The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"Glutaredoxin
".
FunFam 32: Protein disulfide-isomerase A6 homolog
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 11 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 |
---|---|---|
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
12 |
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
(2 more) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
9 | O22263 (/ISS) O22263 (/ISS) O22263 (/ISS) O22263 (/ISS) P38660 (/ISS) Q5R6T1 (/ISS) Q5R6T1 (/ISS) Q63081 (/ISS) Q922R8 (/ISS) |
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).
|
3 | Q15084 (/IPI) Q15084 (/IPI) Q63081 (/IPI) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | Q86IA3 (/IGI) Q86IA3 (/IGI) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | O13811 (/IMP) O13811 (/IMP) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
|
2 | O13811 (/IMP) O13811 (/IMP) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
2 | Q15084 (/IDA) Q15084 (/IDA) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
1 | Q63081 (/TAS) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | Q922R8 (/ISO) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | Q9V438 (/ISS) |
There are 21 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.
|
12 |
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
Q00216 (/IDA)
(2 more) |
Platelet activation GO:0030168
A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.
|
5 | P38660 (/ISS) Q5R6T1 (/ISS) Q5R6T1 (/ISS) Q63081 (/ISS) Q922R8 (/ISS) |
Platelet aggregation GO:0070527
The adhesion of one platelet to one or more other platelets via adhesion molecules.
|
5 | P38660 (/ISS) Q5R6T1 (/ISS) Q5R6T1 (/ISS) Q63081 (/ISS) Q922R8 (/ISS) |
Embryo sac development GO:0009553
The process whose specific outcome is the progression of the embryo sac over time, from its formation to the mature structure. The process begins with the meiosis of the megasporocyte to form four haploid megaspores. Three of the megaspores disintegrate, and the fourth undergoes mitosis giving rise to a binucleate syncytial embryo sac. The two haploid nuclei migrate to the opposite poles of the embryo sac and then undergo two rounds of mitosis generating four haploid nuclei at each pole. One nucleus from each set of four migrates to the center of the cell. Cellularization occurs, resulting in an eight-nucleate seven-celled structure. This structure contains two synergid cells and an egg cell at the micropylar end, and three antipodal cells at the other end. A binucleate endosperm mother cell is formed at the center. The two polar nuclei fuse resulting in a mononucleate diploid endosperm mother cell. The three antipodal cells degenerate.
|
4 | O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) |
Double fertilization forming a zygote and endosperm GO:0009567
Fertilization where one of the two sperm nuclei from the pollen tube fuses with the egg nucleus to form a 2n zygote, and the other fuses with the two polar nuclei to form the 3n primary endosperm nucleus and then develops into the endosperm. The ploidy level of the 2n zygote and 3n primary endosperm nucleus is determined by the ploidy level of the parents involved. An example of this component is found in Arabidopsis thaliana.
|
4 | O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) |
Embryo development ending in seed dormancy GO:0009793
The process whose specific outcome is the progression of the embryo over time, from zygote formation to the end of seed dormancy. An example of this process is found in Arabidopsis thaliana.
|
4 | O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
4 | O22263 (/IEP) O22263 (/IEP) O22263 (/IEP) O22263 (/IEP) |
Response to cadmium ion GO:0046686
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 a cadmium (Cd) ion stimulus.
|
4 | O22263 (/IEP) O22263 (/IEP) O22263 (/IEP) O22263 (/IEP) |
Pollen tube development GO:0048868
The process whose specific outcome is the progression of a pollen tube over time, from its initial formation to a mature structure.
|
4 | O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) O22263 (/IMP) |
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.
|
3 | Q15084 (/TAS) Q15084 (/TAS) Q63081 (/TAS) |
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 | O13811 (/IMP) O13811 (/IMP) |
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 | Q86IA3 (/ISS) Q86IA3 (/ISS) |
Posttranscriptional regulation of gene expression GO:0010608
Any process that modulates the frequency, rate or extent of gene expression after the production of an RNA transcript.
|
2 | Q57WS0 (/IDA) Q57WS0 (/IDA) |
Cellular response to oxidative stress GO:0034599
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
2 | O13811 (/IMP) O13811 (/IMP) |
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).
|
2 | O13811 (/IC) O13811 (/IC) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Cellular protein metabolic process GO:0044267
The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes cellular protein modification.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
1 | Q11067 (/HEP) |
Positive regulation of apoptotic cell clearance GO:2000427
Any process that activates or increases the frequency, rate or extent of apoptotic cell clearance.
|
1 | Q9V438 (/IDA) |
Positive regulation of apoptotic cell clearance GO:2000427
Any process that activates or increases the frequency, rate or extent of apoptotic cell clearance.
|
1 | Q9V438 (/IMP) |
There are 29 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).
|
13 |
O13811 (/IDA)
O13811 (/IDA)
O22263 (/IDA)
O22263 (/IDA)
O22263 (/IDA)
O22263 (/IDA)
Q15084 (/IDA)
Q15084 (/IDA)
Q57WS0 (/IDA)
Q57WS0 (/IDA)
(3 more) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
5 | P38660 (/ISS) Q5R6T1 (/ISS) Q5R6T1 (/ISS) Q63081 (/ISS) Q922R8 (/ISS) |
Melanosome GO:0042470
A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
|
5 | P38660 (/ISS) Q5R6T1 (/ISS) Q5R6T1 (/ISS) Q63081 (/ISS) Q922R8 (/ISS) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
4 | O22263 (/IDA) O22263 (/IDA) O22263 (/IDA) O22263 (/IDA) |
Plant-type cell wall GO:0009505
A more or less rigid stucture lying outside the cell membrane of a cell and composed of cellulose and pectin and other organic and inorganic substances.
|
4 | O22263 (/IDA) O22263 (/IDA) O22263 (/IDA) O22263 (/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).
|
3 | Q4Q9C8 (/ISO) Q4Q9C8 (/ISO) Q922R8 (/ISO) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
2 | Q15084 (/IDA) Q15084 (/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).
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
2 | Q15084 (/TAS) Q15084 (/TAS) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
2 | Q15084 (/IDA) Q15084 (/IDA) |
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.
|
2 | Q57WS0 (/IDA) Q57WS0 (/IDA) |
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.
|
2 | Q4Q9C8 (/ISO) Q4Q9C8 (/ISO) |
Lipid droplet GO:0005811
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
|
2 | Q86IA3 (/HDA) Q86IA3 (/HDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q15084 (/IDA) Q15084 (/IDA) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
2 | Q15084 (/ISS) Q15084 (/ISS) |
Nuclear outer membrane-endoplasmic reticulum membrane network GO:0042175
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
|
2 | Q86IA3 (/IDA) Q86IA3 (/IDA) |
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
|
2 | Q86IA3 (/HDA) Q86IA3 (/HDA) |
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 | Q15084 (/HDA) Q15084 (/HDA) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
1 | Q922R8 (/ISO) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | Q63081 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | Q922R8 (/ISO) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | Q63081 (/IDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | Q922R8 (/ISO) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
1 | Q922R8 (/ISO) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
1 | Q63081 (/TAS) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q922R8 (/ISO) |
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
|
1 | Q9V438 (/HDA) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
1 | Q922R8 (/IDA) |