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Protein O-fucosyltransferase 2

POFUT2, protein O-fucosyltransferase 2, KIAA0958, C21orf80
Fucose is typically found as a terminal modification of branched chain glycoconjugates, but it also exists in direct O-linkage to serine or threonine residues within cystine knot motifs in epidermal growth factor (EGF; MIM 131530)-like repeats or thrombospondin (THBS; see MIM 188060) type-1 repeats. POFUT2 is an O-fucosyltransferase that use THBS type-1 repeats as substrates (Luo et al., 2006 [PubMed 16464857]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: fucosyltransferase, thrombospondin-1, Epidermal Growth Factor, fibrillin-1, Pofut1
Papers on POFUT2
O-fucosylation of CCN1 is required for its secretion.
Simizu et al., Yokohama, Japan. In Febs Lett, Nov 2015
Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.
Haltiwanger et al., Stony Brook, United States. In Curr Biol, Mar 2015
BACKGROUND: O-fucose is added to cysteine-rich domains called thrombospondin type 1 repeats (TSRs) by protein O-fucosyltransferase 2 (POFUT2) and is elongated with glucose by β3-glucosyltransferase (B3GLCT).
Novel roles for O-linked glycans in protein folding.
Haltiwanger et al., Stony Brook, United States. In Glycoconj J, 2014
Pofut2, a related enzyme that modifies Thrombospondin type I repeats (TSRs), has also been hypothesized to play a role in the folding and quality control of TSR-containing proteins.
6-alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin type-1 repeats by protein O-fucosyltransferases 1 and 2.
Haltiwanger et al., Stony Brook, United States. In Glycobiology, 2013
Protein O-fucosyltransferase 1 (Pofut1) and protein O-fucosyltransferase 2 (Pofut2) add O-linked fucose at distinct consensus sequences in properly folded epidermal growth factor (EGF)-like repeats and thrombospondin type-1 (TSR) repeats, respectively.
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.
Gut et al., Basel, Switzerland. In Embo J, 2012
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.
Structural insights into the mechanism of protein O-fucosylation.
Hurtado-Guerrero et al., Zaragoza, Spain. In Plos One, 2010
Two different enzymes are responsible for this modification, Protein O-fucosyltransferase 1 and 2 (POFUT1 and POFUT2, respectively).
O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation.
Holdener et al., Stony Brook, United States. In Dev Biol, 2010
In this study, we verified that mouse protein O-fucosyltransferase-2 (POFUT2) specifically adds O-fucose to TSRs.
O-fucosylation is required for ADAMTS13 secretion.
Majerus et al., Saint Louis, United States. In J Biol Chem, 2007
When the expression of protein O-fucosyltransferase 2 (POFUT2), the enzyme that transfers fucose to serines in TSRs, was reduced using siRNA, the secretion of ADAMTS13 decreased.
O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
Apte et al., Cleveland, United States. In J Biol Chem, 2007
Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
Identification and characterization of abeta1,3-glucosyltransferase that synthesizes the Glc-beta1,3-Fuc disaccharide on thrombospondin type 1 repeats.
Hofsteenge et al., Basel, Switzerland. In J Biol Chem, 2007
The activity profiles of beta1,3-glucosyltransferase and protein O-fucosyltransferase 2, the enzyme that carries out the first step in TSR O-fucosylation, superimpose in endoplasmic reticulum subfractions obtained by density gradient centrifugation.
Molecular cloning and characterization of a novel human beta1,3-glucosyltransferase, which is localized at the endoplasmic reticulum and glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat domain.
Narimatsu et al., Ibaraki, Japan. In Glycobiology, 2006
The TSR domain expressed in Escherichia coli was first fucosylated by the recombinant protein O-fucosyltransferase 2 (POFUT2), after which it became an acceptor substrate for the recombinant beta3Glc-T, which could apparently transfer Glc to the fucosylated TSR domain.
Molecular evolution of protein O-fucosyltransferase genes and splice variants.
Germot et al., Limoges, France. In Glycobiology, 2006
cDNA sequences and genomic structure of POFUT2 are reported.
Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats.
Panin et al., Stony Brook, United States. In J Biol Chem, 2006
A known homologue of O-fucosyltransferase 1 is putative protein O-fucosyltransferase 2. The cDNA sequence encoding O-fucosyltransferase 2 was originally identified during a data base search for fucosyltransferases in Drosophila.
Histology-based expression profiling yields novel prognostic markers in human glioblastoma.
Louis et al., Boston, United States. In J Neuropathol Exp Neurol, 2005
A set of RNAs (including POFUT2, PTDSR, PLOD2, ATF5, and HK2) that were differentially expressed in 3 initially studied, microdissected glioblastomas also provided prognostic information in an independent set of 28 glioblastomas that did not all have perinecrotic palisades.
The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development.
Guipponi et al., Genève, Switzerland. In Genomics, 2004
Here, we isolated and characterized C21orf80 (human chromosome 21 open reading frame 80), a potential novel protein O-fucosyltransferase gene that encodes three alternatively spliced transcripts.
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