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 23: Protein disulfide-isomerase
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 25 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 heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
7 | P05307 (/ISS) P09103 (/ISS) P21195 (/ISS) Q2HWU2 (/ISS) Q5R5B6 (/ISS) Q8R4U2 (/ISS) Q8R4U2 (/ISS) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
6 | C0H4Y6 (/IDA) C0H4Y6 (/IDA) C0H4Y6 (/IDA) P07237 (/IDA) P07237 (/IDA) Q17770 (/IDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
4 | D3Z6P0 (/TAS) P07237 (/TAS) P07237 (/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).
|
4 | P07237 (/IPI) P07237 (/IPI) P09103 (/IPI) Q13087 (/IPI) |
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
3 | P07237 (/IPI) P07237 (/IPI) P09103 (/IPI) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
3 | P07237 (/IDA) P07237 (/IDA) Q13087 (/IDA) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
2 | P07237 (/HDA) P07237 (/HDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | P07237 (/EXP) P07237 (/EXP) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | Q9FF55 (/ISS) Q9FF55 (/ISS) |
Procollagen-proline 4-dioxygenase activity GO:0004656
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2.
|
2 | P07237 (/TAS) P07237 (/TAS) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
2 | D3Z6P0 (/ISO) P09103 (/ISO) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
2 | P54399 (/ISS) P54399 (/ISS) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
2 | P07237 (/IDA) P07237 (/IDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | P04785 (/IMP) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | P09103 (/ISO) |
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
|
1 | Q17770 (/IDA) |
Procollagen-proline 4-dioxygenase activity GO:0004656
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2.
|
1 | P05307 (/ISS) |
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
1 | P09103 (/ISO) |
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
|
1 | Q1HGL1 (/IDA) |
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
|
1 | Q13087 (/TAS) |
Isomerase activity GO:0016853
Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
|
1 | Q1HGL1 (/IDA) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
1 | P04785 (/IPI) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
1 | P09103 (/ISO) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
1 | P04785 (/IPI) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
1 | P09103 (/ISO) |
There are 28 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.
|
3 | C0H4Y6 (/IDA) C0H4Y6 (/IDA) C0H4Y6 (/IDA) |
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline GO:0018401
The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase.
|
3 | P07237 (/IDA) P07237 (/IDA) Q17770 (/IDA) |
Response to oxidative stress GO:0006979
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 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 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Chylomicron assembly GO:0034378
The non-covalent aggregation and arrangement of proteins and lipids in the intestine to form a chylomicron.
|
2 | P07237 (/TAS) P07237 (/TAS) |
Very-low-density lipoprotein particle assembly GO:0034379
The non-covalent aggregation and arrangement of proteins and lipids in the liver to form a very-low-density lipoprotein particle.
|
2 | P07237 (/TAS) P07237 (/TAS) |
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.
|
2 | P07237 (/IMP) P07237 (/IMP) |
Interleukin-12-mediated signaling pathway GO:0035722
A series of molecular signals initiated by the binding of interleukin-12 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
2 | P07237 (/TAS) P07237 (/TAS) |
Interleukin-23-mediated signaling pathway GO:0038155
A series of molecular signals initiated by the binding of interleukin-23 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
2 | P07237 (/TAS) P07237 (/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 | P07237 (/TAS) P07237 (/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 | P07237 (/TAS) P07237 (/TAS) |
Positive regulation of viral entry into host cell GO:0046598
Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell.
|
2 | P07237 (/IMP) P07237 (/IMP) |
Cellular response to hypoxia GO:0071456
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 stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
|
2 | P07237 (/IMP) P07237 (/IMP) |
Regulation of oxidative stress-induced intrinsic apoptotic signaling pathway GO:1902175
Any process that modulates the frequency, rate or extent of an oxidative stress-induced intrinsic apoptotic signaling pathway.
|
2 | P07237 (/IMP) P07237 (/IMP) |
Nematode larval development GO:0002119
The process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew.
|
1 | A0A1S0S010 (/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.
|
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) |
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline GO:0018401
The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase.
|
1 | P09103 (/ISO) |
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline GO:0018401
The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase.
|
1 | P05307 (/ISS) |
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 | Q17770 (/HEP) |
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) |
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.
|
1 | P09103 (/ISO) |
Macromolecule modification GO:0043412
The covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties.
