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:
"Peptidase S8, pro-domain
".
FunFam 3: neuroendocrine convertase 2 isoform X1
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 9 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 |
---|---|---|
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
3 | P16519 (/IDA) P21661 (/IDA) P21661 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
2 | P21661 (/IDA) P21661 (/IDA) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | P21661 (/ISO) P21661 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | P21661 (/TAS) P21661 (/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).
|
2 | P16519 (/IPI) P28841 (/IPI) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P28841 (/EXP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P28841 (/IMP) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | P28841 (/IPI) |
There are 20 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 |
---|---|---|
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
6 | P28841 (/ISS) Q03333 (/ISS) Q5REC2 (/ISS) Q5REC2 (/ISS) Q5REC2 (/ISS) Q9GLR0 (/ISS) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
3 | P21661 (/IMP) P21661 (/IMP) P28841 (/IMP) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
3 | P16519 (/IDA) P21661 (/IDA) P21661 (/IDA) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
3 | P21661 (/IMP) P21661 (/IMP) P28841 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Nervous system development GO:0007399
The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
|
2 | P21661 (/IEP) P21661 (/IEP) |
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
2 | P21661 (/IDA) P21661 (/IDA) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Protein autoprocessing GO:0016540
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
|
2 | P21661 (/IDA) P21661 (/IDA) |
Insulin processing GO:0030070
The formation of mature insulin by proteolysis of the precursor preproinsulin. The signal sequence is first cleaved from preproinsulin to form proinsulin; proinsulin is then cleaved to release the C peptide, leaving the A and B chains of mature insulin linked by disulfide bridges.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Enkephalin processing GO:0034230
The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide.
|
2 | P21661 (/IDA) P21661 (/IDA) |
Islet amyloid polypeptide processing GO:0034231
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
|
2 | P21661 (/ISO) P21661 (/ISO) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | P16519 (/IDA) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9GLR0 (/ISS) |
Nervous system development GO:0007399
The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
|
1 | Q9GLR0 (/ISS) |
Protein autoprocessing GO:0016540
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
|
1 | Q9GLR0 (/ISS) |
Insulin processing GO:0030070
The formation of mature insulin by proteolysis of the precursor preproinsulin. The signal sequence is first cleaved from preproinsulin to form proinsulin; proinsulin is then cleaved to release the C peptide, leaving the A and B chains of mature insulin linked by disulfide bridges.
|
1 | P16519 (/IDA) |
Enkephalin processing GO:0034230
The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide.
|
1 | P16519 (/ISS) |
Islet amyloid polypeptide processing GO:0034231
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
|
1 | P28841 (/IMP) |
Islet amyloid polypeptide processing GO:0034231
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
|
1 | P16519 (/ISS) |
There are 17 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 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.
|
6 | P28841 (/ISS) Q03333 (/ISS) Q5REC2 (/ISS) Q5REC2 (/ISS) Q5REC2 (/ISS) Q9GLR0 (/ISS) |
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.
|
3 | P16519 (/IDA) P21661 (/IDA) P21661 (/IDA) |
Secretory granule lumen GO:0034774
The volume enclosed by the membrane of a secretory granule.
|
3 | P21661 (/TAS) P21661 (/TAS) P28841 (/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 | P21661 (/ISO) P21661 (/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.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | P21661 (/TAS) P21661 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | P21661 (/ISO) P21661 (/ISO) |
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.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
2 | P21661 (/ISO) P21661 (/ISO) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
2 | P21661 (/ISO) P21661 (/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 | P16519 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P16519 (/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 | P28841 (/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 | P28841 (/IDA) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
1 | P28841 (/IDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | P16519 (/IDA) |