Proteins
Curated comments from UniProt
Type | Comment | Proteins |
---|---|---|
MNS4_ARATH | function | Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N-glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum-associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not seem to play role in N-glycan processing of correctly folded proteins destined for secretion. |
MNS4_ARATH | pathway | Protein modification; protein glycosylation. |
A0A1P8BC88_ARATH A0A1P8BC90_ARATH MNS4_ARATH | similarity | Belongs to the glycosyl hydrolase 47 family. |
Function
Gene Ontology
cellular component | |
---|---|
endoplasmic reticulum | ECO |
endoplasmic reticulum membrane | ECO |
endoplasmic reticulum quality control compartment | ECO |
molecular function | |
mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | ECO |
alpha-mannosidase activity | ECO |
calcium ion binding | ECO |
biological process | |
mannose trimming involved in glycoprotein ERAD pathway | ECO |
carbohydrate metabolic process | ECO |
endoplasmic reticulum mannose trimming | ECO |
protein glycosylation | ECO |
Interactions
Interaction Network
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