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:

"
Glutaredoxin
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 17: Protein disulfide-isomerase A4

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 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).
12 P11598 (/IPI) P13667 (/IPI) P13667 (/IPI) P17967 (/IPI) P17967 (/IPI) P27773 (/IPI) P30101 (/IPI) P30101 (/IPI) P30101 (/IPI) P30101 (/IPI)
(2 more)
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
11 A2QFJ8 (/IDA) A2QFJ8 (/IDA) A2QFJ8 (/IDA) G5ED07 (/IDA) P17967 (/IDA) P17967 (/IDA) P38659 (/IDA) Q4WH99 (/IDA) Q4WH99 (/IDA) Q4WH99 (/IDA)
(1 more)
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
10 F1SAD9 (/ISS) G3IDT6 (/ISS) G3RY30 (/ISS) H2QVK7 (/ISS) H9G279 (/ISS) H9G279 (/ISS) M3W9X1 (/ISS) P08003 (/ISS) P13667 (/ISS) P13667 (/ISS)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
7 P13667 (/HDA) P13667 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA)
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
7 P13667 (/IDA) P13667 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA)
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Cysteine-type endopeptidase activity GO:0004197
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Phospholipase C activity GO:0004629
Catalysis of the reaction: a phospholipid + H2O = 1,2-diacylglycerol + a phosphatidate.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
5 P30101 (/IPI) P30101 (/IPI) P30101 (/IPI) P30101 (/IPI) P30101 (/IPI)
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
2 P17967 (/IMP) P17967 (/IMP)
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
2 P08003 (/ISO) Q10057 (/ISO)
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
2 P17967 (/IDA) P17967 (/IDA)
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
2 P08003 (/ISO) P27773 (/ISO)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
2 P17967 (/IDA) P17967 (/IDA)
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 G5ED07 (/IDA)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
1 P11598 (/IDA)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
1 P27773 (/ISO)
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
1 Q10057 (/ISO)
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
1 Q3YMU0 (/ISS)
Protein-disulfide reductase (glutathione) activity GO:0019153
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
1 P11598 (/IMP)
Protein-disulfide reductase (glutathione) activity GO:0019153
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
1 P27773 (/ISO)
MHC class I protein binding GO:0042288
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
1 P11598 (/IDA)
MHC class I protein binding GO:0042288
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
1 P27773 (/ISO)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P27773 (/ISO)

There are 44 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
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
10 F1SAD9 (/ISS) G3IDT6 (/ISS) G3RY30 (/ISS) H2QVK7 (/ISS) H9G279 (/ISS) H9G279 (/ISS) M3W9X1 (/ISS) P08003 (/ISS) P13667 (/ISS) P13667 (/ISS)
Antigen processing and presentation of peptide antigen via MHC class I GO:0002474
The process in which an antigen-presenting cell expresses a peptide antigen on its cell surface in association with an MHC class I protein complex. Class I here refers to classical class I molecules.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent GO:0002479
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex following intracellular transport via a TAP (transporter associated with antigen processing) pathway. The peptide is typically a fragment of a larger exogenous protein which has been degraded within the cell and is dependent on TAP transport from the cytosol to ER for association with the MHC class I molecule. Class I here refers to classical class I molecules.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/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.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/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).
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/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.
3 A2QFJ8 (/IDA) A2QFJ8 (/IDA) A2QFJ8 (/IDA)
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 P17967 (/IMP) P17967 (/IMP)
Protein secretion GO:0009306
The controlled release of proteins from a cell.
2 P13667 (/TAS) P13667 (/TAS)
Protein alpha-1,2-demannosylation GO:0036508
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein.
2 P17967 (/IDA) P17967 (/IDA)
Positive regulation of protein folding GO:1903334
Any process that activates or increases the frequency, rate or extent of protein folding.
2 P11598 (/IDA) P38659 (/IDA)
Positive regulation of protein folding GO:1903334
Any process that activates or increases the frequency, rate or extent of protein folding.
