GDP-fucose protein O-fucosyltransferase 2 (POFUT2) is an enzyme responsible for adding fucose sugars in O linkage to serine or threonine residues in Thrombospondin repeats.[5] The protein is an inverting glycosyltransferase, which means that the enzyme uses GDP-β-L-fucose as a donor substrate and transfers the fucose in O linkage to the protein producing fucose-α-O-serine/threonine.
POFUT2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | POFUT2, C21orf80, FUT13, protein O-fucosyltransferase 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 610249; MGI: 1916863; HomoloGene: 12724; GeneCards: POFUT2; OMA:POFUT2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Almost all glycosyltransferases reside in the Golgi apparatus. However, POFUT2 as well as the related enzyme POFUT1 have recently been shown to reside in the endoplasmic reticulum.
The malaria parasite Plasmodium falciparum requires POFUT2 for efficient transmission to mosquitoes and infection of human liver cells.[6]
See also
editReferences
edit- ^ a b c GRCh38: Ensembl release 89: ENSG00000186866 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020260 – 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.
- ^ GDP-fucose protein O-fucosyltransferase 2, The Universal Protein Resource
- ^ Lopaticki S, Yang AS, John A, Scott NE, Lingford JP, O'Neill MT, et al. (September 2017). "Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts". Nature Communications. 8 (1): 561. Bibcode:2017NatCo...8..561L. doi:10.1038/s41467-017-00571-y. PMC 5601480. PMID 28916755.
External links
edit- POFUT2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)