GLUT4_MOUSE
ID GLUT4_MOUSE Reviewed; 509 AA.
AC P14142; Q3TPK6; Q9JJN9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 4 {ECO:0000305};
DE AltName: Full=GT2 {ECO:0000303|PubMed:2654938};
DE AltName: Full=Glucose transporter type 4, insulin-responsive {ECO:0000303|PubMed:10952468};
DE Short=GLUT-4 {ECO:0000303|PubMed:10952468};
GN Name=Slc2a4 {ECO:0000312|MGI:MGI:95758};
GN Synonyms=Glut4 {ECO:0000303|PubMed:10952468};
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], AND TISSUE SPECIFICITY.
RX PubMed=2654938; DOI=10.1073/pnas.86.9.3150;
RA Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T.,
RA Cornelius P., Pekala P.H., Lane M.D.;
RT "Sequence, tissue distribution, and differential expression of mRNA for a
RT putative insulin-responsive glucose transporter in mouse 3T3-L1
RT adipocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ, and NSY; TISSUE=Muscle;
RX PubMed=10952468; DOI=10.1007/s001250051472;
RA Ueda H., Ikegami H., Kawaguchi Y., Fujisawa T., Nojima K., Babaya N.,
RA Yamada K., Shibata M., Yamato E., Ogihara T.;
RT "Age-dependent changes in phenotypes and candidate gene analysis in a
RT polygenic animal model of type II diabetes; NSY mouse.";
RL Diabetologia 43:932-938(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ; TISSUE=Brain;
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Characterization of quantitative trait loci influencing growth and
RT adiposity using congenic mouse strains.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Spinal ganglion;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [8]
RP EFFECT OF TBC1D4 ON GLUT4 TRANSLOCATION.
RX PubMed=12637568; DOI=10.1074/jbc.c300063200;
RA Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S., Garner C.W.,
RA Lienhard G.E.;
RT "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
RT regulates GLUT4 translocation.";
RL J. Biol. Chem. 278:14599-14602(2003).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-486 AND SER-488, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21907143; DOI=10.1016/j.cmet.2011.06.015;
RA Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D.,
RA Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M.,
RA Kruger M., Jiang Z.Y.;
RT "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into
RT the plasma membrane.";
RL Cell Metab. 14:378-389(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=25586176; DOI=10.1074/jbc.m114.624759;
RA Ando Y., Shinozawa Y., Iijima Y., Yu B.C., Sone M., Ooi Y., Watanaka Y.,
RA Chida K., Hakuno F., Takahashi S.;
RT "Tumor necrosis factor (TNF)-alpha-induced repression of GKAP42 protein
RT levels through cGMP-dependent kinase (cGK)-Ialpha causes insulin resistance
RT in 3T3-L1 adipocytes.";
RL J. Biol. Chem. 290:5881-5892(2015).
RN [13]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26240143; DOI=10.1074/jbc.m115.657361;
RA Fazakerley D.J., Naghiloo S., Chaudhuri R., Koumanov F., Burchfield J.G.,
RA Thomas K.C., Krycer J.R., Prior M.J., Parker B.L., Murrow B.A.,
RA Stoeckli J., Meoli C.C., Holman G.D., James D.E.;
RT "Proteomic Analysis of GLUT4 Storage Vesicles Reveals Tumor Suppressor
RT Candidate 5 (TUSC5) as a Novel Regulator of Insulin Action in Adipocytes.";
RL J. Biol. Chem. 290:23528-23542(2015).
RN [14]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRARG1, AND
RP FUNCTION.
