The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:
"Trypsin-like serine proteases
".
FunFam 3834: Transmembrane protease serine 9
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 13 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 | A0A0B4LEW8 (/ISM) P35005 (/ISM) P42278 (/ISM) |
|
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 | P00766 (/IPI) Q9Y337 (/IPI) |
|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | 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).
|
1 | Q9Y337 (/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 | Q9Y337 (/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 | 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).
|
1 | Q9Y337 (/NAS) |
|
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 (/IMP) |
|
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 | Q9D140 (/ISO) |
|
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) |
|
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).
|
1 | Q9KSQ6 (/IMP) |
|
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).
|
1 | Q9Y337 (/TAS) |
|
Serpin family protein binding GO:0097655
Interacting selectively and non-covalently with any member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors.
|
1 | P00766 (/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 |
|---|---|---|
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
3 | A0A0B4LEW8 (/ISM) P35005 (/ISM) P42278 (/ISM) |
|
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).
|
2 | Q9D140 (/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.
|
1 | Q9Y337 (/IMP) |
|
Positive regulation of antibacterial peptide production GO:0002803
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide production.
|
1 | Q9D140 (/ISO) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9KSQ6 (/ISS) |
|
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.
|
1 | Q9Y337 (/TAS) |
|
Positive regulation of G-protein coupled receptor protein signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q9Y337 (/IDA) |
|
Positive regulation of G-protein coupled receptor protein signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q9D140 (/ISO) |
There are 8 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 | Q9D140 (/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.
|
1 | Q9Y337 (/IMP) |
|
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 | 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.
|
1 | Q9Y337 (/TAS) |
|
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) |
|
Serine protease inhibitor complex GO:0097180
A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.
|
1 | P00766 (/IDA) |
|
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.
|
1 | Q9Y337 (/IDA) |
|
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.
|
1 | Q9D140 (/ISO) |
