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:
"Carboxypeptidase-like, regulatory domain
".
FunFam 4: Carboxypeptidase E
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 14 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).
|
3 | P15087 (/IPI) Q00493 (/IPI) Q00493 (/IPI) |
Carboxypeptidase activity GO:0004180
Catalysis of the hydrolysis of the terminal or penultimate peptide bond at the C-terminal end of a peptide or polypeptide.
|
2 | Q00493 (/IMP) Q00493 (/IMP) |
Carboxypeptidase activity GO:0004180
Catalysis of the hydrolysis of the terminal or penultimate peptide bond at the C-terminal end of a peptide or polypeptide.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Carboxypeptidase activity GO:0004180
Catalysis of the hydrolysis of the terminal or penultimate peptide bond at the C-terminal end of a peptide or polypeptide.
|
2 | P16870 (/TAS) P16870 (/TAS) |
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.
|
2 | Q00493 (/TAS) Q00493 (/TAS) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Neurexin family protein binding GO:0042043
Interacting selectively and non-covalently with neurexins, synaptic cell surface proteins related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals.
|
2 | P16870 (/IPI) P16870 (/IPI) |
Neurexin family protein binding GO:0042043
Interacting selectively and non-covalently with neurexins, synaptic cell surface proteins related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Cell adhesion molecule binding GO:0050839
Interacting selectively and non-covalently with a cell adhesion molecule.
|
2 | P16870 (/IPI) P16870 (/IPI) |
Cell adhesion molecule binding GO:0050839
Interacting selectively and non-covalently with a cell adhesion molecule.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Cobalt ion binding GO:0050897
Interacting selectively and non-covalently with a cobalt (Co) ion.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Carboxypeptidase activity GO:0004180
Catalysis of the hydrolysis of the terminal or penultimate peptide bond at the C-terminal end of a peptide or polypeptide.
|
1 | P15087 (/IDA) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
1 | P15087 (/IDA) |
Cobalt ion binding GO:0050897
Interacting selectively and non-covalently with a cobalt (Co) ion.
|
1 | P15087 (/IMP) |
There are 24 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 |
---|---|---|
Cardiac left ventricle morphogenesis GO:0003214
The process in which the left cardiac ventricle is generated and organized.
|
2 | P16870 (/IMP) P16870 (/IMP) |
Cardiac left ventricle morphogenesis GO:0003214
The process in which the left cardiac ventricle is generated and organized.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Cellular protein modification process GO:0006464
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
|
2 | P16870 (/NAS) P16870 (/NAS) |
Peptide metabolic process GO:0006518
The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Neuropeptide signaling pathway GO:0007218
The series of molecular signals generated as a consequence of a peptide neurotransmitter binding to a cell surface receptor.
|
2 | P16870 (/NAS) P16870 (/NAS) |
Wnt signaling pathway GO:0016055
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.
|
2 | P16870 (/IDA) P16870 (/IDA) |
Wnt signaling pathway GO:0016055
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
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 | Q00493 (/ISO) Q00493 (/ISO) |
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 | Q00493 (/IMP) Q00493 (/IMP) |
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 | Q00493 (/ISO) Q00493 (/ISO) |
Peptide hormone secretion GO:0030072
The regulated release of a peptide hormone from a cell.
|
2 | Q00493 (/IMP) Q00493 (/IMP) |
Protein localization to secretory granule GO:0033366
A process in which a protein is transported to, or maintained in, a location within a secretory granule.
|
2 | Q00493 (/IMP) Q00493 (/IMP) |
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 | Q00493 (/ISO) Q00493 (/ISO) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Protein localization to membrane GO:0072657
A process in which a protein is transported to, or maintained in, a specific location in a membrane.
|
2 | P16870 (/IDA) P16870 (/IDA) |
Protein localization to membrane GO:0072657
A process in which a protein is transported to, or maintained in, a specific location in a membrane.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Negative regulation of branching morphogenesis of a nerve GO:2000173
Any process that stops, prevents, or reduces the frequency, rate or extent of branching morphogenesis of a nerve.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Peptide metabolic process GO:0006518
The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
1 | P15087 (/IDA) |
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.
|
1 | P15087 (/IDA) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
1 | P15087 (/TAS) |
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 | P15087 (/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 | P15087 (/IDA) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
1 | P15087 (/IDA) |
Negative regulation of branching morphogenesis of a nerve GO:2000173
Any process that stops, prevents, or reduces the frequency, rate or extent of branching morphogenesis of a nerve.
|
1 | P15087 (/IMP) |
There are 26 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 |
---|---|---|
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.
|
3 | P15087 (/IDA) P16870 (/IDA) P16870 (/IDA) |
Secretory granule membrane GO:0030667
The lipid bilayer surrounding a secretory granule.
|
3 | P15087 (/IDA) Q00493 (/IDA) Q00493 (/IDA) |
Secretory granule membrane GO:0030667
The lipid bilayer surrounding a secretory granule.
|
3 | P15087 (/TAS) Q00493 (/TAS) Q00493 (/TAS) |
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 | Q00493 (/ISO) Q00493 (/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 | Q00493 (/HDA) Q00493 (/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 | Q00493 (/ISO) Q00493 (/ISO) |
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 | Q00493 (/ISO) Q00493 (/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.
|
2 | P16870 (/TAS) P16870 (/TAS) |
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
|
2 | Q00493 (/ISO) Q00493 (/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 | Q00493 (/ISO) Q00493 (/ISO) |
Secretory granule membrane GO:0030667
The lipid bilayer surrounding a secretory granule.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Dense core granule GO:0031045
Electron-dense organelle with a granular internal matrix; contains proteins destined to be secreted.
|
2 | Q00493 (/ISO) Q00493 (/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 | Q00493 (/ISO) Q00493 (/ISO) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
2 | Q00493 (/ISO) Q00493 (/ISO) |
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 | P16870 (/HDA) P16870 (/HDA) |
Synaptic membrane GO:0097060
A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
|
2 | Q00493 (/ISO) Q00493 (/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 | P15087 (/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.
|
1 | P15087 (/IDA) |
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
|
1 | P15087 (/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 | P15087 (/IDA) |
Dense core granule GO:0031045
Electron-dense organelle with a granular internal matrix; contains proteins destined to be secreted.
|
1 | P15087 (/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 | P15087 (/IDA) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
1 | P15087 (/IDA) |
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
1 | P15087 (/IDA) |
Synaptic membrane GO:0097060
A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
|
1 | P15087 (/IDA) |