ID GLUT4_HUMAN Reviewed; 509 AA. AC P14672; Q05BQ3; Q14CX2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 02-SEP-2026, entry version 252. DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 4 {ECO:0000305}; DE AltName: Full=Glucose transporter type 4, insulin-responsive {ECO:0000303|PubMed:1397719}; DE Short=GLUT-4 {ECO:0000303|PubMed:1397719}; GN Name=SLC2A4 {ECO:0000312|HGNC:HGNC:11009}; GN Synonyms=GLUT4 {ECO:0000303|PubMed:1397719}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2656669; DOI=10.1016/s0021-9258(18)83106-4; RA Fukumoto H., Kayano T., Buse J.B., Edwards Y., Pilch P.F., Bell G.I., RA Seino S.; RT "Cloning and characterization of the major insulin-responsive glucose RT transporter expressed in human skeletal muscle and other insulin-responsive RT tissues."; RL J. Biol. Chem. 264:7776-7779(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-385. RX PubMed=1397719; DOI=10.2337/diab.41.11.1436; RA Buse J.B., Yasuda K., Lay T.P., Seo T.S., Olson A.L., Pessin J.E., RA Karam J.H., Seino S., Bell G.I.; RT "Human GLUT4/muscle-fat glucose-transporter gene. Characterization and RT genetic variation."; RL Diabetes 41:1436-1445(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX PubMed=7916714; DOI=10.1016/0378-1119(93)90438-9; RA Chiaramonte R., Martini R., Taramelli R., Comi P.; RT "Identification of the 5' end of the gene encoding a human insulin- RT responsive glucose transporter."; RL Gene 130:307-308(1993). RN [6] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 489-LEU-LEU-490. RX PubMed=8300557; DOI=10.1016/s0021-9258(17)41949-1; RA Verhey K.J., Birnbaum M.J.; RT "A Leu-Leu sequence is essential for COOH-terminal targeting signal of RT GLUT4 glucose transporter in fibroblasts."; RL J. Biol. Chem. 269:2353-2356(1994). RN [7] RP INTERACTION WITH DAXX, AND SUMOYLATION. RX PubMed=11842083; DOI=10.1074/jbc.m110294200; RA Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.; RT "The insulin-sensitive glucose transporter, GLUT4, interacts physically RT with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to RT SUMO1."; RL J. Biol. Chem. 277:19783-19791(2002). RN [8] RP INTERACTION WITH SRFBP1. RX PubMed=16647043; DOI=10.1016/j.bbrc.2006.04.017; RA Lisinski I., Matsumoto H., Yver D.R., Schuermann A., Cushman S.W., RA Al-Hasani H.; RT "Identification and characterization of p49/STRAP as a novel GLUT4-binding RT protein."; RL Biochem. Biophys. Res. Commun. 344:1179-1185(2006). RN [9] RP PHOSPHORYLATION AT SER-274 BY SGK1. RX PubMed=17382906; DOI=10.1016/j.bbrc.2007.03.029; RA Jeyaraj S., Boehmer C., Lang F., Palmada M.; RT "Role of SGK1 kinase in regulating glucose transport via glucose RT transporter GLUT4."; RL Biochem. Biophys. Res. Commun. 356:629-635(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57. RC TISSUE=Leukemic T-cell; 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 [12] RP PALMITOYLATION AT CYS-223, AND MUTAGENESIS OF CYS-223. RX PubMed=28057756; DOI=10.1074/jbc.m116.747139; RA Du K., Murakami S., Sun Y., Kilpatrick C.L., Luscher B.; RT "DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4 RT Membrane Translocation."; RL J. Biol. Chem. 292:2979-2991(2017). RN [13] RP VARIANT T2D ILE-383. RX PubMed=1918382; DOI=10.1172/jci115437; RA Kusari J., Verma U.S., Buse J.B., Henry R.R., Olefsky J.M.; RT "Analysis of the gene sequences of the insulin receptor and the insulin- RT sensitive glucose transporter (GLUT-4) in patients with common-type non- RT insulin-dependent diabetes mellitus."; RL J. Clin. Invest. 88:1323-1330(1991). RN [14] RP VARIANT T2D ILE-383. RX PubMed=1756912; DOI=10.2337/diab.40.12.1712; RA Choi W.H., O'Rahilly S., Buse J.B., Rees A., Morgan R., Flier J.S., RA Moller D.E.; RT "Molecular scanning of insulin-responsive glucose transporter (GLUT4) gene RT in NIDDM subjects."; RL Diabetes 40:1712-1718(1991). RN [15] RP VARIANT T2D ILE-383. RX PubMed=1521731; DOI=10.1007/bf02342449; RA O'Rahilly S., Krook A., Morgan R., Rees A., Flier J.S., Moller D.E.; RT "Insulin receptor and insulin-responsive glucose transporter (GLUT 4) RT mutations and polymorphisms in a Welsh type 2 (non-insulin-dependent) RT diabetic population."; RL Diabetologia 35:486-489(1992). CC -!- FUNCTION: Insulin-regulated facilitative glucose transporter, which CC plays a key role in removal of glucose from circulation. Response to CC insulin is regulated by its intracellular localization: in the absence CC of insulin, it is efficiently retained intracellularly within storage CC compartments in muscle and fat cells. Upon insulin stimulation, CC translocates from these compartments to the cell surface where it CC transports glucose from the extracellular milieu into the cell. CC {ECO:0000250|UniProtKB:P19357}. 