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:
"Anaphylotoxins (complement system)
".
FunFam 3: Complement C4-A
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 |
---|---|---|
Complement binding GO:0001848
Interacting selectively and non-covalently with any component or product of the complement cascade.
|
1 | P0C0L5 (/IDA) |
Complement component C1q binding GO:0001849
Interacting selectively and non-covalently with the C1q component of the classical complement cascade.
|
1 | P0C0L4 (/IDA) |
Carbohydrate binding GO:0030246
Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
|
1 | P0C0L5 (/IDA) |
There are 8 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 |
---|---|---|
Complement activation GO:0006956
Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway.
|
2 | P0C0L4 (/IGI) P0C0L5 (/IGI) |
Complement activation GO:0006956
Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway.
|
2 | P0C0L4 (/TAS) P0C0L5 (/TAS) |
Regulation of complement activation GO:0030449
Any process that modulates the frequency, rate or extent of complement activation.
|
2 | P0C0L4 (/TAS) P0C0L5 (/TAS) |
Positive regulation of apoptotic cell clearance GO:2000427
Any process that activates or increases the frequency, rate or extent of apoptotic cell clearance.
|
2 | P0C0L4 (/IGI) P0C0L5 (/IGI) |
Opsonization GO:0008228
The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody.
|
1 | P0C0L5 (/TAS) |
Detection of molecule of bacterial origin GO:0032490
The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal.
|
1 | P0C0L5 (/IDA) |
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.
|
1 | P0C0L4 (/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.
|
1 | P0C0L4 (/TAS) |
There are 12 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 |
---|---|---|
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 | P0C0L4 (/TAS) P0C0L5 (/TAS) |
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 | P0C0L4 (/HDA) P0C0L5 (/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.
|
2 | P0C0L4 (/IDA) P0C0L5 (/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.
|
2 | P0C0L4 (/TAS) P0C0L5 (/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.
|
2 | P0C0L4 (/HDA) P0C0L5 (/HDA) |
Blood microparticle GO:0072562
A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids.
|
2 | P0C0L4 (/HDA) P0C0L5 (/HDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | P0C0L4 (/TAS) |
Axon GO:0030424
The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
|
1 | P0C0L4 (/IDA) |
Dendrite GO:0030425
A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
|
1 | P0C0L4 (/IDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
1 | P0C0L4 (/IDA) |
Other organism cell GO:0044216
A cell of a secondary organism with which the first organism is interacting.
|
1 | P0C0L5 (/IDA) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
|
1 | P0C0L4 (/IDA) |