2 P08003 (/ISO) P27773 (/ISO)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
2 P17967 (/IDA) P17967 (/IDA)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
2 P17967 (/IGI) P17967 (/IGI)
Mannose trimming involved in glycoprotein ERAD pathway GO:1904382
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein that occurs as part of glycoprotein ER-associated glycoprotein degradation (gpERAD).
2 P17967 (/IMP) P17967 (/IMP)
Response to hypoxia GO:0001666
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 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 P11598 (/IEP)
Response to ischemia GO:0002931
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a inadequate blood supply.
1 P11598 (/IEP)
Circadian rhythm GO:0007623
Any biological process in an organism that recurs with a regularity of approximately 24 hours.
1 P11598 (/IEP)
Regulation of cell shape GO:0008360
Any process that modulates the surface configuration of a cell.
1 G5ED07 (/IGI)
Body morphogenesis GO:0010171
The process in which the anatomical structures of the soma are generated and organized.
1 G5ED07 (/IGI)
Peptide cross-linking GO:0018149
The formation of a covalent cross-link between or within protein chains.
1 G5ED07 (/IDA)
Oviposition GO:0018991
The deposition of eggs (either fertilized or not) upon a surface or into a medium such as water.
1 G5ED07 (/IGI)
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 P34329 (/HEP)
Response to nutrient levels GO:0031667
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 stimulus reflecting the presence, absence, or concentration of nutrients.
1 P11598 (/IEP)
Response to genistein GO:0033595
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 genistein stimulus.
1 P11598 (/IEP)
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 Q10057 (/IC)
Collagen and cuticulin-based cuticle development GO:0040002
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
1 G5ED07 (/IGI)
Collagen and cuticulin-based cuticle development GO:0040002
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
1 G5ED07 (/IMP)
Positive regulation of embryonic development GO:0040019
Any process that activates or increases the frequency, rate or extent of embryonic development.
1 G5ED07 (/IGI)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
1 P38657 (/ISS)
Response to leptin GO:0044321
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 leptin stimulus. Leptin is a hormone manufactured primarily in the adipocytes of white adipose tissue, and the level of circulating leptin is directly proportional to the total amount of fat in the body. It plays a key role in regulating energy intake and energy expenditure, including appetite and metabolism].
1 P11598 (/IEP)
Nematode male tail tip morphogenesis GO:0045138
The process in which the anatomical structure of the adult male tail tip is generated and organized. In some species of rhabitid nematodes, the male tail tip undergoes a morphological change such that the most posterior hypodermal cells in the tail (hyp8-11 in C. elegans) fuse and retract anteriorly, changing the shape of the tail from a pointed, tapered cone, or spike, to a rounded, blunt dome.
1 G5ED07 (/IGI)
Response to ethanol GO:0045471
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 an ethanol stimulus.
1 P11598 (/IEP)
Response to hyperoxia GO:0055093
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 stimulus indicating increased oxygen tension.
1 P11598 (/IEP)
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
1 P38659 (/IDA)
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
1 P08003 (/ISO)
Cellular response to vitamin D GO:0071305
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 vitamin D stimulus.
1 P11598 (/IDA)
Cellular response to vitamin D GO:0071305
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 vitamin D stimulus.
1 P27773 (/ISO)
Cellular response to transforming growth factor beta stimulus GO:0071560
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 transforming growth factor beta stimulus.
1 P11598 (/IEP)
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 G5ED07 (/IDA)
Nematode male tail mating organ morphogenesis GO:0090597
The process in which the anatomical structures of the nematode male tail mating organ are generated and organized. The male tail is a sensory organ required for mating and, in C. elegans, consists of ray sensilla, an acellular cuticular fan, a sensory hook, and protracting, copulatory spicules.
1 G5ED07 (/IGI)
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 P27773 (/IDA)
Response to benzene GO:1901423
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 benzene stimulus.
1 P11598 (/IEP)
Cellular response to nonylphenol GO:1904148
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 nonylphenol stimulus.
