P17809 (GTR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Solute carrier family 2, facilitated glucose transporter member 1

Alternative name(s):
Glucose transporter type 1, erythrocyte/brain
Short name=GLUT-1
Short name=GT1

Gene names

Name:	Slc2a1
Synonyms:	Glut-1, Glut1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Melanosome By similarity. Note: Localizes primarily at the cell surface By similarity.
Developmental stage	Levels decline 3-fold between days 7.5 and 12.5 of gestation. At 7.5 dpc, expressed more strongly in extraembryonic tissues than in the embryo proper. Expressed in amnion, chorion, and ectoplacental cone. In the yolk sac, expressed more strongly in the mesoderm layer than the ectoderm. Expression fairly widespread in the embryo at 8.5 dpc, but by 10.5 dpc, expression is down-regulated and observed in the eye and the spinal cord. Ref.8 Ref.9
Sequence similarities	Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. [View classification]

Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose starvation Inferred from direct assay PubMed 11259273. Source: MGI response to osmotic stress Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Inferred from direct assay PubMed 11259273PubMed 15975910. Source: MGI caveola Inferred from electronic annotation. Source: Compara cell-cell junction Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 18668520. Source: UniProtKB female pronucleus Inferred from direct assay PubMed 11259273. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: Compara vesicle Inferred from direct assay PubMed 11259273. Source: MGI
Molecular_function	D-glucose transmembrane transporter activity Inferred from direct assay PubMed 18668520. Source: UniProtKB dehydroascorbic acid transporter activity Inferred from direct assay PubMed 18668520. Source: UniProtKB xenobiotic transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Solute carrier family 2, facilitated glucose transporter member 1		PRO_0000050339
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 33	21	Helical; Name=1; Potential
	Topological domain	34 – 66	33	Extracellular Potential
	Transmembrane	67 – 87	21	Helical; Name=2; Potential
	Topological domain	88 – 95	8	Cytoplasmic Potential
	Transmembrane	96 – 116	21	Helical; Name=3; Potential
	Topological domain	117 – 126	10	Extracellular Potential
	Transmembrane	127 – 147	21	Helical; Name=4; Potential
	Topological domain	148 – 155	8	Cytoplasmic Potential
	Transmembrane	156 – 176	21	Helical; Name=5; Potential
	Topological domain	177 – 185	9	Extracellular Potential
	Transmembrane	186 – 206	21	Helical; Name=6; Potential
	Topological domain	207 – 271	65	Cytoplasmic Potential
	Transmembrane	272 – 292	21	Helical; Name=7; Potential
	Topological domain	293 – 307	15	Extracellular Potential
	Transmembrane	308 – 328	21	Helical; Name=8; Potential
	Topological domain	329 – 337	9	Cytoplasmic Potential
	Transmembrane	338 – 358	21	Helical; Name=9; Potential
	Topological domain	359 – 371	13	Extracellular Potential
	Transmembrane	372 – 392	21	Helical; Name=10; Potential
	Topological domain	393 – 401	9	Cytoplasmic Potential
	Transmembrane	402 – 422	21	Helical; Name=11; Potential
	Topological domain	423 – 429	7	Extracellular Potential
	Transmembrane	430 – 450	21	Helical; Name=12; Potential
	Topological domain	451 – 492	42	Cytoplasmic Potential
	Region	279 – 281	3	Defines substrate specificity By similarity
Amino acid modifications
	Modified residue	234	1	Phosphothreonine Ref.10
	Modified residue	478	1	Phosphothreonine By similarity
	Modified residue	490	1	Phosphoserine By similarity
	Glycosylation	45	1	N-linked (GlcNAc...) Ref.11 Ref.12
	Glycosylation	49	1	N-linked (GlcNAc...) Ref.11 Ref.12
Experimental info
	Sequence conflict	52	1	Y → I in AAA37752. Ref.1
	Sequence conflict	193 – 195	3	IFI → VFV in AAA37752. Ref.1
	Sequence conflict	357 – 360	4	LLER → MQEQ in AAB20846. Ref.9
	Sequence conflict	403	1	A → R in AAA37752. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17809 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 464B668853D7636E	FASTA	492	53,985