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: Interacts with NDUFA9 (By similarity). Binds to DAXX CC (PubMed:11842083). Interacts via its N-terminus with SRFBP1 CC (PubMed:16647043). Interacts with TRARG1; the interaction is required CC for proper SLC2A4 recycling after insulin stimulation (By similarity). CC {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P19357, CC ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:16647043}. CC -!- INTERACTION: CC P14672; Q9NP73: ALG13; NbExp=2; IntAct=EBI-367146, EBI-947892; CC P14672; O43889-2: CREB3; NbExp=3; IntAct=EBI-367146, EBI-625022; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14142}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. CC Endomembrane system {ECO:0000269|PubMed:8300557}; Multi-pass membrane CC protein {ECO:0000269|PubMed:8300557}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the CC perinuclear region, undergoing continued recycling to the plasma CC membrane where it is rapidly reinternalized (PubMed:8300557). The CC dileucine internalization motif is critical for intracellular CC sequestration (PubMed:8300557). Insulin stimulation induces CC translocation to the cell membrane (By similarity). CC {ECO:0000250|UniProtKB:P14142, ECO:0000269|PubMed:8300557}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14672-1; Sequence=Displayed; CC Name=2; CC IsoId=P14672-2; Sequence=VSP_056331, VSP_056332; CC -!- TISSUE SPECIFICITY: Skeletal and cardiac muscles; brown and white fat. CC -!- DOMAIN: The dileucine internalization motif is critical for CC intracellular sequestration. {ECO:0000269|PubMed:8300557}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:11842083}. CC -!- PTM: Palmitoylated (PubMed:28057756). Palmitoylation by ZDHHC7 controls CC the insulin-dependent translocation of GLUT4 to the plasma membrane CC (PubMed:28057756). {ECO:0000269|PubMed:28057756}. CC -!- DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial CC disorder of glucose homeostasis caused by a lack of sensitivity to CC insulin. Affected individuals usually have an obese body habitus and CC manifestations of a metabolic syndrome characterized by diabetes, CC insulin resistance, hypertension and hypertriglyceridemia. The disease CC results in long-term complications that affect the eyes, kidneys, CC nerves, and blood vessels. {ECO:0000269|PubMed:1521731, CC ECO:0000269|PubMed:1756912, ECO:0000269|PubMed:1918382}. Note=The CC disease may be caused by variants affecting the gene represented in CC this entry. CC -!- MISCELLANEOUS: Insulin-stimulated phosphorylation of TBC1D4 is required CC for GLUT4 translocation. {ECO:0000250|UniProtKB:P14142}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=GLUT4 entry; CC URL="https://en.wikipedia.org/wiki/Glut4"; 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; M20747; AAA59189.1; -; mRNA. DR EMBL; M91463; AAA52569.1; -; Genomic_DNA. DR EMBL; AC003688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034387; AAH34387.1; -; mRNA. DR EMBL; BC069615; AAH69615.1; -; mRNA. DR EMBL; BC069621; AAH69621.1; -; mRNA. DR EMBL; BC113592; AAI13593.1; -; mRNA. DR EMBL; BC126164; AAI26165.1; -; mRNA. DR EMBL; X58489; CAA41399.1; -; Genomic_DNA. DR CCDS; CCDS11097.1; -. [P14672-1] DR PIR; A49158; A33801. DR RefSeq; NP_001033.1; NM_001042.3. [P14672-1] DR PDB; 7WSM; EM; 3.25 A; A=1-509. DR PDB; 7WSN; EM; 3.31 A; A=1-509. DR AlphaFoldDB; P14672; -. DR EMDB; EMD-32760; -. DR EMDB; EMD-32761; -. DR SMR; P14672; -. DR BioGRID; 112408; 78. DR CORUM; P14672; -. DR FunCoup; P14672; 894. DR IntAct; P14672; 34. DR MINT; P14672; -. DR NDEx; IQUERY-CP-SLC2A4; 22 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000320935; -. DR BindingDB; P14672; -. DR ChEMBL; CHEMBL5874; -. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB01914; D-glucose. DR DrugBank; DB09341; Dextrose, unspecified form. DR DrugBank; DB09502; Fludeoxyglucose (18F). DR DrugBank; DB01296; Glucosamine. DR TCDB; 2.A.1.1.80; the major facilitator superfamily (mfs). DR GlyCosmos; P14672; 1 site, No reported glycans. DR GlyGen; P14672; 1 site. DR iPTMnet; P14672; -. DR PhosphoSitePlus; P14672; -. DR SwissPalm; P14672; -. DR BioMuta; SLC2A4; -. DR DMDM; 121761; -. DR jPOST; P14672; -. DR MassIVE; P14672; -. DR PaxDb; 9606-ENSP00000320935; -. DR PeptideAtlas; P14672; -. DR ProteomicsDB; 53073; -. [P14672-1] DR ProteomicsDB; 58372; -. DR Antibodypedia; 4297; 814 antibodies from 48 providers. DR DNASU; 6517; -. DR Ensembl; ENST00000317370.13; ENSP00000320935.8; ENSG00000181856.16. [P14672-1] DR Ensembl; ENST00000572485.5; ENSP00000461086.1; ENSG00000181856.16. [P14672-2] DR Ensembl; ENST00000672821.1; ENSP00000500577.1; ENSG00000288174.1. [P14672-2] DR