Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling.

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Heteroglycan glucosidase 1; Belongs to the glycosyl hydrolase 31 family.

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Alpha-mannosidase I MNS4; 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 [...]

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Alpha-mannosidase I MNS5; 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 [...]

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Probable glucan 1,3-alpha-glucosidase; Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (By similarity). Essential for stable accumulation of the receptor EFR that determines the specific perception of bacterial elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Required for sustained activation of EFR-mediated signaling, but not receptor FLS2-mediated signaling elicited by the bacterial flagellin flg22.

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Calnexin homolog 2; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity).

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Heteroglycan glucosidase 1; Belongs to the glycosyl hydrolase 31 family.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Alpha-mannosidase I MNS4; 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 [...]

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Alpha-mannosidase I MNS5; 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 [...]

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Probable glucan 1,3-alpha-glucosidase; Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (By similarity). Essential for stable accumulation of the receptor EFR that determines the specific perception of bacterial elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Required for sustained activation of EFR-mediated signaling, but not receptor FLS2-mediated signaling elicited by the bacterial flagellin flg22.

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Calnexin homolog 2; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity).

Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.