GTR8_HUMAN
ID GTR8_HUMAN Reviewed; 477 AA.
AC Q9NY64; Q8WUZ9; Q9NSC4;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
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|HGNC:HGNC:13812};
GN Synonyms=GLUT8 {ECO:0000303|PubMed:10821868},
GN GLUTX1 {ECO:0000303|PubMed:10671487};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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:0000250|UniProtKB:Q9JJZ1}; 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: Highly expressed in testis, but not in testicular
CC carcinoma. Lower amounts present in most other tissues.
CC {ECO:0000269|PubMed:10821868}.
CC -!- INDUCTION: In testis, down-regulated by estrogen.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y17801; CAB89809.1; -; mRNA.
DR EMBL; AJ245937; CAB75702.1; -; mRNA.
DR EMBL; AL445222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87660.1; -; Genomic_DNA.
DR EMBL; BC019043; AAH19043.1; -; mRNA.
DR CCDS; CCDS6870.1; -.
DR RefSeq; NP_001258640.1; NM_001271711.1.
DR RefSeq; NP_001258641.1; NM_001271712.1.
DR RefSeq; NP_055395.2; NM_014580.4.
DR AlphaFoldDB; Q9NY64; -.
DR SMR; Q9NY64; -.
DR BioGRID; 119013; 46.
DR IntAct; Q9NY64; 10.
DR MINT; Q9NY64; -.
DR STRING; 9606.ENSP00000362469; -.
DR BindingDB; Q9NY64; -.
DR ChEMBL; CHEMBL4295964; -.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR TCDB; 2.A.1.1.89; the major facilitator superfamily (mfs).
DR GlyGen; Q9NY64; 1 site.
DR iPTMnet; Q9NY64; -.
DR PhosphoSitePlus; Q9NY64; -.
DR BioMuta; SLC2A8; -.
DR DMDM; 145559479; -.
DR EPD; Q9NY64; -.
DR jPOST; Q9NY64; -.
DR MassIVE; Q9NY64; -.
DR PaxDb; Q9NY64; -.
DR PeptideAtlas; Q9NY64; -.
DR PRIDE; Q9NY64; -.
DR ProteomicsDB; 83182; -.
DR Antibodypedia; 1986; 136 antibodies from 27 providers.
DR DNASU; 29988; -.
DR Ensembl; ENST00000373371.8; ENSP00000362469.3; ENSG00000136856.18.
DR GeneID; 29988; -.
DR KEGG; hsa:29988; -.
DR MANE-Select; ENST00000373371.8; ENSP00000362469.3; NM_014580.5; NP_055395.2.
DR UCSC; uc004bqu.5; human.
DR CTD; 29988; -.
DR DisGeNET; 29988; -.
DR GeneCards; SLC2A8; -.
DR HGNC; HGNC:13812; SLC2A8.
DR HPA; ENSG00000136856; Low tissue specificity.
DR MIM; 605245; gene.
DR neXtProt; NX_Q9NY64; -.
DR OpenTargets; ENSG00000136856; -.
DR PharmGKB; PA37813; -.
DR VEuPathDB; HostDB:ENSG00000136856; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000158795; -.
DR InParanoid; Q9NY64; -.
DR OMA; WNCILAF; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9NY64; -.
DR TreeFam; TF325324; -.
DR PathwayCommons; Q9NY64; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9NY64; -.
DR BioGRID-ORCS; 29988; 23 hits in 1081 CRISPR screens.
DR GenomeRNAi; 29988; -.
DR Pharos; Q9NY64; Tbio.
DR PRO; PR:Q9NY64; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NY64; protein.
DR Bgee; ENSG00000136856; Expressed in left testis and 152 other tissues.
DR ExpressionAtlas; Q9NY64; baseline and differential.
DR Genevisible; Q9NY64; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; TAS:Reactome.
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:0005536; F:glucose binding; IEA:Ensembl.
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:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
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 GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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..477
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 8"
FT /id="PRO_0000050375"
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..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 267..268
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 273
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 394
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 253
FT /note="I -> T (in dbSNP:rs34064803)"
FT /id="VAR_061880"
FT CONFLICT 377
FT /note="S -> N (in Ref. 2; CAB75702)"
FT /evidence="ECO:0000305"
FT CONFLICT 456..457
FT /note="LF -> FS (in Ref. 1; CAB89809)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="T -> I (in Ref. 2; CAB75702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 50819 MW; 0B480F94AF063316 CRC64;
MTPEDPEETQ PLLGPPGGSA PRGRRVFLAA FAAALGPLSF GFALGYSSPA IPSLQRAAPP
APRLDDAAAS WFGAVVTLGA AAGGVLGGWL VDRAGRKLSL LLCSVPFVAG FAVITAAQDV
WMLLGGRLLT GLACGVASLV APVYISEIAY PAVRGLLGSC VQLMVVVGIL LAYLAGWVLE
WRWLAVLGCV PPSLMLLLMC FMPETPRFLL TQHRRQEAMA ALRFLWGSEQ GWEDPPIGAE
QSFHLALLRQ PGIYKPFIIG VSLMAFQQLS GVNAVMFYAE TIFEEAKFKD SSLASVVVGV
IQVLFTAVAA LIMDRAGRRL LLVLSGVVMV FSTSAFGAYF KLTQGGPGNS SHVAISAPVS
AQPVDASVGL AWLAVGSMCL FIAGFAVGWG PIPWLLMSEI FPLHVKGVAT GICVLTNWLM
AFLVTKEFSS LMEVLRPYGA FWLASAFCIF SVLFTLFCVP ETKGKTLEQI TAHFEGR
