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2.A.1.1.91
Solute carrier family 2, facilitated glucose transporter member 3 (Glucose transporter type 3, brain) (GLUT-3 or GLUT3). It mediates the facilitative uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably dehydroascorbate, but not fructose (Seatter et al. 1998, Deng et al. 2015).  GLUT3, a key neuronal transporter, exhibits multiple intermediate states (Sun and Zheng 2019). SLC2A3 may play a role in the progression of colorectal cancer (CRC) by regulating the epithelial-mesenchymal transition (EMT) classical pathway as well as PD-L1 mediated immune responses (Gao et al. 2021). GLUT3 is consistently upregulated in actively proliferating human oral squamous cell carcinoma cells (Paolini et al. 2022). GLUT-1 and GLUT-3 play roles in the development of some types of malignant tumors including glioblastoma, and expression of both is regulated by miRNAs (Beylerli et al. 2022). The overexpression of GLUT3 or GLUT1 may be monitored alone or in combination (GLUT1/GLUT3 ratio) as a biomarker for preeclampsia onset, phenotype, and progression (Agbani et al. 2023).

Accession Number:P11169
Protein Name:Solute carrier family 2, facilitated glucose transporter member 3
Length:496
Molecular Weight:53924.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate dehydroascorbic acid, glucosamine, fucose, xylose, glucose, galactose, mannose, 2-deoxy-D-glucose

Cross database links:

Entrez Gene ID: 6515   
Pfam: PF00083   
KEGG: hsa:6515   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005355 F:glucose transmembrane transporter activity
GO:0005975 P:carbohydrate metabolic process
GO:0019852 P:L-ascorbic acid metabolic process

References (6)

[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.et.al.   3170580
[2] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “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.et.al.   9477959
[5] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[6] “Initial characterization of the human central proteome.”  Burkard T.R.et.al.   21269460
Structure:
4ZW9   4ZWB   4ZWC   5C65     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MGTQKVTPAL IFAITVATIG SFQFGYNTGV INAPEKIIKE FINKTLTDKG NAPPSEVLLT 
61:	SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLIVNLL AVTGGCFMGL CKVAKSVEML 
121:	ILGRLVIGLF CGLCTGFVPM YIGEISPTAL RGAFGTLNQL GIVVGILVAQ IFGLEFILGS 
181:	EELWPLLLGF TILPAILQSA ALPFCPESPR FLLINRKEEE NAKQILQRLW GTQDVSQDIQ 
241:	EMKDESARMS QEKQVTVLEL FRVSSYRQPI IISIVLQLSQ QLSGINAVFY YSTGIFKDAG 
301:	VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAFCSTLMT VSLLLKDNYN 
361:	GMSFVCIGAI LVFVAFFEIG PGPIPWFIVA ELFSQGPRPA AMAVAGCSNW TSNFLVGLLF 
421:	PSAAHYLGAY VFIIFTGFLI TFLAFTFFKV PETRGRTFED ITRAFEGQAH GADRSGKDGV 
481:	MEMNSIEPAK ETTTNV