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Alpha-mannosidase

Degrades free oligosaccharides in the vacuole.

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Alpha-mannosidase 2

Also known as Alpha-mannosidase 2 (Golgi alpha-mannosidase II) (AMan II) (AtGMII) (Man II) (Protein hybrid glycosylation 1).
Encodes a golgi alpha-mannosidase, an enzyme responsible for the formation of major complex-type N-glycans.

Alpha-mannosidase 2C1

Also known as Alpha-mannosidase 2C1 (Alpha mannosidase 6A8B) (Alpha-D-mannoside mannohydrolase) (Mannosidase alpha class 2C member 1).
MAN2C1: Belongs to the glycosyl hydrolase 38 family.

Protein type: EC 3.2.1.24; Glycan Metabolism - other glycan degradation; Hydrolase

Chromosomal Location of Human Ortholog: 15q24.2

Cellular Component: cytosol; vacuole

Molecular Function: alpha-mannosidase activity

Biological Process: mannose metabolic process; oligosaccharide catabolic process; protein deglycosylation

Alpha-mannosidase 2x

Also known as Alpha-mannosidase 2x (Alpha-mannosidase IIx) (Man IIx) (Mannosidase alpha class 2A member 2) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase).
MAN2A2: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. Belongs to the glycosyl hydrolase 38 family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.2.1.114; Glycan Metabolism - N-glycan biosynthesis; Hydrolase; Membrane protein, integral

Cellular Component: Golgi membrane

Molecular Function: alpha-mannosidase activity; hydrolase activity, hydrolyzing N-glycosyl compounds; mannosidase activity

Biological Process: mannose metabolic process; N-glycan processing; protein deglycosylation

Alpha-mannosidase I MNS4

Can convert Man9GlcNAc2 and Man8GlcNAc2 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.

Alpha-mannosidase I MNS5

Can convert Man9GlcNAc2 and Man8GlcNAc2 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.

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