FPGT

FPGT
Identifiers
Aliases	FPGT, GFPP, fucose-1-phosphate guanylyltransferase
External IDs	OMIM: 603609 MGI: 1922790 HomoloGene: 2847 GeneCards: FPGT
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	74,234,086 bp[1]
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)[2]
End	154,799,040 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; Achilles tendon; ; gallbladder; ; secondary oocyte; ; rectum; ; islet of Langerhans; ; jejunal mucosa; ; bronchial epithelial cell; ; corpus epididymis; ; ganglionic eminence;
	Top expressed in
	secondary oocyte; ; interventricular septum; ; olfactory epithelium; ; islet of Langerhans; ; otolith organ; ; Region I of hippocampus proper; ; utricle; ; left colon; ; medial ganglionic eminence; ; seminal vesicula;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; nucleotide binding; transferase activity, transferring phosphorus-containing groups; nucleotidyltransferase activity; GTP binding; catalytic activity; fucose-1-phosphate guanylyltransferase activity;
Cellular component	cytoplasm; cytosol;
Biological process	fucose metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	8790
	75540
	ENSG00000254685
	ENSMUSG00000053870
	O14772
	G5E8F4
	NM_003838; NM_001199328; NM_001199329
	NM_029330
	NP_001186257; NP_001186258; NP_003829
	NP_083606
	Wikidata
View/Edit Human	View/Edit Mouse

Fucose-1-phosphate guanylyltransferase is an enzyme that in humans is encoded by the FPGT gene.[5][6]

L-fucose is a key sugar in glycoproteins and other complex carbohydrates since it may be involved in many of the functional roles of these macromolecules, such as in cell–cell recognition. The fucosyl donor for these fucosylated oligosaccharides is GDP-beta-L-fucose.

There are two alternate pathways for the biosynthesis of GDP-fucose; the major pathway converts GDP-alpha-D-mannose to GDP-beta-L-fucose. The protein encoded by this gene participates in an alternate pathway that is present in certain mammalian tissues, such as liver and kidney, and appears to function as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids.

This pathway involves the phosphorylation of L-fucose to form beta-L-fucose-1-phosphate, and then condensation of the beta-L-fucose-1-phosphate with GTP by fucose-1-phosphate guanylyltransferase to form GDP-beta-L-fucose.[6]

References

GRCh38: Ensembl release 89: ENSG00000254685 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000053870 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD (Dec 1998). "GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme". J Biol Chem. 273 (46): 30165–74. doi:10.1074/jbc.273.46.30165. PMID 9804772.
"Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase".

Quirk S, Seley-Radtke KL (2006). "Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase". Acta Crystallographica Section F. 62 (Pt 4): 392–4. doi:10.1107/S1744309106008529. PMC 2222559. PMID 16582493.
Quirk S, Seley KL (2005). "Identification of catalytic amino acids in the human GTP fucose pyrophosphorylase active site". Biochemistry. 44 (39): 13172–8. doi:10.1021/bi051288d. PMID 16185085.
Quirk S, Seley KL (2005). "Substrate discrimination by the human GTP fucose pyrophosphorylase". Biochemistry. 44 (32): 10854–63. doi:10.1021/bi0503605. PMID 16086588.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000254685 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000053870 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9804772-5] Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD (Dec 1998). "GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme". J Biol Chem. 273 (46): 30165–74. doi:10.1074/jbc.273.46.30165. PMID 9804772.

[entrez-6] "Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase".

FPGT

References

Further reading