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Information on EC 2.4.1.260 - dolichyl-P-Man:Man7GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession A8MR93

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IUBMB Comments
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate.
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Arabidopsis thaliana
UNIPROT: A8MR93
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
alg12, alg12 mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,6-mannosyltransferase
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
loss-of-function mutations in EBS4 results in transfer of incompletely assembled glycans to polypeptides. The complete assembly of the lipid-linked glycans is essential for successful quality control of defective glycoproteins in Arabidopsis
physiological function
overexpression of enzyme in a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, and a mutant lacking EBS3 activity, which catalyzes the ER luminal addition of two terminal alpha1,2 mannose residues in assembling the three-branched N-glycan precursor [glucose(Glc)]3(Man)9[N-acetylglucosamine(GlcNAc)]2, adds an alpha1,6-mannose to the truncated N-glycan precursor accumulated in the double mutant, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the EBS3 mutant suppressor phenotype
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG12_ARATH
497
11
57192
Swiss-Prot
Secretory Pathway (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E38K
the wild-type EBS4 gene but not the mutated EBS4 plasmid carrying the E38K mutation (ebs4-3) is able to complement the yeast DELTAalg12 mutation
R100W
residue R100 is located near the end of the largest luminal loop between the first two predicted transmembrane segments and is absolutely conserved in all known ALG9 enzymes. Mutation suppresses a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, BR1. The mutation prevents the Glc3Man9GlcNAc2 assembly and inhibits the endoplasmic reticulum-associated degradation of bri1-9. Overexpression of EBS4 in the R100W bri1-9 mutant, which encodes the Arabidopsis ortholog of the yeast ALG12 catalyzing the ER luminal alpha1,6 Man addition, adds an alpha1,6 Man to the truncated N-glycan precursor accumulated in R100W bri1-9, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the R100W suppressor phenotype
T70I
mutation leads to attenuated calcium response to the bacterial flagellin flg22 peptide and several other elicitors. Mutant protein is correctly targeted to the plasma membrane, and several of the receptors expressed in the T70I background are underglycosylated
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, Z.; Jin, H.; Fitchette, A.C.; Xia, Y.; Monk, A.M.; Faye, L.; Li, J.
Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis
Plant Cell
21
3792-3802
2009
Arabidopsis thaliana (A8MR93), Arabidopsis thaliana
Manually annotated by BRENDA team
Hong, Z.; Kajiura, H.; Su, W.; Jin, H.; Kimura, A.; Fujiyama, K.; Li, J.
Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis
Proc. Natl. Acad. Sci. USA
109
11437-11442
2012
Arabidopsis thaliana (A8MR93)
Manually annotated by BRENDA team
Trempel, F.; Eschen-Lippold, L.; Bauer, N.; Ranf, S.; Westphal, L.; Scheel, D.; Lee, J.
A mutation in asparagine-linked glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors
FEBS Lett.
2020
1873-3468
2020
Arabidopsis thaliana (A8MR93)
Manually annotated by BRENDA team