1 P11598 (/IEP)
Positive regulation of extrinsic apoptotic signaling pathway GO:2001238
Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.
1 P27773 (/IMP)

There are 42 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 P08003 (/IDA) P11598 (/IDA) P27773 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) V9HVY3 (/IDA) V9HVY3 (/IDA)
(3 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).
13 P11598 (/ISS) P38657 (/ISS) Q4VIT4 (/ISS) Q4VIT4 (/ISS) Q4VIT4 (/ISS) Q4VIT4 (/ISS) Q4VIT4 (/ISS) Q4VIT4 (/ISS) Q5RDG4 (/ISS) Q5RDG4 (/ISS)
(3 more)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
11 A0A1D8PR99 (/IDA) P08003 (/IDA) P11598 (/IDA) P13667 (/IDA) P13667 (/IDA) P27773 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA)
(1 more)
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.
8 P11598 (/IDA) P13667 (/IDA) P13667 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
8 P13667 (/TAS) P13667 (/TAS) P27773 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
MHC class I peptide loading complex GO:0042824
A large, multisubunit complex which consists of the MHC class I-beta 2 microglobulin dimer, the transporter associated with antigen presentation (TAP), tapasin (an MHC-encoded membrane protein), the chaperone calreticulin and the thiol oxidoreductase ERp57. Functions in the assembly of peptides with newly synthesized MHC class I molecules.
6 P11598 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA) P30101 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
5 P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA)
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).
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
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.
5 P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA)
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
Recycling endosome membrane GO:0055038
The lipid bilayer surrounding a recycling endosome.
5 P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS) P30101 (/TAS)
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.
5 P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA) P30101 (/HDA)
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 P17967 (/HDA) P17967 (/HDA) Q10057 (/HDA)
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 A0A1D8PR99 (/IDA) P11598 (/IDA)
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 P08003 (/ISO) P27773 (/ISO)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
2 P17967 (/IDA) P17967 (/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.
2 P11598 (/IDA) P38659 (/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.
2 P08003 (/ISO) P27773 (/ISO)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
2 P08003 (/ISO) P27773 (/ISO)
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
1 P11598 (/IDA)
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
1 P27773 (/ISO)
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.
1 P27773 (/ISO)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P11598 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P27773 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P11598 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P27773 (/ISO)
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.
1 P11598 (/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.
1 P27773 (/ISO)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
1 P11598 (/IDA)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
1 P27773 (/ISO)
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 P27773 (/ISO)
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
1 Q10057 (/ISO)
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.
1 P11598 (/IDA)
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.
1 P27773 (/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 Q3YMU0 (/HDA)
Apical plasma membrane GO:0016324
The region of the plasma membrane located at the apical end of the cell.
1 P11598 (/IDA)
Apical plasma membrane GO:0016324
The region of the plasma membrane located at the apical end of the cell.
1 P27773 (/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 P08003 (/IDA)
MHC class I peptide loading complex GO:0042824
A large, multisubunit complex which consists of the MHC class I-beta 2 microglobulin dimer, the transporter associated with antigen presentation (TAP), tapasin (an MHC-encoded membrane protein), the chaperone calreticulin and the thiol oxidoreductase ERp57. Functions in the assembly of peptides with newly synthesized MHC class I molecules.
1 P27773 (/ISO)
TAP complex GO:0042825
A heterodimer composed of the subunits TAP1 and TAP2 (transporter associated with antigen presentation). Functions in the transport of antigenic peptides from the cytosol to the lumen of the endoplasmic reticulum.
1 P11598 (/IDA)
TAP complex GO:0042825
A heterodimer composed of the subunits TAP1 and TAP2 (transporter associated with antigen presentation). Functions in the transport of antigenic peptides from the cytosol to the lumen of the endoplasmic reticulum.
1 P27773 (/ISO)
Myelin sheath GO:0043209
An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells: Schwann cells supply the myelin for peripheral neurons while oligodendrocytes supply it to those of the central nervous system.
1 P27773 (/HDA)
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