|
1 | Q17770 (/IDA) |
Positive regulation of viral entry into host cell GO:0046598
Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell.
|
1 | P09103 (/ISO) |
Oxidation-reduction process GO:0055114
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
|
1 | Q17770 (/IDA) |
Cellular response to hypoxia GO:0071456
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 stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
|
1 | P09103 (/ISO) |
Protein deglutathionylation GO:0080058
The protein modification process in which a glutathione molecule is removed from a protein amino acid by breaking a disulfide linkage.
|
1 | Q17770 (/IDA) |
Cellular response to interleukin-7 GO:0098761
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 an interleukin-7 stimulus.
|
1 | P09103 (/IDA) |
Regulation of oxidative stress-induced intrinsic apoptotic signaling pathway GO:1902175
Any process that modulates the frequency, rate or extent of an oxidative stress-induced intrinsic apoptotic signaling pathway.
|
1 | P09103 (/ISO) |
There are 31 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).
|
12 |
A0A024R8S5 (/IDA)
A0A024R8S5 (/IDA)
H7BZ94 (/IDA)
P07237 (/IDA)
P07237 (/IDA)
P09103 (/IDA)
P54399 (/IDA)
P54399 (/IDA)
Q17770 (/IDA)
Q2HWU2 (/IDA)
(2 more) |
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).
|
7 | P04785 (/ISS) P05307 (/ISS) P09102 (/ISS) P21195 (/ISS) Q5R5B6 (/ISS) Q8R4U2 (/ISS) Q8R4U2 (/ISS) |
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 | P07237 (/TAS) P07237 (/TAS) Q13087 (/TAS) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
3 | C0H4Y6 (/IDA) C0H4Y6 (/IDA) C0H4Y6 (/IDA) |
External side of plasma membrane GO:0009897
The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
|
3 | P07237 (/IDA) P07237 (/IDA) P09103 (/IDA) |
Procollagen-proline 4-dioxygenase complex GO:0016222
A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase.
|
3 | P07237 (/IDA) P07237 (/IDA) Q17770 (/IDA) |
Microneme GO:0020009
A small, elongated secretory organelle that forms part of the apical complex, located along the main axis of an apicomplexan parasite cell within the extreme apical region and at the periphery under the inner membrane complex. Of the specialized secretory compartments identified in apicomplexans, micronemes discharge their contents first, during initial contact of the parasite's apical pole with the host cell surface. Micronemal proteins function during parasite attachment and penetration into the target cell.
|
3 | C0H4Y6 (/IDA) C0H4Y6 (/IDA) C0H4Y6 (/IDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | P07237 (/NAS) P07237 (/NAS) |
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 | P54399 (/IDA) P54399 (/IDA) |
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
|
2 | P54399 (/IDA) P54399 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
2 | Q9FF55 (/IDA) Q9FF55 (/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 | P54399 (/HDA) P54399 (/HDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | P07237 (/TAS) P07237 (/TAS) |
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
|
2 | P54399 (/IDA) P54399 (/IDA) |
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 | P07237 (/IDA) P07237 (/IDA) |
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
2 | P07237 (/HDA) P07237 (/HDA) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
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.
|
2 | P54399 (/HDA) P54399 (/HDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Fusome GO:0045169
A large intracellular spectrin-rich structure that has been found in insect germline cells and mammalian hematopoietic cells. The fusome is an elongated, branched structure, formed from the spherical spectrosome organelle.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Cell pole GO:0060187
Either of two different areas at opposite ends of an axis of a cell.
|
2 | P54399 (/IDA) P54399 (/IDA) |
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 | P07237 (/HDA) P07237 (/HDA) |
Spindle envelope GO:0070732
An organelle envelope that surrounds the chromosomes and the central part of the spindle apparatus during mitosis and meiosis; observed in many invertebrates. The spindle envelope consists of membrane layers, called parafusorial membranes, derived from endoplasmic reticulum membrane; in male meiosis it forms during prometaphase and persists until early in the ensuing interphase.
|
2 | P54399 (/IDA) P54399 (/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 | P09103 (/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 | P09103 (/ISO) |
External side of plasma membrane GO:0009897
The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
|
1 | P09103 (/ISO) |
Procollagen-proline 4-dioxygenase complex GO:0016222
A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase.
|
1 | P09103 (/ISO) |
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 | P09103 (/IDA) |