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:
"Trypsin-like serine proteases
".
FunFam 32: Kallikrein 1-related peptidase C9
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 |
---|---|---|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
23 |
P00755 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
(13 more) |
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).
|
23 |
P00755 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
(13 more) |
Hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides GO:0016811
Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
|
23 |
P00755 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
(13 more) |
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.
|
9 | P15948 (/IDA) P15948 (/IDA) P15949 (/IDA) P36368 (/IDA) P36369 (/IDA) P36369 (/IDA) Q61759 (/IDA) Q61759 (/IDA) Q9JM71 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
5 | A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) P07288 (/IDA) P07288 (/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).
|
5 | P06870 (/TAS) P06870 (/TAS) P20151 (/TAS) P20151 (/TAS) P36376 (/TAS) |
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).
|
4 | P15945 (/IDA) P20151 (/IDA) P20151 (/IDA) Q9JM71 (/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).
|
3 | P06870 (/NAS) P06870 (/NAS) Q61754 (/NAS) |
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 | P07288 (/IMP) P07288 (/IMP) |
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 | P07288 (/IPI) P07288 (/IPI) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of 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 | P00759 (/IDA) P00759 (/IDA) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of 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 | P07288 (/TAS) P07288 (/TAS) |
Hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides GO:0016811
Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
|
2 | P07288 (/IMP) P07288 (/IMP) |
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 | P15945 (/ISM) |
There are 22 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 |
---|---|---|
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
6 | P15948 (/IDA) P15948 (/IDA) P15949 (/IDA) P36368 (/IDA) P36369 (/IDA) P36369 (/IDA) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
4 | P15945 (/IDA) Q61759 (/IDA) Q61759 (/IDA) Q9JM71 (/IDA) |
Positive regulation of acute inflammatory response GO:0002675
Any process that activates or increases the frequency, rate, or extent of an acute inflammatory response.
|
3 | A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
Response to nutrient GO:0007584
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 nutrient stimulus.
|
3 | A0A0G2JX00 (/IEP) A0A0G2K6G1 (/IEP) G3V8H1 (/IEP) |
Positive regulation of cell population proliferation GO:0008284
Any process that activates or increases the rate or extent of cell proliferation.
|
3 | A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
|
3 | A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
Brain renin-angiotensin system GO:0002035
The process in which an angiotensin-mediated signaling system present in the brain regulates the force with which blood passes through the circulatory system.
|
2 | P36369 (/IDA) P36369 (/IDA) |
Tissue kallikrein-kinin cascade GO:0002255
A series of reactions that takes place outside the cell initiated by the action of tissue (glandular) kallikreins on low molecular weight kininogen in response to tissue damage. Tissue kallikreins are present in glandular tissues and their fluids, such as the salivary glands, sweat glands, pancreas, and kidney. The ultimate products of the tissue kallikrein-kinin cascade include kallidin and bradykinin, agents known to induce smooth muscle contraction, vasoconstriction, and increased vascular permeability.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Antibacterial peptide production GO:0002778
The synthesis or release of an antibacterial peptide during an immune response, resulting in an increase in intracellular or extracellular levels.
|
2 | P07288 (/IDA) P07288 (/IDA) |
Bradykinin biosynthetic process GO:0002936
The chemical reactions and pathways resulting in the formation of the peptide hormone bradykinin.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Regulation of systemic arterial blood pressure GO:0003073
The process that modulates the force with which blood travels through the systemic arterial circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Left ventricular cardiac muscle tissue morphogenesis GO:0003220
The process in which the anatomical structures of left cardiac ventricle muscle are generated and organized.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | P07288 (/IMP) P07288 (/IMP) |
Small GTPase mediated signal transduction GO:0007264
Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals.
|
2 | P00757 (/IDA) P00757 (/IDA) |
Negative regulation of angiogenesis GO:0016525
Any process that stops, prevents, or reduces the frequency, rate or extent of angiogenesis.
|
2 | P07288 (/NAS) P07288 (/NAS) |
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
|
2 | P20151 (/TAS) P20151 (/TAS) |
Vasodilation GO:0042311
An increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Positive regulation of phosphatidylinositol 3-kinase activity GO:0043552
Any process that activates or increases the frequency, rate or extent of phosphatidylinositol 3-kinase activity.
|
2 | P00757 (/IDA) P00757 (/IDA) |
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 | P07288 (/TAS) P07288 (/TAS) |
Positive regulation of vasoconstriction GO:0045907
Any process that activates or increases the frequency, rate or extent of vasoconstriction.
|
2 | P07647 (/IDA) P07647 (/IDA) |
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
|
2 | P00755 (/IMP) P00755 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q61754 (/NAS) |
There are 11 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.
|
23 |
P00755 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
(13 more) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
23 |
P00755 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
(13 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.
|
7 | P07288 (/IDA) P07288 (/IDA) P36368 (/IDA) P36369 (/IDA) P36369 (/IDA) Q61759 (/IDA) Q61759 (/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.
|
6 | P06870 (/HDA) P06870 (/HDA) P07288 (/HDA) P07288 (/HDA) P20151 (/HDA) P20151 (/HDA) |
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 | A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) P06870 (/IDA) P06870 (/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.
|
4 | P07288 (/TAS) P07288 (/TAS) P20151 (/TAS) P20151 (/TAS) |
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.
|
3 | A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) |
Apical part of cell GO:0045177
The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
|
3 | A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/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 | P07288 (/NAS) P07288 (/NAS) |
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 | P07288 (/HDA) P07288 (/HDA) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
2 | P07288 (/IDA) P07288 (/IDA) |