GTR8_BOVIN
ID GTR8_BOVIN Reviewed; 478 AA.
AC P58354; Q1RMN1; Q6XUI2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 8 {ECO:0000305};
DE AltName: Full=Glucose transporter type 8 {ECO:0000303|PubMed:15488990};
DE Short=GLUT-8 {ECO:0000303|PubMed:15488990};
DE AltName: Full=Glucose transporter type X1 {ECO:0000250|UniProtKB:Q9NY64};
GN Name=SLC2A8 {ECO:0000250|UniProtKB:Q9NY64};
GN Synonyms=GLUT8 {ECO:0000303|PubMed:15488990},
GN GLUTX1 {ECO:0000250|UniProtKB:Q9NY64};
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 [MRNA], TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Kidney;
RX PubMed=15488990; DOI=10.1016/j.bbaexp.2004.09.001;
RA Zhao F.-Q., Miller P.J., Wall E.H., Zheng Y.-C., Dong B., Neville M.C.,
RA McFadden T.B.;
RT "Bovine glucose transporter GLUT8: cloning, expression, and developmental
RT regulation in mammary gland.";
RL Biochim. Biophys. Acta 1680:103-113(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-478.
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: Insulin-regulated facilitative hexose transporter that
CC mediates the transport of glucose and fructose. Also able to mediate
CC the transport of dehydroascorbate. {ECO:0000250|UniProtKB:Q9JIF3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:Q9JIF3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:Q9JIF3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF3};
CC -!- ACTIVITY REGULATION: Inhibited by cytochalasin B.
CC {ECO:0000250|UniProtKB:Q9JIF3}.
CC -!- SUBUNIT: Interacts with AP2B1. {ECO:0000250|UniProtKB:Q9JIF3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JJZ1};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:15488990}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Principally intracellular. May move between
CC intracellular vesicles and the plasma membrane. The dileucine
CC internalization motif is critical for intracellular sequestration.
CC {ECO:0000250|UniProtKB:Q9JJZ1}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis and more moderately
CC in lung, kidney, spleen, intestine, skeletal muscle, liver and mammary
CC gland. {ECO:0000269|PubMed:15488990}.
CC -!- INDUCTION: Up-regulated during pregnancy and lactation.
CC {ECO:0000269|PubMed:15488990}.
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; AY208940; AAP43920.1; -; mRNA.
DR EMBL; BC114811; AAI14812.1; -; mRNA.
DR EMBL; AF321324; AAK69606.1; -; mRNA.
DR RefSeq; NP_963286.1; NM_201528.1.
DR AlphaFoldDB; P58354; -.
DR SMR; P58354; -.
DR STRING; 9913.ENSBTAP00000009144; -.
DR PaxDb; P58354; -.
DR PRIDE; P58354; -.
DR GeneID; 282867; -.
DR KEGG; bta:282867; -.
DR CTD; 29988; -.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; P58354; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0070837; P:dehydroascorbic acid transport; ISS:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
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 Pfam; PF00083; Sugar_tr; 1.
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; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..478
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 8"
FT /id="PRO_0000050374"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..13
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000250|UniProtKB:Q9JJZ1"
FT BINDING 162
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 268..269
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 274
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 395
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="P -> A (in Ref. 3; AAK69606)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="S -> N (in Ref. 3; AAK69606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 51417 MW; CBE71D4ABCBAC4CA CRC64;
MTPEDQEETQ PLLRPPGGSA PRGRRVFLAA FAAALGPLSF GFALGYSSPA IPSLRRAAPP
APHLDEDAAS WFGAIVTLGA AAGGVLGGWL LDRAGRKLSL VLCALPFVAG FAVITAAQNL
WMLLGGRLLT GLACGIASLV APVYISEIAY PEVRGLLGSC VQLMVVTGIL LAYLAGWVLE
WRWLAVLGCV PPSFMLLLMC FMPETPRFLL SQHKHQEAMA AMQFLWGYAQ GWEEPPLGAQ
HQDFHVAQLR RPGVYKPFII GISLMAFQQL SGVNAVMFYA ETIFEEAKFK DSSLASVVVG
VIQVLFTATA ALIMDRAGRR LLLTLSGVVM VFSTSAFGTY FKLTEGGPSN SSHVDLPALV
SMEAADTNVG LAWLAVGSMC LFIAGFAVGW GPIPWLLMSE IFPLHVKGVA TGVCVLTNWF
MAFLVTKEFS SLMEVLRPYG AFWLASAFCI FGVLFTLACV PETKGKTLEQ ITAHFEGR
