The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 4: alpha-1,2-Mannosidase

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 3 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Mannosyl-oligosaccharide 1,2-alpha-mannosidase activity GO:0004571
Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide.
3 E1BQI6 (/IMP) Q9BZQ6 (/IMP) Q9BZQ6 (/IMP)
Mannosyl-oligosaccharide 1,2-alpha-mannosidase activity GO:0004571
Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide.
1 Q2HXL6 (/IDA)
Mannosyl-oligosaccharide 1,2-alpha-mannosidase activity GO:0004571
Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide.
1 Q2HXL6 (/ISO)

There are 6 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
3 E1BQI6 (/IMP) Q9BZQ6 (/IMP) Q9BZQ6 (/IMP)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
2 Q9BZQ6 (/TAS) Q9BZQ6 (/TAS)
Glycoprotein catabolic process GO:0006516
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
1 Q2HXL6 (/IDA)
Proteasome-mediated ubiquitin-dependent protein catabolic process GO:0043161
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
1 Q2HXL6 (/IDA)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
1 Q2HXL6 (/IDA)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
1 Q2HXL6 (/ISO)

There are 2 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Endoplasmic reticulum quality control compartment GO:0044322
A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.
2 Q9BZQ6 (/TAS) Q9BZQ6 (/TAS)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
1 Q2HXL6 (/IDA)
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