Solute carrier family 2, facilitated glucose transporter member 7 (SLC2A7), also known as Glucose transporter type 7 (GLUT-7), is a protein that in humans is encoded by the SLC2A7 gene. It belongs to a family of transporters that catalyze the uptake of sugars through facilitated diffusion and contain 12 transmembrane helices as well as functionally significant amino acid residues.
Basic Information of SLC2A7 | |
Protein Name | Solute carrier family 2, facilitated glucose transporter member 7 |
Gene Name | SLC2A7 |
Aliases | Glucose transporter type 7, GLUT-7 |
Organism | Homo sapiens (Human) |
UniProt ID | Q6PXP3 |
Transmembrane Times | 12 |
Length (aa) | 512 |
Sequence | MENKEAGTPPPIPSREGRLQPTLLLATLSAAFGSAFQYGYNLSVVNTPHKVFKSFYNETYFERHATFMDGKLMLLLWSCTVSMFPLGGLLGSLLVGLLVDSCGRKGTLLINNIFAIIPAILMGVSKVAKAFELIVFSRVVLGVCAGISYSALPMYLGELAPKNLRGMVGTMTEVFVIVGVFLAQIFSLQAILGNPAGWPVLLALTGVPALLQLLTLPFFPESPRYSLIQKGDEATARQALRRLRGHTDMEAELEDMRAEARAERAEGHLSVLHLCALRSLRWQLLSIIVLMAGQQLSGINAINYYADTIYTSAGVEAAHSQYVTVGSGVVNIVMTITSAVLVERLGRRHLLLAGYGICGSACLVLTVVLLFQNRVPELSYLGIICVFAYIAGHSIGPSPVPSVVRTEIFLQSSRRAAFMVDGAVHWLTNFIIGFLFPSIQEAIGAYSFIIFAGICLLTAIYIYVVIPETKGKTFVEINRIFAKRNRVKLPEEKEETIDAGPPTASPAKETSF |
As a member of the glucose transporter proteins (GLUTs), GLUT7 (SLC2A7) is comprised of 524 amino acid residues and shares 68% similarity and 53% identity with GLUT5, its most closely related isoform. Studies have shown that GLUT7 appears to contain many of the so-called “signature sequences” that are believed to be typical of the proteins in GLUT family. The expression of SLC2A7 is primarily found in the small intestine and colon, although mRNA has been detected in the testis and prostate as well. Furthermore, although it seems to be unlikely that SLC2A7 plays a key role in taking up glucose from the diet in the initial stages of digestion and absorption, it may be important toward the end of the meal when luminal concentrations of glucose and fructose in the ileum are low.
Fig.1 Structure of protein SLC2A7.
This article aims to assess whether human GLUT2, GLUT5, GLUT7, and GLUT9 are indeed fructose transporters. But the result does not find evidence that GLUT7 or GLUT9 transport fructose or glucose or that the isoleucine residue determines their fructose specificity. Rather, the physiological substrate of GLUT7 awaits to be discovered.
This report describes the function and characterization of GLUT7, which has proved to be involved in the development of the hypothesis that the facilitated hexose transporters may have a selectivity filter at the exo-facial opening of the translocation pore, which helps to determine which hexoses can be transported. If substantiated, the elucidation of this mechanism may be useful in the design of hexose analogs for use in cancer imaging and therapeutics.
This article suggests that GLUT7 represents an intermediate between class II GLUTs and the class I member GLUT2. Comparison between these proteins may provide key information as to the structural determinants for the recognition of fructose as a substrate.
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