GTR6_HUMAN
ID GTR6_HUMAN Reviewed; 507 AA.
AC Q9UGQ3; A6NNU6; Q5SXD7; Q8NCC2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 6 {ECO:0000305};
DE AltName: Full=Glucose transporter type 6 {ECO:0000303|PubMed:30431159};
DE Short=GLUT-6 {ECO:0000303|PubMed:30431159};
GN Name=SLC2A6 {ECO:0000312|HGNC:HGNC:11011};
GN Synonyms=GLUT6 {ECO:0000303|PubMed:30431159};
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP MET-500.
RC TISSUE=Leukocyte;
RX PubMed=10970791; DOI=10.1042/bj3500771;
RA Doege H., Bocianski A., Joost H.-G., Schuermann A.;
RT "Activity and genomic organization of human glucose transporter 9 (GLUT9),
RT a novel member of the family of sugar-transport facilitators predominantly
RT expressed in brain and leucocytes.";
RL Biochem. J. 350:771-776(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-500.
RC TISSUE=Lymphoid tissue;
RA Young J.M., Woodward K.J., Aziz S., Burley M., Kwiatkowski D.J., Povey S.;
RT "Cloning of a sugar transporter gene, a G-beta subunit like gene and three
RT novel genes in human chromosome 9q34.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
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 (Probable). Does not transport glucose
CC (PubMed:30431159). {ECO:0000269|PubMed:30431159,
CC ECO:0000305|PubMed:30431159}.
CC -!- INTERACTION:
CC Q9UGQ3; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-18004831, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:30431159};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGQ3-2; Sequence=VSP_041402;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, spleen and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:10970791}.
CC -!- INDUCTION: By lipopolysaccharide (LPS). {ECO:0000269|PubMed:30431159}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially thought to act as a glucose transporter
CC (PubMed:10970791). However, later studies demonstrated that it does not
CC transport glucose (PubMed:30431159). {ECO:0000269|PubMed:10970791,
CC ECO:0000269|PubMed:30431159}.
CC -!- CAUTION: Was named GLUT9 by a report, but this gene name has already
CC been used for SLC2A9. {ECO:0000305|PubMed:10970791}.
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DR EMBL; Y17803; CAB96996.1; -; mRNA.
DR EMBL; AJ011372; CAB66155.1; -; mRNA.
DR EMBL; AK074927; BAC11297.1; -; mRNA.
DR EMBL; AK222919; BAD96639.1; -; mRNA.
DR EMBL; AK074836; BAC11235.1; -; mRNA.
DR EMBL; AL593848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88093.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88094.1; -; Genomic_DNA.
DR EMBL; BC013740; AAH13740.1; -; mRNA.
DR CCDS; CCDS48052.1; -. [Q9UGQ3-2]
DR CCDS; CCDS6975.1; -. [Q9UGQ3-1]
DR RefSeq; NP_001138571.1; NM_001145099.1. [Q9UGQ3-2]
DR RefSeq; NP_060055.2; NM_017585.3. [Q9UGQ3-1]
DR AlphaFoldDB; Q9UGQ3; -.
DR SMR; Q9UGQ3; -.
DR BioGRID; 116352; 20.
DR IntAct; Q9UGQ3; 7.
DR MINT; Q9UGQ3; -.
DR STRING; 9606.ENSP00000360966; -.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR TCDB; 2.A.1.1.88; the major facilitator superfamily (mfs).
DR GlyGen; Q9UGQ3; 1 site.
DR iPTMnet; Q9UGQ3; -.
DR PhosphoSitePlus; Q9UGQ3; -.
DR SwissPalm; Q9UGQ3; -.
DR BioMuta; SLC2A6; -.
DR DMDM; 150421565; -.
DR EPD; Q9UGQ3; -.
DR jPOST; Q9UGQ3; -.
DR MassIVE; Q9UGQ3; -.
DR MaxQB; Q9UGQ3; -.
DR PaxDb; Q9UGQ3; -.
DR PeptideAtlas; Q9UGQ3; -.
DR PRIDE; Q9UGQ3; -.
