Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase.
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Molecular cloning of human POFUT1 (O-FucT-1) cDNA; recombinant soluble enzyme reproduces the O-fucosyltransferase activity and kinetics of the natively purified enzyme. This is the reference to which UniProt assigns EC 2.4.1.221.
"Expression of a soluble form of human O-FucT-1 in insect cells yielded a protein of the predicted molecular weight with O-FucT-1 kinetic and enzymatic properties similar to those of O-FucT-1 purified from CHO cells."
Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism.
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Genome-wide survey of Drosophila enzymes in fucosylated-glycan metabolism that identified fly O-fucosyltransferase genes; not a characterization of human POFUT1.
"We also identified two novel genes coding for O-fucosyltransferases and a gene responsible for a fucosidase enzyme in the Drosophila genome."
O-fucosylation of notch occurs in the endoplasmic reticulum.
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Human O-FucT-1 (POFUT1) is a soluble protein that localizes to the ER, retained by a C-terminal KDEL-like motif; O-fucosylation of proteins (Notch) occurs in the ER, distinguishing POFUT1 from the Golgi FUT family.
"O-FucT-1 is a soluble protein that localizes to the endoplasmic reticulum (ER)."
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Because O-FucT-1 recognizes only properly folded EGF-like repeats, and given its unique ER localization, it may function in a quality-control step.
"The fact that O-FucT-1 recognizes properly folded epidermal growth factor-like repeats, together with this unique localization, suggests that it may play a role in quality control."
Defining the membrane proteome of NK cells.
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Large-scale MS catalog of the NK-like (YTS) cell membrane proteome (1843 proteins) in which POFUT1 was detected in a crude membrane fraction.
"Mass spectrometric analysis identified 1843 proteins with high confidence scores."
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations.
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POFUT1 is an ER-resident enzyme that O-fucosylates EGF-like repeats using GDP-fucose and is essential for Notch signal transduction in mammals.
"POFUT1 is an ER-resident protein that catalyzes O-linked fucosylation of an acceptor site on an EGF-like repeat of a recipient protein, using GDP-fucose as the donor substrate."
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CRISPR knockout of POFUT1 suppresses normal and oncogenic ligand-independent Notch1 signaling and blocks Notch1 surface delivery; rescue requires catalytic activity (impaired by active-site R240A). Supports the IMP regulation-of-Notch annotation.
"Normal and oncogenic signaling are rescued by wild-type POFUT1 but rescue is impaired by an active-site R240A mutation."
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Reported Dowling-Degos missense mutations (except M262T) fail to rescue Notch1 signaling, consistent with loss of function underlying the disease.
"The reported Dowling-Degos mutations of POFUT1, except for M262T, fail to rescue Notch1 signaling efficiently in the CRISPR-engineered POFUT1-/- background."
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Whether the enzyme-independent chaperone activity described for Drosophila Ofut1 extends to mammalian POFUT1 is explicitly unresolved.
"Whether the enzyme-independent chaperone activity of Pofut1 extends to mammals is not clear."
Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains.
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Original biochemical identification of the GDP-fucose:polypeptide fucosyltransferase: it attaches fucose by an O-glycosidic linkage to a Ser/Thr in EGF domains.
"The enzyme catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains."
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The enzyme requires a properly folded, disulfide-bonded EGF domain rather than a linear consensus peptide, establishing folding-dependent acceptor recognition.
"the enzyme appears to require more than just a consensus primary sequence and likely requires that the EGF domain disulfide bonds be properly formed"
FutureHouse Falcon deep-research report for POFUT1
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Deep-research synthesis: POFUT1 is best supported as a soluble ER-luminal protein O-fucosyltransferase acting on folded EGF repeats, with Notch O-fucosylation as the central downstream axis; Golgi/cytosol/nucleus/plasma-membrane localizations and direct apoptosis/pyroptosis roles are over-extensions to avoid.
"POFUT1 is consistently described as an ER-localized, soluble luminal enzyme"