|Protein Name||Solute carrier family 2, facilitated glucose transporter member 1|
|Ref Sequence Id||NP_777027.1|
|Amino Acid Lenth||492|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||widely distributed and are present on the surface of probably all mammalian cells; highest levels are in placenta, brain, and kidney|
|Protein Function||catalyses facilitative diffusion of glucose into erythrocytes and is responsible for glucose supply to the brain and other organs; mediates the basal-level cellular uptake of glucose into many tissues; functionally important either for transport of glucose or for the regulation of transport activity|
|Biochemical Properties||belongs to the sugar porter subfamily of the major facilitator superfamily; comprises 12 transmembrane segments organized into two discretely folded domains, namely the amino- and carboxy-terminaldomains; extracellular loop of 33 amino acids connects transmembrane segments M1 and M2|
|Significance in milk||nutrient transport systems for milk precursors and constituents|
|PTMs||Glycosylated: M1 and M2 and contains a potential site for asparagine-linked gloycosylation (Asn-Xaa- Thr/Ser; Fig. 2)|
|Bibliography||1. Deng, D. et al. (2014) ‘Crystal structure of the human glucose transporter GLUT1’, Nature, 510(7503), pp. 121–125. doi: 10.1038/nature13306. |
2. Mueckler, M. et al. (1985) ‘Sequence and structure of a human glucose transporter’, Science, 229(4717), pp. 941–945. doi: 10.1126/science.3839598.
3. Thorens, B. et al. (1988) ‘Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney, and β-pancreatic islet cells’, Cell, 55(2), pp. 281–290. doi: 10.1016/0092-8674(88)90051-7.