	10 20 30 40 50 60 MDPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH RYGEPIPSTT 70 80 90 100 110 120 LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVAAVLM GFSKLGKSFE 130 140 150 160 170 180 MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM 190 200 210 220 230 240 GNADLWPLLL SVIFIPALLQ CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD 250 260 270 280 290 300 LQEMKEEGRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK 310 320 330 340 350 360 AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL MTIALALLER 370 380 390 400 410 420 LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAIAVAGFS NWTSNFIVGM 430 440 450 460 470 480 CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE 490 ELFHPLGADS QV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence, tissue distribution, and differential expression of mRNA for a putative insulin-responsive glucose transporter in mouse 3T3-L1 adipocytes." Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T., Cornelius P., Pekala P.H., Lane M.D. Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"3T3-L1 adipocyte glucose transporter (HepG2 class): sequence and regulation of protein and mRNA expression by insulin, differentiation, and glucose starvation." Reed B.C., Shade D., Alperovich F., Vang M. Arch. Biochem. Biophys. 279:261-274(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[7]	"Identification of two enhancer elements in the gene encoding the type 1 glucose transporter from the mouse which are responsive to serum, growth factor, and oncogenes." Murakami T., Nishiyama T., Shirotani T., Shinohara Y., Kan M., Ishii K., Kanai F., Nakazuru S., Ebina Y. J. Biol. Chem. 267:9300-9306(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
[8]	"Differential screening of a PCR-generated mouse embryo cDNA library: glucose transporters are differentially expressed in early postimplantation mouse embryos." Smith D.E., Gridley T. Development 116:555-561(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 151-237, DEVELOPMENTAL STAGE. Strain: C57BL/6. Tissue: Embryo.
[9]	"Glucose transporter gene expression in early mouse embryos." Hogan A., Heyner S., Charron M.J., Copeland N.G., Gilbert D.J., Jenkins N.A., Thorens B., Schultz G.A. Development 113:363-372(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 357-463, DEVELOPMENTAL STAGE. Strain: CD-1. Tissue: Embryo.
[10]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, MASS SPECTROMETRY. Tissue: Macrophage.
[11]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45 AND ASN-49, MASS SPECTROMETRY. Tissue: Myoblast.
[12]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45 AND ASN-49, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M23384 mRNA. Translation: AAA37752.1. M22998 mRNA. Translation: AAA37707.1. AK170873 mRNA. Translation: BAE42084.1. AL606975 Genomic DNA. Translation: CAM21633.1. CH466552 Genomic DNA. Translation: EDL30474.1. BC055340 mRNA. Translation: AAH55340.1. X69697 mRNA. Translation: CAA49367.1. S77924 mRNA. Translation: AAB20846.2.
IPI	IPI00308691.
PIR	A44887. S09705.
RefSeq	NP_035530.2. NM_011400.3.
UniGene	Mm.21002.
3D structure databases
ProteinModelPortal	P17809.
SMR	P17809. Positions 19-465.
ModBase	Search...
Protein-protein interaction databases
IntAct	P17809. 2 interactions.
MINT	MINT-348833.
PTM databases
PhosphoSite	P17809.
Proteomic databases
PaxDb	P17809.
PRIDE	P17809.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030398; ENSMUSP00000030398; ENSMUSG00000028645.
GeneID	20525.
KEGG	mmu:20525.
Organism-specific databases
CTD	6513.
MGI	MGI:95755. Slc2a1.
Phylogenomic databases
eggNOG	COG0477.
GeneTree	ENSGT00630000089621.
HOGENOM	HOG000202871.
HOVERGEN	HBG014816.
InParanoid	Q6GTI3.
KO	K07299.
OMA	HRYGERI.
OrthoDB	EOG4QNMW2.
Gene expression databases
ArrayExpress	P17809.
Bgee	P17809.
Genevestigator	P17809.
GermOnline	ENSMUSG00000028645. Mus musculus.
Family and domain databases
InterPro	IPR002439. Glu_transpt_1. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR005828. Sub_transporter. IPR003663. Sugar/inositol_transpt. IPR005829. Sugar_transporter_CS. [Graphical view]
Pfam	PF00083. Sugar_tr. 1 hit. [Graphical view]
PRINTS	PR01190. GLUCTRSPORT1. PR00171. SUGRTRNSPORT.
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR00879. SP. 1 hit.
PROSITE	PS50850. MFS. 1 hit. PS00216. SUGAR_TRANSPORT_1. 1 hit. PS00217. SUGAR_TRANSPORT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SLC2A1. mouse.
NextBio	298763.
SOURCE	Search...

Entry information

Entry name

GTR1_MOUSE

Accession

Primary (citable) accession number: P17809
Secondary accession number(s): Q61608, Q6GTI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 131 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program