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.
^ abcGRCh38: Ensembl release 89: ENSG00000186866 – Ensembl, May 2017
^ abcGRCm38: 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. PMC5601480. PMID 28916755.
fucose, protein, fucosyltransferase, pofut2, enzyme, responsible, adding, fucose, sugars, linkage, serine, threonine, residues, thrombospondin, repeats, protein, inverting, glycosyltransferase, which, means, that, enzyme, uses, fucose, donor, substrate, transf. 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 b L fucose as a donor substrate and transfers the fucose in O linkage to the protein producing fucose a O serine threonine POFUT2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes4AP5 4AP6IdentifiersAliasesPOFUT2 C21orf80 FUT13 protein O fucosyltransferase 2External IDsOMIM 610249 MGI 1916863 HomoloGene 12724 GeneCards POFUT2Gene location Human Chr Chromosome 21 human 1 Band21q22 3Start45 263 928 bp 1 End45 287 898 bp 1 Gene location Mouse Chr Chromosome 10 mouse 2 Band10 10 C1Start77 095 052 bp 2 End77 105 409 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright uterine tubestromal cell of endometriumanterior pituitaryright lobe of thyroid glandcanal of the cervixleft lobe of thyroid glandsural nervepancreatic ductal cellleft uterine tubegallbladderTop expressed inexternal carotid arteryinternal carotid arteryfossacondylevas deferensmolarbody of femurbelly corddermisatriumMore reference expression dataBioGPSn aGene ontologyMolecular functiontransferase activity fucosyltransferase activity glycosyltransferase activity peptide O fucosyltransferase activityCellular componentGolgi apparatus endoplasmic reticulum endoplasmic reticulum membraneBiological processregulation of gene expression fucose metabolic process protein glycosylation regulation of epithelial to mesenchymal transition mesoderm formation regulation of secretion protein O linked fucosylation fucosylation carbohydrate metabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez2327580294EnsemblENSG00000186866ENSMUSG00000020260UniProtQ9Y2G5Q8VHI3RefSeq mRNA NM 015227NM 133634NM 133635NM 030262RefSeq protein NP 056042NP 598368NP 084538Location UCSC Chr 21 45 26 45 29 MbChr 10 77 1 77 11 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse 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 editPeptide O fucosyltransferaseReferences 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 editPOFUT2 protein human at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title GDP fucose protein O fucosyltransferase 2 amp oldid 1180274280, wikipedia, wiki, book, books, library,
