GTR8_RAT
ID GTR8_RAT Reviewed; 478 AA.
AC Q9JJZ1; Q9JMA6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 8 {ECO:0000305};
DE AltName: Full=Glucose transporter type 8 {ECO:0000303|PubMed:10821868};
DE Short=GLUT-8 {ECO:0000303|PubMed:10821868};
DE AltName: Full=Glucose transporter type X1 {ECO:0000303|PubMed:10671487};
GN Name=Slc2a8 {ECO:0000312|RGD:620611};
GN Synonyms=Glut8 {ECO:0000303|PubMed:10821868},
GN Glutx1 {ECO:0000303|PubMed:10671487};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 12-LEU-LEU-13.
RC TISSUE=Testis;
RX PubMed=10671487; DOI=10.1074/jbc.275.7.4607;
RA Ibberson M.R., Uldry M.A., Thorens B.;
RT "GLUTX1, a novel mammalian glucose transporter expressed in the central
RT nervous system and insulin-sensitive tissues.";
RL J. Biol. Chem. 275:4607-4612(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Ishibashi K.;
RT "Molecular cloning of a new putative glucose transporter.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10821868; DOI=10.1074/jbc.275.21.16275;
RA Doege H., Schuermann A., Bahrenberg G., Brauers A., Joost H.-G.;
RT "GLUT8, a novel member of the sugar transport facilitator family with
RT glucose transport activity.";
RL J. Biol. Chem. 275:16275-16280(2000).
RN [4]
RP FUNCTION.
RX PubMed=23396969; DOI=10.1074/jbc.m112.436790;
RA Corpe C.P., Eck P., Wang J., Al-Hasani H., Levine M.;
RT "Intestinal dehydroascorbic acid (DHA) transport mediated by the
RT facilitative sugar transporters, GLUT2 and GLUT8.";
RL J. Biol. Chem. 288:9092-9101(2013).
CC -!- FUNCTION: Insulin-regulated facilitative hexose transporter that
CC mediates the transport of glucose and fructose (PubMed:10671487). Also
CC able to mediate the transport of dehydroascorbate (PubMed:23396969).
CC {ECO:0000269|PubMed:10671487, ECO:0000269|PubMed:23396969}.
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:0000269|PubMed:10671487}.
CC -!- SUBUNIT: Interacts with AP2B1. {ECO:0000250|UniProtKB:Q9JIF3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10671487};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10671487}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Principally intracellular (PubMed:10671487). May
CC move between intracellular vesicles and the plasma membrane
CC (PubMed:10671487). The dileucine internalization motif is critical for
CC intracellular sequestration (PubMed:10671487).
CC {ECO:0000269|PubMed:10671487}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult and pubertal testis, but
CC not prepubertal testis (PubMed:10821868). Moderate expression in
CC hypothalamus, cerebellum, brainstem, hippocampus, and adrenal gland
CC (PubMed:10821868). Lower amounts present in most other tissues
CC (PubMed:10821868). {ECO:0000269|PubMed:10821868}.
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; AJ245935; CAB75729.1; -; mRNA.
DR EMBL; AB033418; BAA94383.1; -; mRNA.
DR RefSeq; NP_445946.2; NM_053494.2.
DR AlphaFoldDB; Q9JJZ1; -.
DR SMR; Q9JJZ1; -.
DR STRING; 10116.ENSRNOP00000022326; -.
DR GlyGen; Q9JJZ1; 1 site.
DR jPOST; Q9JJZ1; -.
DR PaxDb; Q9JJZ1; -.
DR GeneID; 85256; -.
DR KEGG; rno:85256; -.
DR UCSC; RGD:620611; rat.
DR CTD; 29988; -.
DR RGD; 620611; Slc2a8.
DR VEuPathDB; HostDB:ENSRNOG00000022274; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9JJZ1; -.
DR OMA; WNCILAF; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9JJZ1; -.
DR TreeFam; TF325324; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9JJZ1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000022274; Expressed in testis and 20 other tissues.
DR Genevisible; Q9JJZ1; RN.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; ISO:RGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0007141; P:male meiosis I; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein 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_0000050377"
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..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..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..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..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 MOTIF 12..13
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000269|PubMed:10671487"
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 MUTAGEN 12..13
FT /note="LL->AA: Changes subcellular location mainly to the
FT plasma membrane, threreby increasing transport activity."
FT /evidence="ECO:0000269|PubMed:10671487"
FT CONFLICT 83..84
FT /note="GG -> QGA (in Ref. 2; BAA94383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 51459 MW; 95841FC1F18C9EE9 CRC64;
MSPEDPQETQ PLLRSPGARA PGGRRVFLAT FAAALGPLSF GFALGYSSPA IPSLRRTAPP
ALRLGDTAAS WFGAVVTLGA AAGGVLGGWL LDRAGRKLSL LLCTVPFVTG FAVITAARDV
WMLLGGRLLT GLACGVASLV APVYISEIAY PAVRGLLGSC VQLMVVTGIL LAYVAGWVLE
WRWLAVLGCV PPTLMLLLMC YMPETPRFLL TQHQYQEAMA ALRFLWGSEE GWEEPPVGAE
HQGFQLAMLR RPGVHKPLII GICLMVFQQL SGVNAIMFYA NTIFEEAKFK DSSLASVTVG
IIQVLFTAVA ALIMDRAGRK LLLALSGVIM VFSMSAFGTY FKLTQSGPSN SSHVGLLVPI
SAEPADVHLG LAWLAVGSMC LFIAGFAVGW GPIPWLLMSE IFPLHIKGVA TGVCVLTNWF
MAFLVTKEFN SIMEILRPYG AFWLTAAFCI LSVLFTLTFV PETKGRTLEQ ITAHFEGR