Ensembl; ENST00000673224.1; ENSP00000499804.1; ENSG00000288174.1. [P14672-1] DR GeneID; 6517; -. DR KEGG; hsa:6517; -. DR MANE-Select; ENST00000317370.13; ENSP00000320935.8; NM_001042.3; NP_001033.1. DR UCSC; uc002gfp.4; human. [P14672-1] DR AGR; HGNC:11009; -. DR ClinPGx; PA35879; -. DR CTD; 6517; -. DR DisGeNET; 6517; -. DR GeneCards; SLC2A4; -. DR HGNC; HGNC:11009; SLC2A4. DR HPA; ENSG00000181856; Tissue enhanced (heart muscle, skeletal muscle). DR MalaCards; SLC2A4; -. DR MIM; 125853; phenotype. DR MIM; 138190; gene. DR OpenTargets; ENSG00000181856; -. DR VEuPathDB; HostDB:ENSG00000181856; -. DR eggNOG; KOG0569; Eukaryota. DR GeneTree; ENSGT00940000160688; -. DR HOGENOM; CLU_001265_30_5_1; -. DR InParanoid; P14672; -. DR OMA; VAQFLCM; -. DR OrthoDB; 4540492at2759; -. DR PAN-GO; P14672; 7 GO annotations based on evolutionary models. DR PhylomeDB; P14672; -. DR PathwayCommons; P14672; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-189200; Cellular hexose transport. DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation. DR SignaLink; P14672; -. DR SIGNOR; P14672; -. DR Agora; ENSG00000181856; -. DR BioGRID-ORCS; 6517; 11 hits in 1154 CRISPR screens. DR GeneWiki; GLUT4; -. DR GenomeRNAi; 6517; -. DR Pharos; P14672; Tchem. DR PRO; PR:P14672; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P14672; protein. DR Bgee; ENSG00000181856; Expressed in gastrocnemius and 94 other cell types or tissues. DR ExpressionAtlas; P14672; baseline and differential. DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl. DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0012505; C:endomembrane system; EXP:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0042383; C:sarcolemma; ISS:ARUK-UCL. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl. DR GO; GO:0030315; C:T-tubule; IEA:Ensembl. DR GO; GO:0005802; C:trans-Golgi network; IDA:ARUK-UCL. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:Ensembl. DR GO; GO:0012506; C:vesicle membrane; IDA:MGI. DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProt. DR GO; GO:0015304; F:D-glucose uniporter activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB. DR GO; GO:0098708; P:D-glucose import across plasma membrane; NAS:BHF-UCL. DR GO; GO:1904659; P:D-glucose transmembrane transport; ISS:UniProtKB. DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central. DR GO; GO:0042593; P:glucose homeostasis; IDA:MGI. DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:UniProtKB. DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL. DR GO; GO:0007616; P:long-term memory; ISS:ARUK-UCL. DR GO; GO:0031550; P:positive regulation of brain-derived neurotrophic factor receptor signaling pathway; ISS:ARUK-UCL. DR GO; GO:0098694; P:regulation of synaptic vesicle budding from presynaptic endocytic zone membrane; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; ISS:ARUK-UCL. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0070343; P:white fat cell proliferation; ISS:UniProt. DR CDD; cd17431; MFS_GLUT_Class1; 1. DR FunFam; 1.20.1250.20:FF:000029; solute carrier family 2, facilitated glucose transporter member 4; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 NCBIfam; TIGR00879; SP; 1. DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1. DR PANTHER; PTHR23503:SF120; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 4; 1. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01193; GLUCTRSPORT4. 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. DR PDBsum; 7WSM; -. DR PDBsum; 7WSN; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; KW Diabetes mellitus; Disease variant; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphoprotein; Proteomics identification; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation. FT CHAIN 1..509 FT /note="Solute carrier family 2, facilitated glucose FT transporter member 4" FT /id="PRO_0000050363" FT TOPO_DOM 1..24 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 25..45 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 46..81 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 82..102 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 103..111 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 112..132 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 133..142 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 143..163 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 164..171 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 172..192 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 193..201 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 202..222 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 223..287 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 288..308 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 309..323 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 324..344 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 345..353 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 354..374 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 375..