; protein.
DR Bgee; ENSMUSG00000027690; Expressed in islet of Langerhans and 55 other tissues.
DR ExpressionAtlas; P14246; baseline and differential.
DR Genevisible; P14246; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
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:MGI.
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; ISO:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0008643; P:carbohydrate transport; TAS:MGI.
DR GO; GO:0009758; P:carbohydrate utilization; ISO:MGI.
DR GO; GO:0071398; P:cellular response to fatty acid; ISO:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; ISS: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; 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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..523
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050347"
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..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..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..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..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..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 313..314
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 319
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 348
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 411
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 419
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16377570"
FT CONFLICT 106
FT /note="G -> D (in Ref. 2; CAA33719)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="T -> N (in Ref. 1; CAA34855)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="S -> T (in Ref. 2; CAA33719)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="F -> L (in Ref. 1; CAA34855)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="P -> S (in Ref. 1; CAA34855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57107 MW; F12B5376CBDB5F63 CRC64;
MSEDKITGTL AFTVFTAVLS SFQFGYDIGV INAPQEVIIS HYRHVLGVPL DDRKAAINYD
VNGTDTPLTV TPAYTTPAPW DEEETEGSAH IVTMLWSLSV SSFAVGGMVA SFFGGWLGDK
LGRIKAMLAA NSLSLTGALL MGCSKFGPAH ALIIAGRSVS GLYCGLISGL VPMYIGEIAP
TTLRGALGTL HQLALVTGIL ISQIAGLSFI LGNQDHWHIL LGLSAVPALL QCLLLLFCPE
SPRYLYIKLE EEVRAKKSLK RLRGTEDVTK DINEMKKEKE EASTEQKVSV IQLFTDANYR
QPILVALMLH MAQQFSGING IFYYSTSIFQ TAGISQPVYA TIGVGAINMI FTAVSVLLVE
KAGRRTLFLT GMIGMFFCTI FMSVGLVLLD KFAWMSYVSM TAIFLFVSFF EIGPGPIPWF
MVAEFFSQGP RPTALALAAF SNWVCNFVIA LCFQYIADFL GPYVFFLFAG VVLVFTLFTF
FKVPETKGKS FEEIAAEFRK KSGSAPPRKA AVQMEFLASS ESV
