EC Number   |
General Information |
Reference |
|---|
   3.2.1.209 | malfunction |
endoplasmic reticulum mannosidase I knockdown does not affect binding of an endoplasmic reticulum-associated degradation substrate glycoprotein to EDEM1 |
715589 |
| 3.2.1.209 | physiological function |
endoplasmic reticulum mannosidase I activity is not required for association of H2a with EDEM1 |
715589 |
| 3.2.1.209 | physiological function |
in the MNS3 single mutant, formation of aberrant N-glycans is observed. A triple mutant lacking mannosidases MNS1, MNS2, both EC 3.2.1.209, and MNS3 reveals the almost exclusive presence of Man9GlcNAc2 glycans. The MNS triple mutants display short, radially swollen roots and altered cell walls. Pharmacological inhibition of class I alpha-mannosidases in wild-type seedlings results in a similar root phenotype |
751841 |
| 3.2.1.209 | physiological function |
mutation results in the formation of aberrant N-glycans in the Mns3 single mutant. In the Mns1/Mns2/Mns3 triple mutant, Man(9)GlcNAc(2) glycans are almost exclusively present. The Mns triple mutants display short, radially swollen roots and altered cell walls |
751841 |
| 3.2.1.209 | physiological function |
overexpression of misfolded protein leads to increased expression of mannosidase ERManI. Expression of ER degradation-enhancing mannosidase-like protein EDEM1 results in stabilization of a higher molecular weight form of ERManI. Knockdown of ERManI, but not EDEM1, diminishes basal endoplasmic reticulum-associated degradation |
754232 |
| 3.2.1.209 | physiological function |
presence of the lectin hOS-9 enhances ER-associated degradation (ERAD) of misfolded glycoproteins, the enhancement depends on the N-glycan structures of the substrate. N-glycans lacking the terminal mannose from the C branch are recognized by hOS-9 and targeted for degradation |
754087 |
