GTR2_CHICK
ID GTR2_CHICK Reviewed; 533 AA.
AC Q90592;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 2 {ECO:0000305};
DE AltName: Full=Glucose transporter type 2, liver {ECO:0000250|UniProtKB:P11168};
DE Short=GLUT-2 {ECO:0000303|PubMed:8161202};
GN Name=SLC2A2 {ECO:0000250|UniProtKB:P11168};
GN Synonyms=GLUT2 {ECO:0000303|PubMed:8161202};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8161202; DOI=10.1006/abbi.1994.1154;
RA Wang M.Y., Tsai M.Y., Wang C.;
RT "Identification of chicken liver glucose transporter.";
RL Arch. Biochem. Biophys. 310:172-179(1994).
CC -!- FUNCTION: Facilitative hexose transporter that mediates the transport
CC of glucose, fructose and galactose. Likely mediates the bidirectional
CC transfer of glucose across the plasma membrane of hepatocytes and is
CC responsible for uptake of glucose by the beta cells.
CC {ECO:0000250|UniProtKB:P11168}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915,
CC ChEBI:CHEBI:4139; Evidence={ECO:0000250|UniProtKB:P11168};
CC -!- ACTIVITY REGULATION: D-glucose and maltose competitively inhibit
CC fructose transport. D-glucose, D-fructose and maltose inhibit
CC deoxyglucose transport. {ECO:0000250|UniProtKB:P11168}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11168};
CC Multi-pass membrane protein {ECO:0000255}.
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; Z22932; CAA80519.1; -; mRNA.
DR PIR; S43230; S43230.
DR RefSeq; NP_997061.1; NM_207178.1.
DR AlphaFoldDB; Q90592; -.
DR SMR; Q90592; -.
DR STRING; 9031.ENSGALP00000015129; -.
DR PaxDb; Q90592; -.
DR GeneID; 396272; -.
DR KEGG; gga:396272; -.
DR CTD; 6514; -.
DR VEuPathDB; HostDB:geneid_396272; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; Q90592; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q90592; -.
DR Reactome; R-GGA-352832; Glucose transport.
DR PRO; PR:Q90592; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central.
DR GO; GO:0015755; P:fructose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015757; P:galactose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
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; -; 2.
DR InterPro; IPR002440; Glc_transpt_2.
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; PR01191; GLUCTRSPORT2.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..533
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050350"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 205
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 326..327
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 332
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 361
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 424
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 432
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 533 AA; 57699 MW; D06284CDC2779A3D CRC64;
MDGKSKMQAE KHLTGTLVLS VFTAVLGFFQ YGYSLGVINA PQKVIEAHYG RMLGAIPMVR
HATNTSRDNA TITVTIPGTE AWGSSEGTLA PSAGFEDPTV SPHILTMYWS LSVSMFAVGG
MVSSFTVGWI GDRLGRVKAM LVVNVLSIAG NLLMGLAKMG PSHILIIAGR AITGLYCGLS
SGLVPMYVSE VSPTALRGAL GTLHQLAIVT GILISQVLGL DFLLGNDELW PLLLGLSGVA
ALLQFFLLLL CPESPRYLYI KLGKVEEAKK SLKRLRGNCD PMKEIAEMEK EKQEAASEKR
VSIGQLFSSS KYRQAVIVAL MVQISQQFSG INAIFYYSTN IFQRAGVGQP VYATIGVGVV
NTVFTVISVF LVEKAGRRSL FLAGLMGMLI SAVAMTVGLV LLSQFAWMSY VSMVAIFLFV
IFFEVGPGPI PWFIVAELFS QGPRPAAIAV AGFCNWACNF IVGMCFQYIA DLCGPYVFVV
FAVLLLVFFL FAYLKVPETK GKSFEEIAAA FRRKKLPAKS MTELEDLRGG EEA