RX PubMed=26629404; DOI=10.1016/j.molmet.2015.08.003;
RA Beaton N., Rudigier C., Moest H., Mueller S., Mrosek N., Roeder E.,
RA Rudofsky G., Ruelicke T., Ukropec J., Ukropcova B., Augustin R.,
RA Neubauer H., Wolfrum C.;
RT "TUSC5 regulates insulin-mediated adipose tissue glucose uptake by
RT modulation of GLUT4 recycling.";
RL Mol. Metab. 4:795-810(2015).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=27354378; DOI=10.1083/jcb.201509052;
RA Bruno J., Brumfield A., Chaudhary N., Iaea D., McGraw T.E.;
RT "SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
RT trafficking in adipocytes.";
RL J. Cell Biol. 214:61-76(2016).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=27739494; DOI=10.1038/srep35438;
RA Liu T., Yu B., Kakino M., Fujimoto H., Ando Y., Hakuno F., Takahashi S.I.;
RT "A novel IRS-1-associated protein, DGKzeta regulates GLUT4 translocation in
RT 3T3-L1 adipocytes.";
RL Sci. Rep. 6:35438-35438(2016).
CC -!- FUNCTION: Insulin-regulated facilitative glucose transporter, which
CC plays a key role in removal of glucose from circulation
CC (PubMed:26240143, PubMed:26629404). Response to insulin is regulated by
CC its intracellular localization: in the absence of insulin, it is
CC efficiently retained intracellularly within storage compartments in
CC muscle and fat cells (PubMed:26240143, PubMed:26629404). Upon insulin
CC stimulation, translocates from these compartments to the cell surface
CC where it transports glucose from the extracellular milieu into the cell
CC (PubMed:26240143, PubMed:26629404). {ECO:0000269|PubMed:26240143,
CC ECO:0000269|PubMed:26629404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P19357};
CC -!- SUBUNIT: Binds to DAXX (By similarity). Interacts via its N-terminus
CC with SRFBP1 (By similarity). Interacts with NDUFA9 (By similarity).
CC Interacts with TRARG1; the interaction is required for proper SLC2A4
CC recycling after insulin stimulation (PubMed:26629404).
CC {ECO:0000250|UniProtKB:P14672, ECO:0000250|UniProtKB:P19357,
CC ECO:0000269|PubMed:26629404}.
CC -!- INTERACTION:
CC P14142; Q3U7R1: Esyt1; NbExp=2; IntAct=EBI-7540210, EBI-8398881;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907143,
CC ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:26240143,
CC ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27739494}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21907143}. Endomembrane system
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass
CC membrane protein {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404,
CC ECO:0000269|PubMed:27354378}. Note=Localizes primarily to the
CC perinuclear region, undergoing continued recycling to the plasma
CC membrane where it is rapidly reinternalized (PubMed:26629404,
CC PubMed:26240143, PubMed:27354378). The dileucine internalization motif
CC is critical for intracellular sequestration (PubMed:26240143,
CC PubMed:26629404). Insulin stimulation induces translocation to the cell
CC membrane (PubMed:27739494). {ECO:0000269|PubMed:26240143,
CC ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378,
CC ECO:0000269|PubMed:27739494}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles
CC (PubMed:2654938, PubMed:26240143). Expressed in brown and white adipose
CC tissues (PubMed:2654938, PubMed:26240143).
CC {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:2654938}.
CC -!- DOMAIN: The dileucine internalization motif is critical for
CC intracellular sequestration. {ECO:0000250|UniProtKB:P14672}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P14672}.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC7 controls the insulin-
CC dependent translocation of GLUT4 to the plasma membrane.
CC {ECO:0000250|UniProtKB:P14672}.
CC -!- DISEASE: Note=Defects in Slc2a4 may be the cause of certain post-
CC receptor defects in non-insulin-dependent diabetes mellitus (NIDDM).
CC -!- MISCELLANEOUS: Insulin-stimulated phosphorylation of TBC1D4 is required
CC for GLUT4 translocation. {ECO:0000269|PubMed:12637568}.
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; M23383; AAA37753.1; -; mRNA.
DR EMBL; AB008453; BAB03251.1; -; mRNA.
DR EMBL; AY902342; AAX90627.1; -; Genomic_DNA.
DR EMBL; AK137607; BAE23429.1; -; mRNA.
DR EMBL; AK164310; BAE37730.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12494.1; -; Genomic_DNA.
