P11169 (GTR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Solute carrier family 2, facilitated glucose transporter member 3

Alternative name(s):
Glucose transporter type 3, brain
Short name=GLUT-3

Gene names

Name:	SLC2A3
Synonyms:	GLUT3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Facilitative glucose transporter. Probably a neuronal glucose transporter.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Highly expressed in brain. Expressed in many tissues. Ref.1
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	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Traceable author statement. Source: Reactome water-soluble vitamin metabolic process Traceable author statement. Source: Reactome
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular function	glucose transmembrane transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Solute carrier family 2, facilitated glucose transporter member 3		PRO_0000050353
Regions
	Topological domain	1 – 5	5	Cytoplasmic Potential
	Transmembrane	6 – 26	21	Helical; Name=1; Potential
	Topological domain	27 – 64	38	Extracellular Potential
	Transmembrane	65 – 85	21	Helical; Name=2; Potential
	Topological domain	86 – 93	8	Cytoplasmic Potential
	Transmembrane	94 – 114	21	Helical; Name=3; Potential
	Topological domain	115 – 124	10	Extracellular Potential
	Transmembrane	125 – 145	21	Helical; Name=4; Potential
	Topological domain	146 – 153	8	Cytoplasmic Potential
	Transmembrane	154 – 174	21	Helical; Name=5; Potential
	Topological domain	175 – 183	9	Extracellular Potential
	Transmembrane	184 – 204	21	Helical; Name=6; Potential
	Topological domain	205 – 269	65	Cytoplasmic Potential
	Transmembrane	270 – 290	21	Helical; Name=7; Potential
	Topological domain	291 – 304	14	Extracellular Potential
	Transmembrane	305 – 325	21	Helical; Name=8; Potential
	Topological domain	326 – 334	9	Cytoplasmic Potential
	Transmembrane	335 – 355	21	Helical; Name=9; Potential
	Topological domain	356 – 368	13	Extracellular Potential
	Transmembrane	369 – 389	21	Helical; Name=10; Potential
	Topological domain	390 – 399	10	Cytoplasmic Potential
	Transmembrane	400 – 420	21	Helical; Name=11; Potential
	Topological domain	421 – 427	7	Extracellular Potential
	Transmembrane	428 – 448	21	Helical; Name=12; Potential
	Topological domain	449 – 496	48	Cytoplasmic Potential
	Region	277 – 279	3	Defines substrate specificity By similarity
Amino acid modifications
	Modified residue	485	1	Phosphoserine Ref.9
	Glycosylation	43	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	85	1	V → L. Corresponds to variant rs17728193 [ dbSNP | Ensembl ].		VAR_052502

Sequences

	Sequence		Length	Mass (Da)
	P11169 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: F601CD6892F16516	FASTA	496	53,924
	10 20 30 40 50 60 MGTQKVTPAL IFAITVATIG SFQFGYNTGV INAPEKIIKE FINKTLTDKG NAPPSEVLLT 70 80 90 100 110 120 SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLIVNLL AVTGGCFMGL CKVAKSVEML 130 140 150 160 170 180 ILGRLVIGLF CGLCTGFVPM YIGEISPTAL RGAFGTLNQL GIVVGILVAQ IFGLEFILGS 190 200 210 220 230 240 EELWPLLLGF TILPAILQSA ALPFCPESPR FLLINRKEEE NAKQILQRLW GTQDVSQDIQ 250 260 270 280 290 300 EMKDESARMS QEKQVTVLEL FRVSSYRQPI IISIVLQLSQ QLSGINAVFY YSTGIFKDAG 310 320 330 340 350 360 VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAFCSTLMT VSLLLKDNYN 370 380 390 400 410 420 GMSFVCIGAI LVFVAFFEIG PGPIPWFIVA ELFSQGPRPA AMAVAGCSNW TSNFLVGLLF 430 440 450 460 470 480 PSAAHYLGAY VFIIFTGFLI TFLAFTFFKV PETRGRTFED ITRAFEGQAH GADRSGKDGV 490 MEMNSIEPAK ETTTNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues." Kayano T., Fukumoto H., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I. J. Biol. Chem. 263:15245-15248(1988) [PubMed: 3170580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Fetal skeletal muscle.
[2]	"Resistance and expression of glucose transporters in human skeletal muscle." Stuart C.A., Wen K.G., Acosta M., Wood T.G. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum.
[7]	"Molecular characterization and cloning of glucose transporters in human articular chondrocytes." Neama G., Richardson S., Bell S., Carter S., Mobasheri A. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-453. Tissue: Articular cartilage.
[8]	"QLS motif in transmembrane helix VII of the glucose transporter family interacts with the C-1 (position) of D-glucose and is involved in substrate selection at the exofacial binding site." Seatter M.J., de la Rue S.A., Porter L.M., Gould G.W. Biochemistry 37:1322-1326(1998) [PubMed: 9477959] [Abstract] Cited for: SUBSTRATE SPECIFICITY SITE.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M20681 mRNA. Translation: AAB61083.1. AF274892 , AF274889, AF274890, AF274891 Genomic DNA. Translation: AAF82116.1. CR457413 mRNA. Translation: CAG33694.1. AK312386 mRNA. Translation: BAG35303.1. CH471116 Genomic DNA. Translation: EAW88644.1. CH471116 Genomic DNA. Translation: EAW88645.1. BC039196 mRNA. Translation: AAH39196.1. AY034634 mRNA. Translation: AAK56796.1.
IPI	IPI00003909.
PIR	A31986. T14798.
RefSeq	NP_008862.1. NM_006931.2.
UniGene	Hs.419240.
3D structure databases
ProteinModelPortal	P11169.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11169. 3 interactions.
MINT	MINT-4999361.
STRING	P11169.
PTM databases
PhosphoSite	P11169.
Polymorphism databases
DMDM	121760.
Proteomic databases
PRIDE	P11169.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000075120; ENSP00000075120; ENSG00000059804.
GeneID	6515.
KEGG	hsa:6515.
UCSC	uc001qtr.1. human.
Organism-specific databases
CTD	6515.
GeneCards	GC12M008071.
H-InvDB	HIX0026355.
HGNC	HGNC:11007. SLC2A3.
HPA	CAB002763. HPA006539.
MIM	138170. gene.
neXtProt	NX_P11169.
PharmGKB	PA35877.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08890.
HOGENOM	HBG744444.
HOVERGEN	HBG014816.
InParanoid	P11169.
OMA	GNAPPSE.
OrthoDB	EOG4QNMW2.
PhylomeDB	P11169.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15518. Transmembrane transport of small molecules. REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P11169.
Bgee	P11169.
CleanEx	HS_SLC2A3.
Genevestigator	P11169.
GermOnline	ENSG00000059804. Homo sapiens.
Family and domain databases
InterPro	IPR002945. Glc_transpt_3. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR005828. Sub_transporter. IPR003663. Sugar/inositol_transpt. IPR005829. Sugar_transporter_CS. [Graphical view]
KO	K08142.
Pfam	PF00083. Sugar_tr. 1 hit. [Graphical view]
PRINTS	PR01192. GLUCTRSPORT3. 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
NextBio	25335.
SOURCE	Search...

Entry information

Entry name

GTR3_HUMAN

Accession

Primary (citable) accession number: P11169
Secondary accession number(s): B2R606 , D3DUU6, Q6I9U2, Q9UG15

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.