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
".

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.
« Back to all FunFams

FunFam 10: Kallikrein related peptidase 11

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
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).
11 Q9H2R5 (/NAS) Q9P0G3 (/NAS) Q9P0G3 (/NAS) Q9UKQ9 (/NAS) Q9UKQ9 (/NAS) Q9UKQ9 (/NAS) Q9UKQ9 (/NAS) Q9UKQ9 (/NAS) Q9UKR3 (/NAS) Q9UKR3 (/NAS)
(1 more)
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).
5 P49862 (/TAS) P49862 (/TAS) Q9H2R5 (/TAS) Q9UBX7 (/TAS) Q9Y337 (/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 A0A0B6VJJ8 (/ISO) Q8CGR5 (/ISO) Q8CGR5 (/ISO) Q9D140 (/ISO)
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).
4 Q9H2R5 (/IPI) Q9UKR3 (/IPI) Q9UKR3 (/IPI) Q9Y337 (/IPI)
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.
4 A0A0B6VJJ8 (/ISO) Q91VE3 (/ISO) Q91VE3 (/ISO) Q9D140 (/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).
3 Q9P0G3 (/IDA) Q9P0G3 (/IDA) Q9Y337 (/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.
3 P49862 (/IMP) P49862 (/IMP) Q9Y337 (/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).
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
2 Q9UKR3 (/IDA) Q9UKR3 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 Q8CGR6 (/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).
1 Q9Y337 (/EXP)
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 Q9Y337 (/TAS)
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
1 Q8CGR6 (/ISO)
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
1 Q8CGR6 (/ISS)

There are 25 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
Cornification GO:0070268
A type of programmed cell death that occurs in the epidermis, morphologically and biochemically distinct from apoptosis. It leads to the formation of corneocytes, i.e. dead keratinocytes containing an amalgam of specific proteins (e.g., keratin, loricrin, SPR and involucrin) and lipids (e.g., fatty acids and ceramides), which are necessary for the function of the cornified skin layer (mechanical resistance, elasticity, water repellence and structural stability).
5 Q9P0G3 (/TAS) Q9P0G3 (/TAS) Q9UKR3 (/TAS) Q9UKR3 (/TAS) Q9Y337 (/TAS)
Positive regulation of antibacterial peptide production GO:0002803
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide production.
4 A0A0B6VJJ8 (/ISO) Q91VE3 (/ISO) Q91VE3 (/ISO) Q9D140 (/ISO)
Positive regulation of G protein-coupled receptor signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G protein-coupled receptor signaling pathway activity.
4 A0A0B6VJJ8 (/ISO) Q8CGR5 (/ISO) Q8CGR5 (/ISO) Q9D140 (/ISO)
Positive regulation of antibacterial peptide production GO:0002803
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide production.
3 P49862 (/IMP) P49862 (/IMP) Q9Y337 (/IMP)
Epidermis development GO:0008544
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
3 P49862 (/TAS) P49862 (/TAS) Q9Y337 (/TAS)
Positive regulation of G protein-coupled receptor signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G protein-coupled receptor signaling pathway activity.
3 Q9P0G3 (/IDA) Q9P0G3 (/IDA) Q9Y337 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 Q9P0G3 (/IDA) Q9P0G3 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 Q8CGR5 (/ISO) Q8CGR5 (/ISO)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 Q9UKR3 (/NAS) Q9UKR3 (/NAS)
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
2 Q9P0G3 (/IDA) Q9P0G3 (/IDA)
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
2 Q8CGR5 (/ISO) Q8CGR5 (/ISO)
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
2 P49862 (/TAS) P49862 (/TAS)
Negative regulation of G protein-coupled receptor signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G protein-coupled receptor signaling pathway.
2 Q9P0G3 (/IDA) Q9P0G3 (/IDA)
Negative regulation of G protein-coupled receptor signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G protein-coupled receptor signaling pathway.
2 Q8CGR5 (/ISO) Q8CGR5 (/ISO)
Negative regulation of G protein-coupled receptor signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G protein-coupled receptor signaling pathway.
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Positive regulation of G protein-coupled receptor signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G protein-coupled receptor signaling pathway activity.
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
2 Q9P0G3 (/IDA) Q9P0G3 (/IDA)
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
2 Q8CGR5 (/ISO) Q8CGR5 (/ISO)
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
2 Q9P0G3 (/IDA) Q9P0G3 (/IDA)
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
2 Q8CGR5 (/ISO) Q8CGR5 (/ISO)
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
2 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
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 Q8CGR6 (/IDA)

There are 16 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.
8 P49862 (/TAS) P49862 (/TAS) Q9D140 (/TAS) Q9P0G3 (/TAS) Q9P0G3 (/TAS) Q9UKR3 (/TAS) Q9UKR3 (/TAS) Q9Y337 (/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.
6 A0A0B6VJJ8 (/ISO) Q8CGR5 (/ISO) Q8CGR5 (/ISO) Q91VE3 (/ISO) Q91VE3 (/ISO) Q9D140 (/ISO)
Epidermal lamellar body GO:0097209
A specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
4 A0A0B6VJJ8 (/ISO) Q91VE3 (/ISO) Q91VE3 (/ISO) Q9D140 (/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.
3 Q8CGR6 (/IDA) Q9P0G3 (/IDA) Q9P0G3 (/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.
3 P49862 (/IMP) P49862 (/IMP) Q9Y337 (/IMP)
Epidermal lamellar body GO:0097209
A specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
3 P49862 (/IDA) P49862 (/IDA) Q9Y337 (/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 Q9QYN3 (/IDA) Q9QYN3 (/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 Q8CGR5 (/ISS) Q8CGR5 (/ISS)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 Q9UKR3 (/IDA) Q9UKR3 (/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 Q9UBX7 (/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.
1 Q9Y337 (/TAS)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q8CGR6 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q8CGR6 (/ISS)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 Q9Y337 (/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.
1 Q8CGR6 (/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.
1 Q9UBX7 (/HDA)