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..417 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 418..438 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 439..445 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 446..466 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 467..509 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 7..13 FT /note="Interaction with SRFBP1" FT /evidence="ECO:0000269|PubMed:16647043" FT MOTIF 489..490 FT /note="Dileucine internalization motif" FT /evidence="ECO:0000269|PubMed:8300557" 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:0000269|PubMed:17382906" FT MOD_RES 486 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P14142" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P14142" FT LIPID 223 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:28057756" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT VAR_SEQ 342..415 FT /note="LLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVA FT FFEIGPGPIPWFIVAELFSQGP -> TAHLWNGPSHWLHLPGCPGGVVGGAGGAPDAPS FT PGPGGHVWLCHPDDCGSAPAGASSSHELRLHCGHLWLRGIF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056331" FT VAR_SEQ 416..509 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056332" FT VARIANT 55 FT /note="S -> R (in dbSNP:rs35198331)" FT /id="VAR_052503" FT VARIANT 78 FT /note="T -> S (in dbSNP:rs5434)" FT /id="VAR_012060" FT VARIANT 358 FT /note="A -> V (in dbSNP:rs8192702)" FT /id="VAR_020336" FT VARIANT 383 FT /note="V -> I (in T2D; dbSNP:rs121434581)" FT /evidence="ECO:0000269|PubMed:1521731, FT ECO:0000269|PubMed:1756912, ECO:0000269|PubMed:1918382" FT /id="VAR_007170" FT VARIANT 385 FT /note="I -> T (in dbSNP:rs775242206)" FT /evidence="ECO:0000269|PubMed:1397719" FT /id="VAR_007171" FT MUTAGEN 223 FT /note="C->S: Loss of palmitoylation." FT /evidence="ECO:0000269|PubMed:28057756" FT MUTAGEN 489..490 FT /note="LL->AA: Changes subcellular location mainly to the FT plasma membrane." FT /evidence="ECO:0000269|PubMed:8300557" FT CONFLICT 151..154 FT /note="Missing (in Ref. 2; AAA52569)" FT /evidence="ECO:0000305" FT HELIX 22..43 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 49..64 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 74..98 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 101..106 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 109..127 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 136..163 FT /evidence="ECO:0007829|PDB:7WSM" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7WSN" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 175..189 FT /evidence="ECO:0007829|PDB:7WSM" FT STRAND 192..196 FT /evidence="ECO:0007829|PDB:7WSM" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 202..208 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 210..219 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:7WSN" FT HELIX 229..233 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 238..248 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 254..269 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 275..279 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 285..299 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 303..316 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 322..343 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 350..372 FT /evidence="ECO:0007829|PDB:7WSM" FT TURN 373..376 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 380..397 FT /evidence="ECO:0007829|PDB:7WSM" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 402..410 FT /evidence="ECO:0007829|PDB:7WSM" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 416..445 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 449..467 FT /evidence="ECO:0007829|PDB:7WSM" FT HELIX 476..482 FT /evidence="ECO:0007829|PDB:7WSM" SQ SEQUENCE 509 AA; 54787 MW; 8E20CD97562C1EBF CRC64; MPSGFQQIGS EDGEPPQQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK VIEQSYNETW LGRQGPEGPS SIPPGTLTTL WALSVAIFSV GGMISSFLIG IISQWLGRKR AMLVNNVLAV LGGSLMGLAN AAASYEMLIL GRFLIGAYSG LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI VIGILIAQVL GLESLLGTAS LWPLLLGLTV LPALLQLVLL PFCPESPRYL YIIQNLEGPA RKSLKRLTGW ADVSGVLAEL KDEKRKLERE RPLSLLQLLG SRTHRQPLII AVVLQLSQQL SGINAVFYYS TSIFETAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR TLHLLGLAGM CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM AVAGFSNWTS NFIIGMGFQY VAEAMGPYVF LLFAVLLLGF FIFTFLRVPE TRGRTFDQIS AAFHRTPSLL EQEVKPSTEL EYLGPDEND //