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Information on EC 2.4.1.221 - peptide-O-fucosyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q9V6X7
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2.4.1.221 peptide-O-fucosyltransferaseIUBMB Comments
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins. In EGF domains, the attachment of O-linked fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
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Word Map
- 2.4.1.221
- notch
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o-fucosylation
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o-fucose
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factor-like
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o-linked
- thrombospondin
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fringe
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dowling-degos
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egf-like
- poglut1
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notch-ligand
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lunatic
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plagl2
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somitogenesis
- dll1
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genodermatosis
- hidradenitis
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o-glucosyltransferase
- drug development
- medicine
- molecular biology
- diagnostics
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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=
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[protein]-(L-serine/L-threonine)
=
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[protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Synonyms
pofut1, protein o-fucosyltransferase 1, pofut2, o-fucosyltransferase, ofut1, protein o-fucosyltransferase 2, o-fut1, o-fuct-1, o-fucosyltransferase 1, alpha-6-fucosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-6-fucosyltransferase
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core alpha6FucT
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fucosyltransferase, guanosine diphosphofucose-glycoprotein
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GDP-fucose glycoprotein fucosyltransferase
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GDP-fucose protein O-fucosyltransferase
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GDP-fucose:polypeptide fucosyltransferase
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GDP-L-fucose-glycoprotein fucosyltransferase
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GDP-L-fucose:polypeptide fucosyltransferase
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glycoprotein fucosyltransferase
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guanosine diphosphofucose-glycoprotein fucosyltransferase
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N-acetyl-beta-D-glucosaminide alpha1-->6-fucosyltransferase
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N-glycan alpha-6-fucosyltransferase
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O-fucT-1
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Pofut1
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POFUT2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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transglycosylation
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:protein-(L-serine/L-threonine) O-alpha-L-fucosyltransferase (configuration-inverting)
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins. In EGF domains, the attachment of O-linked fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
CAS REGISTRY NUMBER
COMMENTARY
9033-08-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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essential for Notch signaling
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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essential for Notch signaling
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?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
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O-glycome of Drosophila melanogaster by mass spectrometry, using beta-elimination to release the O-linked sugar modifications from total protein extracts of fly embryos, overview
physiological function
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Notch is a transmembrane receptor that shares homology with proteins containing epidermal growth factor-like repeats and mediates the cell-cell interactions necessary for many cell fate decisions. O-fucosyltransferase 1 catalyzes the O-fucosylation of these epidermal growth factor-like repeats. This O-fucose elongates, resulting in an O-linked tetrasaccharide that regulates the signaling activities of Notch. Fucosylation occurs in the lumen of the endoplasmicreticulum and Golgi. GDP-fucose uptake into the ER and Golgi is essential for fucosylation, Efr, a multifunctional nucleotide sugar transporter, and Golgi GDP-fucose transporter Gfr are involved in the biosynthesis of heparan sulfate-glycosaminoglycan chains and the O-fucosylation of Notch. Gfr but not Efr is crucial for the fucosylation of N-glycans, overview
physiological function
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O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Ofut1 might have a chaperone-like activity in Drosophila that is required for cell-surface expression of Notch in flies. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OFUT1_DROME
402
0
46834
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R254A
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expression of a mutant, Ofut1R245A, lacking fucosyltransferase activity, rescues the requirement for Ofut1 in embryonic neurogenesis. Lack of requirement for O-fucosylation is further supported by the absence of embryonic phenotypes in Gmd mutants, which lack all forms of fucosylation. Requirements for O-fucose during imaginal development are evaluated by characterizing clones of cells expressing only Ofut1R245A. These clones phenocopy fringe mutant clones, indicating that the absence of O-fucose is functionally equivalent to the absence of elongated O-fucose
additional information
additional information
enzyme disruption mutant, enzyme is essential for Notch signaling, Fringe function, for physical interaction of Notch with its ligand Delta, and lateral inhibition during neuroblast segregation
additional information
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down-regulation of enzyme by RNA interference in Notch-secreting cells inhibits both Delta-Notch and Serrate-Notch binding. Overexpression of enzyme in cultured cells increases Serrate-Notch binding but inhibits Delta-Notch binding
additional information
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analysis of O-fut 1 homozygous mutant cells shows that O-fut1 is required for the endocytic transportation of Notch to the early endosome which is shown to be independent of the O-fucosyltransferase activity of O-fut1
additional information
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O-fut 1 overexpression and analysis of O-fut 1 homozygous mutant cells indicates that O-fut 1 promotes the turnover of Notch, which consequently downregulates Notch signaling
additional information
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O-fut1 protein added to conditioned medium and endocytosed is sufficient to rescue normal Notch transportation to the early endosome in O-fut1 knockdown cells
additional information
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using O-fut I knock out mutants it is shown that the localization of Notch in the region from the subapical complex (SAC) to the apical portion of the adherens junctions (AJs) depends on its O-fucosylation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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O-fucosylation is dispensable for many Notch signaling events during Drosophila development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
ang, Y.; Shao, L.; Shi, S.; Harris, R.J.; Spellman, M.W.; Stanley, P.; Haltiwanger, R.S.
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase
J. Biol. Chem.
276
40338-40345
2001
Candida elegans, Drosophila melanogaster, Homo sapiens (Q9H488), Homo sapiens, Mus musculus (Q91ZW2), Mus musculus
Okajima, T.; Xu, A.; Irvine, K.D.
Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe
J. Biol. Chem.
278
42340-42345
2003
Drosophila melanogaster
Okajima, T.; Xu, A.; Lei, L.; Irvine, K.D.
Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding
Science
307
1599-1603
2005
Drosophila melanogaster
Sasamura, T.; Sasaki, N.; Miyashita, F.; Nakao, S.; Ishikawa, H.O.; Ito, M.; Kitagawa, M.; Harigaya, K.; Spana, E.; Bilder, D.; Perrimon, N.; Matsuno, K.
neurotic, a novel maternal neurogenic gene, encodes an O-fucosyltransferase that is essential for Notch-Delta interactions
Development
130
4785-4795
2003
Drosophila melanogaster (Q9V6X7)
Okajima, T.; Reddy, B.; Matsuda, T.; Irvine, K.D.
Contributions of chaperone and glycosyltransferase activities of O-fucosyltransferase 1 to Notch signaling
BMC Biol.
6
1-10
2008
Drosophila melanogaster
Sasamura, T.; Ishikawa, H.O.; Sasaki, N.; Higashi, S.; Kanai, M.; Nakao, S.; Ayukawa, T.; Aigaki, T.; Noda, K.; Miyoshi, E.; Taniguchi, N.; Matsuno, K.
The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila
Development
134
1347-1356
2007
Drosophila melanogaster
Sasaki, N.; Sasamura, T.; Ishikawa, H.O.; Kanai, M.; Ueda, R.; Saigo, K.; Matsuno, K.
Polarized exocytosis and transcytosis of Notch during its apical localization in Drosophila epithelial cells
Genes Cells
12
89-103
2007
Drosophila melanogaster
Rana, N.A.; Haltiwanger, R.S.
Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
Curr. Opin. Struct. Biol.
21
583-589
2011
Drosophila melanogaster, Mus musculus
Ishikawa, H.; Ayukawa, T.; Nakayama, M.; Higashi, S.; Kamiyama, S.; Nishihara, S.; Aoki, K.; Ishida, N.; Sanai, Y.; Matsuno, K.
Two pathways for importing GDP-fucose into the endoplasmic reticulum lumen function redundantly in the O-fucosylation of notch in Drosophila
J. Biol. Chem.
285
4122-4129
2010
Drosophila melanogaster
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