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 19: Alpha-mannosidase 2
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 |
---|---|---|
Alpha-mannosidase activity GO:0004559
Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
|
1 | Q9LFR0 (/IDA) |
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).
|
1 | Q9LFR0 (/IPI) |
Mannosidase activity GO:0015923
Catalysis of the hydrolysis of mannosyl compounds, substances containing a group derived from a cyclic form of mannose or a mannose derivative.
|
1 | Q24451 (/IDA) |
There are 7 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 N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
|
1 | Q9LFR0 (/IDA) |
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 | Q24451 (/IMP) |
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
|
1 | Q24451 (/IDA) |
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
|
1 | Q24451 (/IMP) |
Rhodopsin biosynthetic process GO:0016063
The chemical reactions and pathways resulting in the formation of rhodopsin, a brilliant purplish-red, light-sensitive visual pigment found in the rod cells of the retinas.
|
1 | Q24451 (/IMP) |
Encapsulation of foreign target GO:0035010
Events resulting in the formation of a multilayered cellular sheath surrounding an invader and thus preventing its development. This defense mechanism is often seen in insects in response to nematodes or parasitoids, which are too large to be phagocytosed by individual hemocytes. In some organisms the capsule is blackened due to melanization.
|
1 | Q24451 (/IMP) |
Hyperosmotic salinity response GO:0042538
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
|
1 | Q9LFR0 (/IMP) |
There are 5 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 |
---|---|---|
Endosome GO:0005768
A vacuole to which materials ingested by endocytosis are delivered.
|
1 | Q9LFR0 (/IDA) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
1 | Q24451 (/NAS) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
1 | Q9LFR0 (/IDA) |
Golgi stack GO:0005795
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
|
1 | Q24451 (/NAS) |
Trans-Golgi network GO:0005802
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
|
1 | Q9LFR0 (/IDA) |