GTR2_BOVIN
ID GTR2_BOVIN Reviewed; 510 AA.
AC P58351; A6QPH3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
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:11599048};
GN Name=SLC2A2 {ECO:0000250|UniProtKB:P11168};
GN Synonyms=GLUT2 {ECO:0000303|PubMed:11599048};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 257-398.
RX PubMed=11599048; DOI=10.1002/mrd.1099;
RA Augustin R., Pocar P., Navarrete-Santos A., Wrenzycki C., Gandolfi F.,
RA Niemann H., Fischer B.;
RT "Glucose transporter expression is developmentally regulated in in vitro
RT derived bovine preimplantation embryos.";
RL Mol. Reprod. Dev. 60:370-376(2001).
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; BC149324; AAI49325.1; -; mRNA.
DR EMBL; AF308828; AAK63201.1; -; mRNA.
DR RefSeq; NP_001096692.1; NM_001103222.1.
DR AlphaFoldDB; P58351; -.
DR SMR; P58351; -.
DR STRING; 9913.ENSBTAP00000050612; -.
DR PaxDb; P58351; -.
DR Ensembl; ENSBTAT00000055725; ENSBTAP00000050612; ENSBTAG00000005386.
DR GeneID; 282357; -.
DR KEGG; bta:282357; -.
DR CTD; 6514; -.
DR VEuPathDB; HostDB:ENSBTAG00000005386; -.
DR VGNC; VGNC:34800; SLC2A2.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000155708; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P58351; -.
DR OMA; PQCIPMN; -.
DR OrthoDB; 430696at2759; -.
DR TreeFam; TF313762; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000005386; Expressed in liver and 23 other tissues.
DR ExpressionAtlas; P58351; baseline.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 2"
FT /id="PRO_0000050345"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 312..313
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 318
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 347
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 410
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 418
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 258
FT /note="L -> W (in Ref. 2; AAK63201)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="R -> G (in Ref. 2; AAK63201)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="N -> S (in Ref. 2; AAK63201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56060 MW; C91767EF2C079617 CRC64;
MTEDKVTGTL VLAVFTAVLS SFQFGYDIGV INAPQQVIIT HYRHVLGVSL DDRIAINNYA
LNSTEELPTS LGDPTPVSWA EEETMTSASL ITMFWSLSVS SFAVGGMIAS FFGGLLGDKL
GRIKALLVAN ILSLVGALLM GFSKLGPSHI LIISGRGISG LYCGLISGLI PMYIGEIAPT
TLRGAIGALH QLAIVTGILI SQIVGLDFIL GNHELWHILL GLSAVPAILQ CLLLFFCPES
PRYLYIKLDE EAKAKKSLKR LRGSDDITKD ITEMRKEREE ASNEKKVSII QLFTNASYRQ
PILVALMLHA AQQFSGINGI FYYSTSIFQT AGISQPVYAT IGVGAVNTVF TAVSVFLVEK
AGRRSLFLIG MSGMFVCAIF MSVGLVLLSK FPWMNYVSMT AIFLFVSFFE IGPGPIPWFM
VAEFFSQGPR PAALAIAAFS NWTGNFIIAL CFQYIADFCG PYVFFLLLVW SWPLFCSHFL
KFQKPKENPL RKSQQSSERR GVQLKRQKLL