DR ProteomicsDB; 84259; -. [Q9UGQ3-1]
DR ProteomicsDB; 84260; -. [Q9UGQ3-2]
DR Antibodypedia; 18448; 131 antibodies from 21 providers.
DR DNASU; 11182; -.
DR Ensembl; ENST00000371897.8; ENSP00000360964.4; ENSG00000160326.14. [Q9UGQ3-2]
DR Ensembl; ENST00000371899.9; ENSP00000360966.4; ENSG00000160326.14. [Q9UGQ3-1]
DR Ensembl; ENST00000625425.2; ENSP00000486637.1; ENSG00000281165.3. [Q9UGQ3-2]
DR Ensembl; ENST00000626271.3; ENSP00000487067.1; ENSG00000281165.3. [Q9UGQ3-1]
DR GeneID; 11182; -.
DR KEGG; hsa:11182; -.
DR MANE-Select; ENST00000371899.9; ENSP00000360966.4; NM_017585.4; NP_060055.2.
DR UCSC; uc004cee.4; human. [Q9UGQ3-1]
DR CTD; 11182; -.
DR DisGeNET; 11182; -.
DR GeneCards; SLC2A6; -.
DR HGNC; HGNC:11011; SLC2A6.
DR HPA; ENSG00000160326; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 606813; gene.
DR neXtProt; NX_Q9UGQ3; -.
DR OpenTargets; ENSG00000160326; -.
DR PharmGKB; PA35881; -.
DR VEuPathDB; HostDB:ENSG00000160326; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000159976; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9UGQ3; -.
DR OMA; VMVVFAC; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9UGQ3; -.
DR TreeFam; TF325324; -.
DR PathwayCommons; Q9UGQ3; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR SignaLink; Q9UGQ3; -.
DR BioGRID-ORCS; 11182; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; SLC2A6; human.
DR GeneWiki; SLC2A6; -.
DR GenomeRNAi; 11182; -.
DR Pharos; Q9UGQ3; Tbio.
DR PRO; PR:Q9UGQ3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UGQ3; protein.
DR Bgee; ENSG00000160326; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q9UGQ3; baseline and differential.
DR Genevisible; Q9UGQ3; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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: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; 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: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; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..507
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 6"
FT /id="PRO_0000050373"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..462
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..6
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT BINDING 174
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 286..287
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 418
FT /ligand="D-hexose"
FT /ligand_id="ChEBI:CHEBI:4194"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 346..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_041402"
FT VARIANT 500
FT /note="T -> M (in dbSNP:rs3094378)"
FT /evidence="ECO:0000269|PubMed:10970791, ECO:0000269|Ref.2"
FT /id="VAR_025426"
SQ SEQUENCE 507 AA; 54539 MW; 32C6E2EB11588477 CRC64;
MQEPLLGAEG PDYDTFPEKP PPSPGDRARV GTLQNKRVFL ATFAAVLGNF SFGYALVYTS
PVIPALERSL DPDLHLTKSQ ASWFGSVFTL GAAAGGLSAM ILNDLLGRKL SIMFSAVPSA
AGYALMAGAH GLWMLLLGRT LTGFAGGLTA ACIPVYVSEI APPGVRGALG ATPQLMAVFG
SLSLYALGLL LPWRWLAVAG EAPVLIMILL LSFMPNSPRF LLSRGRDEEA LRALAWLRGT
DVDVHWEFEQ IQDNVRRQSS RVSWAEARAP HVCRPITVAL LMRLLQQLTG ITPILVYLQS
IFDSTAVLLP PKDDAAIVGA VRLLSVLIAA LTMDLAGRKV LLFVSAAIMF AANLTLGLYI
HFGPRPLSPN STAGLESESW GDLAQPLAAP AGYLTLVPLL ATMLFIMGYA VGWGPITWLL
MSEVLPLRAR GVASGLCVLA SWLTAFVLTK SFLPVVSTFG LQVPFFFFAA ICLVSLVFTG
CCVPETKGRS LEQIESFFRT GRRSFLR
