GTR6_MOUSE
ID GTR6_MOUSE Reviewed; 497 AA.
AC Q3UDF0; A2AR26; Q3TLU5; Q8BTN2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 6 {ECO:0000305};
DE AltName: Full=Glucose transporter type 6 {ECO:0000303|PubMed:29664675};
DE Short=GLUT-6 {ECO:0000303|PubMed:29664675};
GN Name=Slc2a6 {ECO:0000312|MGI:MGI:2443286};
GN Synonyms=Glut6 {ECO:0000303|PubMed:29664675};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=29664675; DOI=10.1152/ajpendo.00082.2018;
RA Byrne F.L., Olzomer E.M., Brink R., Hoehn K.L.;
RT "Knockout of glucose transporter GLUT6 has minimal effects on whole body
RT metabolic physiology in mice.";
RL Am. J. Physiol. 315:E286-E293(2018).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30431159; DOI=10.1002/1873-3468.13298;
RA Maedera S., Mizuno T., Ishiguro H., Ito T., Soga T., Kusuhara H.;
RT "GLUT6 is a lysosomal transporter that is regulated by inflammatory stimuli
RT and modulates glycolysis in macrophages.";
RL FEBS Lett. 593:195-208(2019).
CC -!- FUNCTION: Probable sugar transporter that acts as a regulator of
CC glycolysis in macrophages (PubMed:30431159). Does not transport glucose
CC (By similarity). {ECO:0000250|UniProtKB:Q9UGQ3,
CC ECO:0000269|PubMed:30431159}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9UGQ3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UDF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UDF0-2; Sequence=VSP_060214;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain and spleen
CC (PubMed:29664675). Also expressed in lung, heart, muscle, liver,
CC kidney, fat, whole blood, testes, ovaries and uterus (PubMed:29664675).
CC {ECO:0000269|PubMed:29664675}.
CC -!- DISRUPTION PHENOTYPE: Mild metabolic effects (PubMed:29664675,
CC PubMed:30431159). Mice grow normally and glucose metabolism in male or
CC female mice is normal (PubMed:29664675). Minimal metabolic effects are
CC observed: female mice display a minor decrease in fat accumulation when
CC fed Western diet and have a lower respiratory exchange ratio when fed
CC chow diet (PubMed:29664675). Mice also exhibit a subtle phenotype in
CC response to lipopolysaccharide administration, characterized by slight
CC changes in the metabolome associated with glycolysis (PubMed:30431159).
CC {ECO:0000269|PubMed:29664675, ECO:0000269|PubMed:30431159}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {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; AK089246; BAC40811.1; -; mRNA.
DR EMBL; AK150104; BAE29311.1; -; mRNA.
DR EMBL; AK166312; BAE38697.1; -; mRNA.
DR EMBL; AL845266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08351.1; -; Genomic_DNA.
DR EMBL; BC141168; AAI41169.1; -; mRNA.
DR CCDS; CCDS15822.1; -. [Q3UDF0-1]
DR CCDS; CCDS50544.1; -. [Q3UDF0-2]
DR RefSeq; NP_001171098.1; NM_001177627.1. [Q3UDF0-2]
DR RefSeq; NP_766247.2; NM_172659.2. [Q3UDF0-1]
DR AlphaFoldDB; Q3UDF0; -.
DR SMR; Q3UDF0; -.
DR STRING; 10090.ENSMUSP00000049103; -.
DR GlyGen; Q3UDF0; 2 sites.
DR iPTMnet; Q3UDF0; -.
DR PhosphoSitePlus; Q3UDF0; -.
DR MaxQB; Q3UDF0; -.
DR PaxDb; Q3UDF0; -.
DR PRIDE; Q3UDF0; -.
DR ProteomicsDB; 330692; -. [Q3UDF0-1]
DR ProteomicsDB; 340807; -.
DR Antibodypedia; 18448; 131 antibodies from 21 providers.
DR DNASU; 227659; -.
DR Ensembl; ENSMUST00000045702; ENSMUSP00000049103; ENSMUSG00000036067. [Q3UDF0-1]
DR Ensembl; ENSMUST00000102890; ENSMUSP00000099954; ENSMUSG00000036067. [Q3UDF0-2]
DR GeneID; 227659; -.
DR KEGG; mmu:227659; -.
DR UCSC; uc008iwv.1; mouse. [Q3UDF0-1]
DR UCSC; uc008iww.1; mouse.
DR CTD; 11182; -.
DR MGI; MGI:2443286; Slc2a6.
DR VEuPathDB; HostDB:ENSMUSG00000036067; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000159976; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q3UDF0; -.
DR OMA; VMVVFAC; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q3UDF0; -.
DR TreeFam; TF325324; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR BioGRID-ORCS; 227659; 6 hits in 76 CRISPR screens.
DR PRO; PR:Q3UDF0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UDF0; protein.
DR Bgee; ENSMUSG00000036067; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; Q3UDF0; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:UniProtKB.
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; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..497
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 6"
FT /id="PRO_0000447625"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..80
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..138
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..312
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 313..333
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..358
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..385
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..406
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 448..468
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 5..6
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT BINDING 173
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 284..285
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 408
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 343..397
FT /note="SASVMFAANLTLGLYVQFVPRPLTPNSTVEIVTLGDTAFNYLTLIPLLATML
FT FIM -> S (in isoform 2)"
FT /id="VSP_060214"
FT CONFLICT 8
FT /note="T -> A (in Ref. 1; BAE38697)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="T -> I (in Ref. 1; BAC40811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54433 MW; 9FE4DD2CC9B244E3 CRC64;
MQEPLLRTEG LDYDTFPEVP ATPGERERAG ALKNRRVFLA TFAAVLGNFS FGYALVYTSP
VIPELKLSSD PALHLDKIQA SWFGSVFTLG AAAGGLSAML LNDLLGRKLS IMFSAVPSAI
GYAIMAGARG LWMLLLGRML TGFAGGLTAA CIPVYVSEIA PPDVRGALGA TPQLMAVFGS
LSLYALGLLL PWRWLAVAGE GPVLIMILLL SFMPNSPRFL LSKSRDEEAL QALTWLRADS
EVHWEFEQIQ DNVRRQSSRV SWAEAREPRV YRPVLIAVLM RFLQQLTGIT PILVYLQTIF
DNTSVVLPSQ QDAAIVGAVR LLSVLIAAVT MDLAGRKVLL YVSASVMFAA NLTLGLYVQF
VPRPLTPNST VEIVTLGDTA FNYLTLIPLL ATMLFIMGYA MGWGPITWLL MSEVLPLRAR
GVASGLCVLV SWLTAFVLTN YFLLAVNAFG LQVPFFFFSA ICLLSLLFTG CCVPETRGRS
LEQIEAFFHT RRMSFRP
