P97571
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 |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:29153 |
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
11 structures for P97571
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1KXR | X-ray | 207 A | A/B | 27-356 | PDB |
| 1QXP | X-ray | 280 A | A/B | 60-647 | PDB |
| 1TL9 | X-ray | 180 A | A | 27-356 | PDB |
| 1TLO | X-ray | 190 A | A | 27-356 | PDB |
| 2G8E | X-ray | 225 A | A | 27-356 | PDB |
| 2G8J | X-ray | 161 A | A | 27-356 | PDB |
| 2NQG | X-ray | 204 A | A | 27-356 | PDB |
| 2NQI | X-ray | 204 A | A | 27-356 | PDB |
| 2R9C | X-ray | 180 A | A | 27-356 | PDB |
| 2R9F | X-ray | 160 A | A | 27-356 | PDB |
| AF-P97571-F1 | Predicted | AlphaFoldDB |
No variants for P97571
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P97571 | |||||
No associated diseases with P97571
8 regional properties for P97571
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Cysteine peptidase, cysteine active site | 109 - 120 | IPR000169 |
| domain | Peptidase C2, calpain, catalytic domain | 37 - 362 | IPR001300 |
| domain | EF-hand domain | 557 - 613 | IPR002048-1 |
| domain | EF-hand domain | 614 - 649 | IPR002048-2 |
| binding_site | EF-Hand 1, calcium-binding site | 627 - 639 | IPR018247 |
| domain | Peptidase C2, calpain, large subunit, domain III | 371 - 513 | IPR022682 |
| domain | Peptidase C2, calpain, domain III | 365 - 521 | IPR022683 |
| domain | Calpain subdomain III | 366 - 523 | 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 | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cornified envelope | A type of plasma membrane that has been modified through addition of distinct intracellular and extracellular components, including ceramide, found in cornifying epithelial cells (corneocytes). |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 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. |
| cytoskeletal protein binding | Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). |
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| 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. |
17 GO annotations of biological process
| Name | Definition |
|---|---|
| aging | A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). |
| brain development | The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.). |
| cellular response to hydrogen peroxide | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus. |
| mammary gland involution | The tissue remodeling that removes differentiated mammary epithelia during weaning. |
| negative regulation of actin filament polymerization | Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization. |
| negative regulation of NIK/NF-kappaB signaling | Any process that stops, prevents or reduces the frequency, rate or extent of NIK/NF-kappaB signaling. |
| positive regulation of cardiac muscle cell apoptotic process | Any process that increases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death. |
| positive regulation of leukocyte tethering or rolling | Any process that activates or increases the frequency, rate or extent of leukocyte tethering or rolling. |
| positive regulation of vascular permeability | Any process that increases the extent to which blood vessels can be pervaded by fluid. |
| protein autoprocessing | Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| receptor catabolic process | The chemical reactions and pathways resulting in the breakdown of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
| regulation of catalytic activity | Any process that modulates the activity of an enzyme. |
| response to angiotensin | 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 an angiotensin stimulus. Angiotensin is any of three physiologically active peptides (angiotensin II, III, or IV) processed from angiotensinogen. |
| response to arsenic-containing substance | 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 an arsenic stimulus from compounds containing arsenic, including arsenates, arsenites, and arsenides. |
| self proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds. |
19 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q27971 | CAPN2 | Calpain-2 catalytic subunit | Bos taurus (Bovine) | PR |
| Q27970 | CAPN1 | Calpain-1 catalytic subunit | Bos taurus (Bovine) | PR |
| P00789 | Calpain-1 catalytic subunit | Gallus gallus (Chicken) | PR | |
| Q9VXH6 | CalpC | Calpain-C | Drosophila melanogaster (Fruit fly) | PR |
| O14815 | CAPN9 | Calpain-9 | Homo sapiens (Human) | PR |
| Q6MZZ7 | CAPN13 | Calpain-13 | Homo sapiens (Human) | PR |
| Q9HC96 | CAPN10 | Calpain-10 | Homo sapiens (Human) | PR |
| P07384 | CAPN1 | Calpain-1 catalytic subunit | Homo sapiens (Human) | PR |
| Q9ESK3 | Capn10 | Calpain-10 | Mus musculus (Mouse) | PR |
| G3UZ78 | Adgb | Androglobin | Mus musculus (Mouse) | PR |
| O08529 | Capn2 | Calpain-2 catalytic subunit | Mus musculus (Mouse) | PR |
| Q9D805 | Capn9 | Calpain-9 | Mus musculus (Mouse) | PR |
| Q3UW68 | Capn13 | Calpain-13 | Mus musculus (Mouse) | PR |
| O35350 | Capn1 | Calpain-1 catalytic subunit | Mus musculus (Mouse) | PR |
| P43367 | CAPN2 | Calpain-2 catalytic subunit | Sus scrofa (Pig) | PR |
| P35750 | CAPN1 | Calpain-1 catalytic subunit | Sus scrofa (Pig) | PR |
| Q07009 | Capn2 | Calpain-2 catalytic subunit | Rattus norvegicus (Rat) | PR |
| O35920 | Capn9 | Calpain-9 | Rattus norvegicus (Rat) | PR |
| Q5BK10 | Capn13 | Calpain-13 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEELITPVY | CTGVSAQVQK | QRDKELGLGR | HENAIKYLGQ | DYENLRARCL | QNGVLFQDDA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FPPVSHSLGF | KELGPNSSKT | YGIKWKRPTE | LLSNPQFIVD | GATRTDICQG | ALGDCWLLAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IASLTLNETI | LHRVVPYGQS | FQEGYAGIFH | FQLWQFGEWV | DVVVDDLLPT | KDGKLVFVHS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AQGNEFWSAL | LEKAYAKVNG | SYEALSGGCT | SEAFEDFTGG | VTEWYDLQKA | PSDLYQIILK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALERGSLLGC | SINISDIRDL | EAITFKNLVR | GHAYSVTDAK | QVTYQGQRVN | LIRMRNPWGE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VEWKGPWSDN | SYEWNKVDPY | EREQLRVKME | DGEFWMSFRD | FIREFTKLEI | CNLTPDALKS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RTLRNWNTTF | YEGTWRRGST | AGGCRNYPAT | FWVNPQFKIR | LEEVDDADDY | DSRESGCSFL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LALMQKHRRR | ERRFGRDMET | IGFAVYQVPR | ELAGQPVHLK | RDFFLANASR | AQSEHFINLR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EVSNRIRLPP | GEYIVVPSTF | EPNKEGDFLL | RFFSEKKAGT | QELDDQIQAN | LPDEKVLSEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EIDDNFKTLF | SKLAGDDMEI | SVKELQTILN | RIISKHKDLR | TNGFSLESCR | SMVNLMDRDG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NGKLGLVEFN | ILWNRIRNYL | TIFRKFDLDK | SGSMSAYEMR | MAIEAAGFKL | NKKLHELIIT |
| 670 | 680 | 690 | 700 | 710 | |
| RYSEPDLAVD | FDNFVCCLVR | LETMFRFFKI | LDTDLDGVVT | FDLFKWLQLT | MFA |