DR EMBL; CH466596; EDL12496.1; -; Genomic_DNA.
DR EMBL; BC014282; AAH14282.1; -; mRNA.
DR CCDS; CCDS36201.1; -.
DR PIR; B30310; B30310.
DR RefSeq; NP_033230.2; NM_009204.2.
DR AlphaFoldDB; P14142; -.
DR SMR; P14142; -.
DR BioGRID; 203307; 7.
DR DIP; DIP-42440N; -.
DR ELM; P14142; -.
DR IntAct; P14142; 1.
DR MINT; P14142; -.
DR STRING; 10090.ENSMUSP00000018710; -.
DR ChEMBL; CHEMBL1250410; -.
DR GlyGen; P14142; 1 site.
DR iPTMnet; P14142; -.
DR PhosphoSitePlus; P14142; -.
DR SwissPalm; P14142; -.
DR jPOST; P14142; -.
DR MaxQB; P14142; -.
DR PaxDb; P14142; -.
DR PeptideAtlas; P14142; -.
DR PRIDE; P14142; -.
DR ProteomicsDB; 271349; -.
DR Antibodypedia; 4297; 799 antibodies from 46 providers.
DR DNASU; 20528; -.
DR Ensembl; ENSMUST00000018710; ENSMUSP00000018710; ENSMUSG00000018566.
DR GeneID; 20528; -.
DR KEGG; mmu:20528; -.
DR UCSC; uc007jsy.1; mouse.
DR CTD; 6517; -.
DR MGI; MGI:95758; Slc2a4.
DR VEuPathDB; HostDB:ENSMUSG00000018566; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000160688; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P14142; -.
DR OMA; KVQWRFF; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P14142; -.
DR TreeFam; TF313762; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR BioGRID-ORCS; 20528; 2 hits in 71 CRISPR screens.
DR PRO; PR:P14142; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P14142; protein.
DR Bgee; ENSMUSG00000018566; Expressed in hindlimb stylopod muscle and 182 other tissues.
DR ExpressionAtlas; P14142; baseline and differential.
DR Genevisible; P14142; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; IDA:MGI.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015304; F:glucose uniporter activity; ISS:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005360; F:insulin-responsive glucose:proton symporter activity; TAS:MGI.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IDA:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0046323; P:glucose import; ISO:MGI.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0031550; P:positive regulation of brain-derived neurotrophic factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0098694; P:regulation of synaptic vesicle budding from presynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0007614; P:short-term memory; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002441; Glc_transpt_4.
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; PR01193; GLUCTRSPORT4.
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; Cytoplasm; Diabetes mellitus; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..509
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 4"
FT /id="PRO_0000050364"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 7..13
FT /note="Interaction with SRFBP1"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT MOTIF 489..490
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT BINDING 177
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 298..299
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 304
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 333
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 396
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 404
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19357"
FT MOD_RES 274
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 223
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CONFLICT 11
FT /note="D -> DVK (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="A -> V (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Q -> R (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="R -> P (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="Missing (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="A -> R (in Ref. 1; AAA37753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 54755 MW; A174212455EE0390 CRC64;
MPSGFQQIGS DDGEPPRQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK VIEQSYNATW
LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG IISQWLGRKR AMLANNVLAV
LGGALMGLAN AAASYEILIL GRFLIGAYSG LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI
VIGILVAQVL GLESMLGTAT LWPLLLALTV LPALLQLILL PFCPESPRYL YIIRNLEGPA
RKSLKRLTGW ADVSDALAEL KDEKRKLERE RPMSLLQLLG SRTHRQPLII AVVLQLSQQL
SGINAVFYYS TSIFESAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR TLHLLGLAGM
CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM
AVAGFSNWTC NFIVGMGFQY VADAMGPYVF LLFAVLLLGF FIFTFLKVPE TRGRTFDQIS
AAFRRTPSLL EQEVKPSTEL EYLGPDEND
