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 named:
"Golgi alpha-mannosidase II
".
FunFam 22: Glucosidase II alpha subunit
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 7 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 |
|---|---|---|
|
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
2 | Q14697 (/HDA) Q14697 (/HDA) |
|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
2 | Q14697 (/IPI) Q14697 (/IPI) |
|
Glucan 1,3-alpha-glucosidase activity GO:0033919
Catalysis of the hydrolysis of terminal (1->3)-alpha-D-glucosidic links in 1,3-alpha-D-glucans.
|
2 | Q14697 (/IDA) Q14697 (/IDA) |
|
Alpha-glucosidase activity GO:0090599
Catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose.
|
2 | Q14697 (/IDA) Q14697 (/IDA) |
|
Alpha-1,4-glucosidase activity GO:0004558
Catalysis of the hydrolysis of terminal, non-reducing alpha-(1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
|
1 | Q8BVW0 (/IDA) |
|
Glucan 1,3-alpha-glucosidase activity GO:0033919
Catalysis of the hydrolysis of terminal (1->3)-alpha-D-glucosidic links in 1,3-alpha-D-glucans.
|
1 | Q4R4N7 (/ISS) |
|
Alpha-glucosidase activity GO:0090599
Catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose.
|
1 | Q4R4N7 (/ISS) |
There are 4 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 |
|---|---|---|
|
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
|
2 | Q14697 (/TAS) Q14697 (/TAS) |
|
N-glycan processing GO:0006491
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
|
2 | Q14697 (/IDA) Q14697 (/IDA) |
|
Glucose metabolic process GO:0006006
The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
|
1 | Q8BVW0 (/IC) |
|
N-glycan processing GO:0006491
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
|
1 | Q4R4N7 (/ISS) |
There are 7 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 lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q14697 (/TAS) Q14697 (/TAS) |
|
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | Q14697 (/HDA) Q14697 (/HDA) |
|
Glucosidase II complex GO:0017177
A heterodimeric complex that catalyzes the trimming of glucose residues from N-linked core glycans on newly synthesized glycoproteins.
|
2 | Q14697 (/IDA) Q14697 (/IDA) |
|
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
2 | Q14697 (/IMP) Q14697 (/IMP) |
|
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
2 | Q14697 (/HDA) Q14697 (/HDA) |
|
Glucosidase II complex GO:0017177
A heterodimeric complex that catalyzes the trimming of glucose residues from N-linked core glycans on newly synthesized glycoproteins.
|
1 | Q4R4N7 (/ISS) |
|
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | Q4R4N7 (/ISS) |
