The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:
"Glutaredoxin
".
FunFam 78786: Protein disulfide-isomerase A2
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 5 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 |
|---|---|---|
|
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | D3Z6P0 (/TAS) Q13087 (/TAS) |
|
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 | Q13087 (/IPI) |
|
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
|
1 | Q13087 (/TAS) |
|
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | Q13087 (/IDA) |
|
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | D3Z6P0 (/ISO) |
There are 3 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.
|
1 | Q13087 (/TAS) |
|
Protein retention in ER lumen GO:0006621
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
|
1 | Q13087 (/TAS) |
|
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
1 | Q13087 (/TAS) |
There are 1 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 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 | Q13087 (/TAS) |