GLUT4_CANLF
ID GLUT4_CANLF Reviewed; 162 AA.
AC Q9XST2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 4 {ECO:0000305};
DE AltName: Full=Glucose transporter type 4, insulin-responsive {ECO:0000250|UniProtKB:P14672};
DE Short=GLUT-4 {ECO:0000250|UniProtKB:P14672};
DE Flags: Fragment;
GN Name=SLC2A4 {ECO:0000250|UniProtKB:P14672};
GN Synonyms=GLUT4 {ECO:0000250|UniProtKB:P14672};
GN ORFNames=B146 {ECO:0000303|PubMed:10964405};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
RX PubMed=10964405; DOI=10.1006/abio.2000.4674;
RA Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D.;
RT "A method for the large-scale cloning of nuclear proteins and nuclear
RT targeting sequences on a functional basis.";
RL Anal. Biochem. 284:231-239(2000).
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: Binds to DAXX. Interacts via its N-terminus with SRFBP1 (By
CC similarity). Interacts with NDUFA9 (By similarity). Interacts with
CC TRARG1; the interaction is required for proper SLC2A4 recycling after
CC insulin stimulation (By similarity). {ECO:0000250|UniProtKB:P14142,
CC ECO:0000250|UniProtKB:P14672, ECO:0000250|UniProtKB:P19357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14142};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}.
CC Endomembrane system {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P14142}. 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 (By similarity). The
CC dileucine internalization motif is critical for intracellular
CC sequestration (By similarity). Insulin stimulation induces
CC translocation to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672}.
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 -!- 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}.
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DR EMBL; AJ388533; CAB46835.1; -; mRNA.
DR RefSeq; NP_001152799.1; NM_001159327.1.
DR STRING; 9612.ENSCAFP00000023753; -.
DR PaxDb; Q9XST2; -.
DR GeneID; 403673; -.
DR KEGG; cfa:403673; -.
DR CTD; 6517; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; Q9XST2; -.
DR OrthoDB; 749998at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS: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:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
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:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
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; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN <1..>162
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 4"
FT /id="PRO_0000050362"
FT TOPO_DOM <1..13
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..>162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 86
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 94
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT NON_TER 1
FT NON_TER 162
SQ SEQUENCE 162 AA; 17454 MW; 0C58CBB23C6AD2BB CRC64;
TSIFETAGVG QPAYATIGAG VVNTVFTLVS VFLVERAGRR TLHLLGLAGM CGCAILMTIA
LLLLERLPAM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM AVAGFCNWTS
NFIIGMGFQY IAXAMGPYVF LLFAVLLLAF FIFTFLKVPE TR
