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Information on EC 2.4.1.225 - N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q9Y169

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IUBMB Comments
Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9Y169
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Drosophila melanogaster
Synonyms
diphosphoglucuronate:oligosaccharide uridine glucuronosyltransferase, exostosin, exostosin-1, exostosin-2, Exostosin1, Exostosin2, exotose-2, EXT-1, EXT-2, EXT-3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphoglucuronate:oligosaccharide uridine glucuronosyltransferase
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exostosin-1
exostosin-2
exotose-2
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extosin
284657, 284659
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gene EXTL1 glycosyltransferase
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gene EXTL2 glycosyltransferase
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glucuronosyltransferase
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heparan glucuronosyltransferase II
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heparan sulfate co-polymerase
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heparan sulfate glucuronosyltransferase
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N-acetylglucosaminylproteoglycan beta-1,4-glucuronosyltransferase
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sister of tout velu
48
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sister of tout-velu
48
c.f. EC 2.4.1.224
tout-velu
48
c.f. EC 2.4.1.224
UDP-glucuronate:oligosaccharide
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucuronate:N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase
Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
CAS REGISTRY NUMBER
COMMENTARY hide
145539-84-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
show the reaction diagram
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-
?
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
EXT isozymes are localized mainly in the cis- and middle-Golgi stacks. Rotini, Rti, mediates the retrograde transport of EXT enzymes within the Golgi complex. Rotini regulates the sub-compartmental distribution of EXTs in the Golgi
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations in the tumor suppressor genes EXT1 and EXT2 disturb heparan sulfate proteoglycan biosynthesis and cause multiple osteochondroma. A reduction in Rti shifts the steady-state distribution of EXTs to the trans-Golgi. These accumulated EXTs tend to be degraded and their re-entrance towards the route for polymerizing GAG chains is disengaged. Conversely, EXTs are mislocalized towards the transitional endoplasmic reticulum/cis-Golgi when Rti is overexpressed. Both loss of function and overexpression of rti result in incomplete heparan sulfate proteoglycans and perturb Hedgehog signaling
physiological function
exostosin (EXT) genes encode glycosyltransferases required for glycosaminoglycan chain polymerization in the biosynthesis of heparan sulfate proteoglycans. Synthesis of heparan sulfate proteoglycans requires sequential enzymatic modifications of glycoproteins in the Golgi. Drosophila Golgi phosphoprotein 3, GOLPH3 or rotini, Rti, regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins. Rti regulates the stability of EXTs. Proper function of EXTs depends not only on their enzymatic activities but also on their sub-compartmental distributions
malfunction
mutations in the tumor suppressor genes EXT1 and EXT2 disturb heparan sulfate proteoglycan biosynthesis and cause multiple osteochondroma. A reduction in Rti shifts the steady-state distribution of EXTs to the trans-Golgi. These accumulated EXTs tend to be degraded and their re-entrance towards the route for polymerizing GAG chains is disengaged. Conversely, EXTs are mislocalized towards the transitional endoplasmic reticulum/cis-Golgi when Rti is overexpressed. Both loss of function and overexpression of rti result in incomplete heparan sulfate proteoglycans and perturb Hedgehog signaling
physiological function
exostosin (EXT) genes encode glycosyltransferases required for glycosaminoglycan chain polymerization in the biosynthesis of heparan sulfate proteoglycans. Synthesis of heparan sulfate proteoglycans requires sequential enzymatic modifications of glycoproteins in the Golgi. Drosophila Golgi phosphoprotein 3, GOLPH3 or rotini, Rti, regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins. Rti regulates the stability of EXTs. Proper function of EXTs depends not only on their enzymatic activities but also on their sub-compartmental distributions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
EXT2_DROME
717
1
82726
Swiss-Prot
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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formation of heterooligomers of ttv and sotv, co-immunoprecipitation experiments
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Rti regulates the stability of EXT isozymes
Rti regulates the stability of EXT isozymes
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene EXT2, recombinant expression of Myc-DKK-tagged enzyme in S2 cells, interaction analysis with GOLPH3 via yeast two-hybrid assay
expressed in HEK-293 cells
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gene EXT1, recombinant expression of Myc-DKK-tagged enzyme in S2 cells, interaction analysis with GOLPH3 via yeast two-hybrid assay
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, C.; Belenkaya, T.Y.; Khodoun, M.; Tauchi, M.; Lin, X.; Lin, X.
Distinct and collaborative roles of Drosophila EXT family proteins in morphopgen signalling and gradient formation
Development
131
1563-1575
2005
Drosophila melanogaster
Manually annotated by BRENDA team
Bornemann, D.J.; Duncan, J.E.; Staatz, W.; Selleck, S.; Warrior, R.
Abrogation of heparan sulfate synthesis in Drosophila disrupts the Wingless, Hedgehog and Decapentaplegic signaling pathways
Development
131
1927-198
2004
Drosophila melanogaster
Manually annotated by BRENDA team
Dasgupta, U.; Dixit, B.L.; Rusch, M.; Selleck, S.; The, I.
Functional conservation of the human EXT1 tumor suppressor gene and its Drosophila homolog tout velu
Dev. Genes Evol.
217
555-561
2007
Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team
Nadanaka, S.; Kitagawa, H.
Heparan sulphate biosynthesis and disease
J. Biochem.
144
7-14
2008
Caenorhabditis elegans, Drosophila melanogaster (Q9V730), Drosophila melanogaster (Q9Y169), Homo sapiens, Homo sapiens (Q16394), Homo sapiens (Q93063)
Manually annotated by BRENDA team
Chang, W.L.; Chang, C.W.; Chang, Y.Y.; Sung, H.H.; Lin, M.D.; Chang, S.C.; Chen, C.H.; Huang, C.W.; Tung, K.S.; Chou, T.B.
The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins
Development
140
2798-2807
2013
Drosophila melanogaster (Q9V730), Drosophila melanogaster (Q9Y169)
Manually annotated by BRENDA team
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