GLUT4_PIG
ID GLUT4_PIG Reviewed; 174 AA.
AC Q9XT10;
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};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10784183; DOI=10.2527/2000.784934x;
RA McNeel R.L., Ding S.T., Smith E.O., Mersmann H.J.;
RT "Effect of feed restriction on adipose tissue transcript concentrations in
RT genetically lean and obese pigs.";
RL J. Anim. Sci. 78:934-942(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; AF141956; AAD38524.1; -; mRNA.
DR AlphaFoldDB; Q9XT10; -.
DR SMR; Q9XT10; -.
DR STRING; 9823.ENSSSCP00000018998; -.
DR PaxDb; Q9XT10; -.
DR eggNOG; KOG0569; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9XT10; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q9XT10; SS.
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; 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 PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN <1..>174
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 4"
FT /id="PRO_0000050365"
FT TOPO_DOM <1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..>174
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT REGION 2..8
FT /note="Interaction with SRFBP1"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19357"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 174
SQ SEQUENCE 174 AA; 18208 MW; 988C9FD312FA23D8 CRC64;
QQIGSEDGEP PQQRVTGTLV LAVFSAVLGS LQFGYNIGVI NAPQKVIEQS YNETWLGRQG
PNGPGSIPPG TLTTLWALSV AIFSVGGMFS SFLLGIISQW LGRKKAMLFN NTLAVLAGAL
MGLAKAAASY EMLILGRFLI GAYSGLASGL VPMYVGEIAP THLRGALGTL NQLA
