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Information on EC 2.4.1.256 - dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase and Organism(s) Homo sapiens

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IUBMB Comments
This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an alpha-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
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Homo sapiens
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Word Map
  • 2.4.1.256
  • lipid-linked
  • oligosaccharide
  • tomography
  • antidepressants
  • ligation-dependent
  • sanger
  • dilatation
  • n-glycosylation
  • neighbouring
  • arrhythmias
  • exercise-induced
  • t-wave
  • 12-lead
  • ejection
  • desmosome
  • arrhythmogenic
  • cardiomyopathy
  • bundle-branch
  • electrocardiogram
  • tachycardia
  • culprit
  • borderline
  • antipsychotics
  • probands
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alg10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-glucosyl phosphate:alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol alpha-1,2-glucosyltransferase
This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an alpha-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
compared to most GT-C superfamily enzymes, ALG10 shows two additional central membrane segments, resulting in a 1-8-4 organization with the N-terminus oriented toward the cytoplasmic face of the ER membrane and the C-terminus facing the lumen. The conserved patterns in ALG10 align with STT3 and DPY19
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AG10A_HUMAN
473
11
55606
Swiss-Prot
Secretory Pathway (Reliability: 1)
AG10B_HUMAN
473
11
55448
Swiss-Prot
Secretory Pathway (Reliability: 1)
F8VXJ0_HUMAN
126
3
14576
TrEMBL
Secretory Pathway (Reliability: 1)
F8VWA9_HUMAN
77
1
8790
TrEMBL
Secretory Pathway (Reliability: 2)
A8K8X3_HUMAN
473
11
55561
TrEMBL
Secretory Pathway (Reliability: 1)
F5H5T2_HUMAN
77
1
9018
TrEMBL
Secretory Pathway (Reliability: 2)
F5GZZ6_HUMAN
126
3
14616
TrEMBL
Secretory Pathway (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Albuquerque-Wendt, A.; Huette, H.J.; Buettner, F.F.R.; Routier, F.H.; Bakker, H.
Membrane topological model of glycosyltransferases of the GT-C superfamily
Int. J. Mol. Sci.
20
4842
2019
Homo sapiens (Q5BKT4)
Manually annotated by BRENDA team