GTR2_PIG
ID GTR2_PIG Reviewed; 524 AA.
AC O62786; I3LNT8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 91.
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:0000250|UniProtKB:P11168};
GN Name=SLC2A2 {ECO:0000250|UniProtKB:P11168};
GN Synonyms=GLUT2 {ECO:0000250|UniProtKB:P11168};
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 [LARGE SCALE MRNA].
RX PubMed=30723633; DOI=10.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 378-497.
RA Canty J.M., Young R.F., Fallavollita J.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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; may comprise part
CC of the glucose-sensing mechanism of the beta cell. May also participate
CC with the Na(+)/glucose cotransporter in the transcellular transport of
CC glucose in the small intestine and kidney. Also able to mediate the
CC transport of dehydroascorbate. {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 -!- PTM: N-glycosylated; required for stability and retention at the cell
CC surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}.
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; DQIR01026554; HCZ82029.1; -; mRNA.
DR EMBL; AEMK02000089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF054835; AAC12737.1; -; mRNA.
DR AlphaFoldDB; O62786; -.
DR SMR; O62786; -.
DR STRING; 9823.ENSSSCP00000025763; -.
DR PaxDb; O62786; -.
DR Ensembl; ENSSSCT00015007461; ENSSSCP00015002985; ENSSSCG00015005572.
DR Ensembl; ENSSSCT00030014685; ENSSSCP00030006595; ENSSSCG00030010642.
DR Ensembl; ENSSSCT00040074016; ENSSSCP00040031727; ENSSSCG00040054435.
DR Ensembl; ENSSSCT00045028790; ENSSSCP00045019927; ENSSSCG00045016833.
DR Ensembl; ENSSSCT00050037499; ENSSSCP00050015571; ENSSSCG00050027864.
DR Ensembl; ENSSSCT00055033225; ENSSSCP00055026460; ENSSSCG00055016698.
DR Ensembl; ENSSSCT00070046626; ENSSSCP00070039339; ENSSSCG00070023372.
DR eggNOG; KOG0569; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; O62786; -.
DR OMA; PQCIPMN; -.
DR TreeFam; TF313762; -.
DR Reactome; R-SSC-189200; Cellular hexose transport.
DR Reactome; R-SSC-422356; Regulation of insulin secretion.
DR Reactome; R-SSC-8981373; Intestinal hexose absorption.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 13.
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; -; 1.
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; Phosphoprotein; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..524
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050349"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..89
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..150
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..239
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..338
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..360
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..389
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..394
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..413
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..458
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..463
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..482
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 193
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 314..315
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 320
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 349
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 412
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 420
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11168"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 446
FT /note="C -> R (in Ref. 3; AAC12737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57263 MW; C5379AB7ABA07833 CRC64;
MTEDKITGTL VFAVLTAVLG SFQFGYDIGV INAPQQVIIT HYRHVLGVPL DDRKAINSYA
INSTEELPTG PYPGDPTPTS WAEEETTASA SLIIMLWSLS VSIFAIGGMI ASFFGGMLGD
RLGRIKAMLV ANILSLVGAL LMWFSKLGPS HILIISGRGI SGLYCGLISG LVPMYIGEIA
PTKFRGAIGA LHQLAIVTGI LVSQIIGLDF LLGNHELWHI LLGLSAVPAV LQSLMLFFCP
ESPRYLYIKL DEEAKARKSL KKLRGSDDVT KDITEMRKER EEASSEKKVS IIQLFTNSSY
RQPILVALML HMAQQFSGIN GIFYYSTSIF QTAGISQPVY ATIGVGAINT IFTALSVFLV
EKAGRRSLFL IGMSGMFVCA IFMSVGLVLL DKLPWMSYVS MTAIFLFVSF FEIGPGPIPW
FMVAEFFSQG PRPAALAMAA FSNWTCNFII ALCFQYIADF CGPYVFFLFA GVVLVFTLFT
FFKVPETKGK SFEEIAAEFQ KKSGSAQSPK AAVEMEFLGA TETV
