P06815
Gene name |
CAPN1 |
Protein name |
Calpain-1 catalytic subunit |
Names |
Calcium-activated neutral proteinase 1, CANP 1, Calpain mu-type, Calpain-1 large subunit, Micromolar-calpain, muCANP |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
|
EC number |
3.4.22.52: 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
1 structures for P06815
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P06815-F1 | Predicted | AlphaFoldDB |
No variants for P06815
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P06815 | |||||
No associated diseases with P06815
6 regional properties for P06815
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | EF-hand domain | 148 - 202 | IPR002048-1 |
| domain | EF-hand domain | 203 - 238 | IPR002048-2 |
| binding_site | EF-Hand 1, calcium-binding site | 216 - 228 | IPR018247 |
| domain | Peptidase C2, calpain, large subunit, domain III | 3 - 102 | IPR022682 |
| domain | Peptidase C2, calpain, domain III | 1 - 110 | IPR022683 |
| domain | Calpain subdomain III | 2 - 112 | IPR033883 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.22.52 | Cysteine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent cysteine-type endopeptidase activity | Catalysis of the hydrolysis of nonterminal peptide bonds in a polypeptide chain by a mechanism using a cysteine residue at the enzyme active center, and requiring the presence of calcium. |
| 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| regulation of catalytic activity | Any process that modulates the activity of an enzyme. |
| self proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| RESGCSFVLA | LMQKHRRRER | RFGRDMETIG | FAVYEVPREL | VGQPALHLKR | DFFLANASRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RSEQFINLRE | VSTRFRLPPG | EYVVVPSTFE | PNKEGDFVLR | FFSEKRAGTQ | ELDDQIQANL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PDEQVLSAEE | IDENFKALFR | QLAGEDLEIS | VRELQTILNR | ITSKHKDLRT | KGFSMESCRS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MVNLMDRDGN | GKLGLVEFNI | LWNRIRNYLA | IFRKFDLDKS | GSMSAYEMRM | AIESAGFKLN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KKLYELIITR | YSEPDLAVDF | DNFVCCLVRL | ETMFRFFKTL | DTDLDGVVTF | DLFKWLQLTM |
| FA |