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Information on EC 2.4.1.376 - EGF-domain serine glucosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8NBL1
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2.4.1.376 EGF-domain serine glucosyltransferaseIUBMB Comments
The enzyme, found in animals and insects, is involved in the biosynthesis of the alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-alpha-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
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Word Map
- 2.4.1.376
- notch
-
o-glucosylation
-
o-glucose
- drosophila
-
factor-like
- pofut1
-
o-fucosyltransferase
-
dowling-degos
-
o-linked
-
xylosyltransferases
- trisaccharide
-
xylosylation
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
=
+
+
[protein with EGF-like domain]-L-serine
=
+
[protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
Synonyms
protein o-glucosyltransferase, protein o-glucosyltransferase 1, poglut2, poglut3, poglut, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:[protein with EGF-like domain]-L-serine O-beta-glucosyltransferase (configuration-inverting)
The enzyme, found in animals and insects, is involved in the biosynthesis of the alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-alpha-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
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
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain 1]-L-serine
UDP + [factor VII protein with EGF-like domain 1]-3-O-(beta-D-glucosyl)-L-serine
-
-
-
?
UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 12]-L-serine
UDP + [Notch1 protein with EGF-like domain 12]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
-
-
?
UDP-alpha-D-glucose + [protein with EGF-like domain]-L-serine
UDP + [protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
-
-
?
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
highest activity
-
-
?
UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 11]-L-serine435
UDP + [Notch1 protein with EGF-like domain 11]-3-O-(beta-D-glucosyl)-L-serine435
-
-
-
-
?
UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain]-L-serine
UDP + [Notch1 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
when glycosylating EGF repeats, the enzyme exhibits significant protein O-xylosyltransferase, preferring EGF repeats with a diserine motif in the consensus O-glucosylation motif (C1-X-S-S-(P/A)-C2)
-
-
?
UDP-alpha-D-glucose + [Notch3 protein with EGF-like domain 10]-L-serine435
UDP + [Notch3 protein with EGF-like domain 10]-3-O-(beta-D-glucosyl)-L-serine435
-
-
-
-
?
additional information
?
-
-
the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
-
-
-
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
UDP-alpha-D-glucose + [protein with EGF-like domain]-L-serine
UDP + [protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
-
-
?
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
highest activity
-
-
?
UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 11]-L-serine435
UDP + [Notch1 protein with EGF-like domain 11]-3-O-(beta-D-glucosyl)-L-serine435
-
-
-
-
?
UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain]-L-serine
UDP + [Notch1 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
when glycosylating EGF repeats, the enzyme exhibits significant protein O-xylosyltransferase, preferring EGF repeats with a diserine motif in the consensus O-glucosylation motif (C1-X-S-S-(P/A)-C2)
-
-
?
UDP-alpha-D-glucose + [Notch3 protein with EGF-like domain 10]-L-serine435
UDP + [Notch3 protein with EGF-like domain 10]-3-O-(beta-D-glucosyl)-L-serine435
-
-
-
-
?
additional information
?
-
-
the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
-
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is necessary for efficient trafficking of endogenous Notch1 from the endoplasmic reticulum to the cell surface in HEK-293T cells
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). PGLT1_HUMAN
392
0
46189
Swiss-Prot
Secretory Pathway (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complexes with three different EGF-like domains and either UDP, UDP-2-deoxy-2-fluoro-glucose or UDP-methyl-glucose, hanging drop vapor diffusion method, using 10-20% (w/v) PEG 5000 MME, 50 mM MES pH 6.5, 2-10 mM CaCl2, 0-250 mM NaCl, 5-10% (v/v) glycerol or 2-methyl-2,4-pentanediol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D233E
-
the mutation causes a class of adult-onset limb-girdle muscular dystrophy with reduced Notch signaling in muscular stem cells, called satellite cells, and hypoglycosylation on alpha-dystroglycan in muscles
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG Sepharose affinity chromatography, HiTrap Sepharose column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, H.; Takeuchi, H.
Protein O-glucosylation another essential role of glucose in biology
Curr. Opin. Struct. Biol.
56
64-71
2019
Homo sapiens
Li, Z.; Fischer, M.; Satkunarajah, M.; Zhou, D.; Withers, S.; Rini, J.
Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1)
Nat. Commun.
8
185
2017
Homo sapiens (Q8NBL1), Homo sapiens
Takeuchi, H.; Fernandez-Valdivia, R.; Caswell, D.; Nita-Lazar, A.; Rana, N.; Garner, T.; Weldeghiorghis, T.; Macnaughtan, M.; Jafar-Nejad, H.; Haltiwanger, R.
Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
Proc. Natl. Acad. Sci. USA
108
16600-16605
2011
Homo sapiens, Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.4.1.376)
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Release 2023.1 (January 2023)
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