GLUT4_HUMAN
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 03-AUG-2022, entry version 233.
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 NIDDM 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 NIDDM 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 NIDDM 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; 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: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]:
CC A multifactorial disorder of glucose homeostasis caused by a lack of
CC sensitivity to the body's own insulin. Affected individuals usually
CC have an obese body habitus and manifestations of a metabolic syndrome
CC characterized by diabetes, insulin resistance, hypertension and
CC hypertriglyceridemia. The disease results in long-term complications
CC that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:1521731, ECO:0000269|PubMed:1756912,
CC ECO:0000269|PubMed:1918382}. Note=The disease may be caused by variants
CC affecting the gene represented in 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";
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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_001042.2. [P14672-1]
DR AlphaFoldDB; P14672; -.
DR SMR; P14672; -.
DR BioGRID; 112408; 60.
DR CORUM; P14672; -.
DR IntAct; P14672; 5.
DR MINT; P14672; -.
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 GlyGen; P14672; 1 site.
DR iPTMnet; P14672; -.
DR PhosphoSitePlus; P14672; -.
DR SwissPalm; P14672; -.
DR BioMuta; SLC2A4; -.
DR DMDM; 121761; -.
DR EPD; P14672; -.
DR jPOST; P14672; -.
DR MassIVE; P14672; -.
DR PaxDb; P14672; -.
DR PeptideAtlas; P14672; -.
DR PRIDE; P14672; -.
DR ProteomicsDB; 53073; -. [P14672-1]
DR ProteomicsDB; 58372; -.
DR Antibodypedia; 4297; 799 antibodies from 46 providers.
DR DNASU; 6517; -.
DR Ensembl; ENST00000317370.13; ENSP00000320935.8; ENSG00000181856.15. [P14672-1]
DR Ensembl; ENST00000572485.5; ENSP00000461086.1; ENSG00000181856.15. [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 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 neXtProt; NX_P14672; -.
DR OpenTargets; ENSG00000181856; -.
DR PharmGKB; PA35879; -.
DR VEuPathDB; HostDB:ENSG00000181856; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000160688; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P14672; -.
DR OMA; KVQWRFF; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P14672; -.
DR TreeFam; TF313762; -.
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 BioGRID-ORCS; 6517; 9 hits in 1071 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 tissues.
DR ExpressionAtlas; P14672; baseline and differential.
DR Genevisible; P14672; HS.
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; ISS: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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
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:0010021; P:amylopectin biosynthetic process; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
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:0071470; P:cellular response to osmotic stress; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IDA:BHF-UCL.
DR GO; GO:0046323; P:glucose import; NAS:BHF-UCL.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; 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:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
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 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 Alternative splicing; Cell membrane; Cytoplasm; Diabetes mellitus;
KW Disease variant; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport; 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 NIDDM; 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"
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
