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2.A.1.1.29
Glucosamine/glucose/fructose uniporter, Glut-2, Glut2 or ATG9A; it may also transport dehydroascorbate (Mardones et al., 2011Maulén et al., 2003), and cotransports water against an osmotic gradient (Naftalin, 2008).  Mutations may give rise to the rare autosomal recessive Fanconi-Bickel syndrome (Batool et al. 2019). It mediate intestinal transport of quercetrin (Li et al. 2020). It also functions in autophagy (see below).
    The cryoelectron microscopy structure of the human ATG9A isoform at 2.9-Å resolution has been solved (Guardia et al. 2020). The structure reveals a fold with a homotrimeric domain-swapped architecture, multiple membrane spans, and a network of branched cavities, consistent with ATG9A being a membrane transporter. Mutational analyses support a role for the cavities in the function of ATG9A. Structure-guided molecular simulations predict that ATG9A causes membrane bending, explaining the localization of this protein to small vesicles and highly curved edges of growing autophagosomes (Guardia et al. 2020). Both GLUT2 and GLUT3 have been expressed in yeast and exhibit most of the characteristics of the proteins expressed in humans (Schmidl et al. 2020).  

Accession Number:P11168
Protein Name:Gtr2 aka Glut2 aka SLC2A2
Length:524
Molecular Weight:57490.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate glucose, Glucosamine

Cross database links:

RefSeq: NP_000331.1   
Entrez Gene ID: 6514   
Pfam: PF00083   
OMIM: 138160  gene
227810  phenotype
KEGG: hsa:6514    hsa:6514   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0005624 C:membrane fraction
GO:0005975 P:carbohydrate metabolic process
GO:0015758 P:glucose transport
GO:0055085 P:transmembrane transport
GO:0016323 C:basolateral plasma membrane
GO:0031526 C:brush border membrane
GO:0005829 C:cytosol
GO:0005768 C:endosome
GO:0055056 F:D-glucose transmembrane transporter activity
GO:0033300 F:dehydroascorbic acid transporter activity
GO:0005355 F:glucose transmembrane transporter activity
GO:0031018 P:endocrine pancreas development
GO:0006112 P:energy reserve metabolic process
GO:0015755 P:fructose transport
GO:0050796 P:regulation of insulin secretion
GO:0009749 P:response to glucose stimulus
GO:0043434 P:response to peptide hormone stimulus
GO:0044281 P:small molecule metabolic process

References (14)

[1] “Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein.”  Fukumoto H.et.al.   3399500
[2] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[3] “Sequence variations of the pancreatic islet/liver glucose transporter (GLUT2) gene in Japanese subjects with noninsulin dependent diabetes mellitus.”  Matsubara A.et.al.   7593414
[4] “Variability of the pancreatic islet beta cell/liver (GLUT 2) glucose transporter gene in NIDDM patients.”  Tanizawa Y.et.al.   8063045
[5] “A mutation in the Glut2 glucose transporter gene of a diabetic patient abolishes transport activity.”  Mueckler M.et.al.   8027028
[6] “A mutation in GLUT2, not in phosphorylase kinase subunits, in hepato-renal glycogenosis with Fanconi syndrome and low phosphorylase kinase activity.”  Burwinkel B.et.al.   10987651
[7] “Mutation analysis of the GLUT2 gene in patients with Fanconi-Bickel syndrome.”  Sakamoto O.et.al.   11044475
[8] “Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein.”  Fukumoto H.et.al.   3399500
[9] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[10] “Sequence variations of the pancreatic islet/liver glucose transporter (GLUT2) gene in Japanese subjects with noninsulin dependent diabetes mellitus.”  Matsubara A.et.al.   7593414
[11] “Variability of the pancreatic islet beta cell/liver (GLUT 2) glucose transporter gene in NIDDM patients.”  Tanizawa Y.et.al.   8063045
[12] “A mutation in the Glut2 glucose transporter gene of a diabetic patient abolishes transport activity.”  Mueckler M.et.al.   8027028
[13] “A mutation in GLUT2, not in phosphorylase kinase subunits, in hepato-renal glycogenosis with Fanconi syndrome and low phosphorylase kinase activity.”  Burwinkel B.et.al.   10987651
[14] “Mutation analysis of the GLUT2 gene in patients with Fanconi-Bickel syndrome.”  Sakamoto O.et.al.   11044475

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FASTA formatted sequence
1:	MTEDKVTGTL VFTVITAVLG SFQFGYDIGV INAPQQVIIS HYRHVLGVPL DDRKAINNYV 
61:	INSTDELPTI SYSMNPKPTP WAEEETVAAA QLITMLWSLS VSSFAVGGMT ASFFGGWLGD 
121:	TLGRIKAMLV ANILSLVGAL LMGFSKLGPS HILIIAGRSI SGLYCGLISG LVPMYIGEIA 
181:	PTALRGALGT FHQLAIVTGI LISQIIGLEF ILGNYDLWHI LLGLSGVRAI LQSLLLFFCP 
241:	ESPRYLYIKL DEEVKAKQSL KRLRGYDDVT KDINEMRKER EEASSEQKVS IIQLFTNSSY 
301:	RQPILVALML HVAQQFSGIN GIFYYSTSIF QTAGISKPVY ATIGVGAVNM VFTAVSVFLV 
361:	EKAGRRSLFL IGMSGMFVCA IFMSVGLVLL NKFSWMSYVS MIAIFLFVSF FEIGPGPIPW 
421:	FMVAEFFSQG PRPAALAIAA FSNWTCNFIV ALCFQYIADF CGPYVFFLFA GVLLAFTLFT 
481:	FFKVPETKGK SFEEIAAEFQ KKSGSAHRPK AAVEMKFLGA TETV