O70370
Gene name |
Ctss (Cats) |
Protein name |
Cathepsin S |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13040 |
EC number |
3.4.22.27: Cysteine endopeptidases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
8 structures for O70370
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4BPV | X-ray | 200 A | A/B/C/D/E/K | 116-340 | PDB |
| 4BQV | X-ray | 170 A | A/B/C/D/E/F/G/H | 116-340 | PDB |
| 4BS5 | X-ray | 125 A | A | 116-340 | PDB |
| 4BS6 | X-ray | 120 A | A/B | 116-340 | PDB |
| 4BSQ | X-ray | 196 A | A | 116-340 | PDB |
| 4MZO | X-ray | 147 A | A/B/C/D/E/F/G/H | 116-340 | PDB |
| 4MZS | X-ray | 185 A | A/B | 116-340 | PDB |
| AF-O70370-F1 | Predicted | AlphaFoldDB |
17 variants for O70370
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388642662 | 38 | L>I | No | EVA | |
| rs250718036 | 72 | L>F | No | EVA | |
| rs228354008 | 97 | L>S | No | EVA | |
| rs246388285 | 99 | R>Q | No | EVA | |
| rs3388642975 | 101 | G>D | No | EVA | |
| rs3388648662 | 103 | L>M | No | EVA | |
| rs217318565 | 106 | P>L | No | EVA | |
| rs3388646409 | 114 | T>S | No | EVA | |
| rs3388651698 | 126 | T>A | No | EVA | |
| rs3388645023 | 132 | K>N | No | EVA | |
| rs3388645062 | 145 | G>R | No | EVA | |
| rs3388644615 | 168 | I>L | No | EVA | |
| rs253031261 | 187 | K>E | No | EVA | |
| rs220525835 | 218 | T>M | No | EVA | |
| rs3388649821 | 269 | F>I | No | EVA | |
| rs3388648709 | 279 | P>L | No | EVA | |
| rs33128450 | 334 | Y>D | No | EVA |
No associated diseases with O70370
6 regional properties for O70370
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Cysteine peptidase, cysteine active site | 141 - 152 | IPR000169 |
| domain | Peptidase C1A, papain C-terminal | 123 - 339 | IPR000668 |
| domain | Cathepsin propeptide inhibitor domain (I29) | 36 - 96 | IPR013201 |
| active_site | Cysteine peptidase, histidine active site | 285 - 295 | IPR025660 |
| active_site | Cysteine peptidase, asparagine active site | 302 - 321 | IPR025661 |
| domain | Papain-like cysteine endopeptidase | 124 - 338 | IPR039417 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.22.27 | Cysteine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell surface | The external part of the cell wall and/or plasma membrane. |
| early endosome lumen | The volume enclosed by the membrane of an early endosome. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| intracellular membrane-bounded organelle | 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. |
| late endosome | A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center. |
| lysosome | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| phagocytic vesicle | A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| collagen binding | Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
| cysteine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. |
| cysteine-type peptidase activity | Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. |
| fibronectin binding | Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. |
| laminin binding | Binding to a laminin, a major glycoprotein constituent of the basement membrane of cells. |
| peptidase activity | 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. |
| proteoglycan binding | Binding to a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans. |
13 GO annotations of biological process
| Name | Definition |
|---|---|
| antigen processing and presentation of exogenous peptide antigen via MHC class II | The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class II protein complex. The peptide antigen is typically, but not always, processed from a whole protein. |
| antigen processing and presentation of peptide antigen | The process in which an antigen-presenting cell expresses peptide antigen in association with an MHC protein complex on its cell surface, including proteolysis and transport steps for the peptide antigen both prior to and following assembly with the MHC protein complex. The peptide antigen is typically, but not always, processed from an endogenous or exogenous protein. |
| basement membrane disassembly | The controlled breakdown of the basement membrane in the context of a normal process such as imaginal disc eversion. |
| bone resorption | The process in which specialized cells known as osteoclasts degrade the organic and inorganic portions of bone, and endocytose and transport the degradation products. |
| collagen catabolic process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
| immune response | Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. |
| positive regulation of cation channel activity | Any process that activates or increases the frequency, rate or extent of cation channel activity. |
| positive regulation of inflammatory response | Any process that activates or increases the frequency, rate or extent of the inflammatory response. |
| protein processing | 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. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| proteolysis involved in protein catabolic process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. |
| regulation of sensory perception of pain | Any process that modulates the frequency, rate or extent of the sensory perception of pain, the series of events required for an organism to receive a painful stimulus, convert it to a molecular signal, and recognize and characterize the signal. |
| response to acidic pH | 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 pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P09668 | CTSH | Pro-cathepsin H | Homo sapiens (Human) | PR |
| P49935 | Ctsh | Pro-cathepsin H | Mus musculus (Mouse) | PR |
| P56203 | Ctsw | Cathepsin W | Mus musculus (Mouse) | PR |
| Q8BM88 | Ctso | Cathepsin O | Mus musculus (Mouse) | PR |
| P00786 | Ctsh | Pro-cathepsin H | Rattus norvegicus (Rat) | PR |
| P22895 | P34 probable thiol protease | Glycine max (Soybean) (Glycine hispida) | PR | |
| O65493 | XCP1 | Cysteine protease XCP1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q94B08 | GCP1 | Germination-specific cysteine protease 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LT77 | RDL2 | Probable cysteine protease RDL2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRAPGHAAIR | WLFWMPLVCS | VAMEQLQRDP | TLDYHWDLWK | KTHEKEYKDK | NEEEVRRLIW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKNLKFIMIH | NLEYSMGMHT | YQVGMNDMGD | MTNEEILCRM | GALRIPRQSP | KTVTFRSYSN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTLPDTVDWR | EKGCVTEVKY | QGSCGACWAF | SAVGALEGQL | KLKTGKLISL | SAQNLVDCSN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EEKYGNKGCG | GGYMTEAFQY | IIDNGGIEAD | ASYPYKATDE | KCHYNSKNRA | ATCSRYIQLP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FGDEDALKEA | VATKGPVSVG | IDASHSSFFF | YKSGVYDDPS | CTGNVNHGVL | VVGYGTLDGK |
| 310 | 320 | 330 | |||
| DYWLVKNSWG | LNFGDQGYIR | MARNNKNHCG | IASYCSYPEI |