Q5RAV7
Gene name |
CARD8 |
Protein name |
Caspase recruitment domain-containing protein 8 |
Names |
|
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100172562 |
EC number |
|
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 Q5RAV7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RAV7-F1 | Predicted | AlphaFoldDB |
2 variants for Q5RAV7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs174321575 | 49 | R>S | No | Ensembl | |
| rs174321526 | 297 | A>V | No | Ensembl |
No associated diseases with Q5RAV7
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| NLRP3 inflammasome complex | An inflammasome complex that consists of three components, NLRP3 (NALP3), PYCARD and caspase-1. It is activated upon exposure to whole pathogens, as well as a number of structurally diverse pathogen- and danger-associated molecular patterns (PAMPs and DAMPs) and environmental irritants. Whole pathogens demonstrated to activate the NLRP3 inflammasome complex include the fungi Candida albicans and Saccharomyces cerevisiae, bacteria that produce pore-forming toxins, including Listeria monocytogenes and Staphylococcus aureus, and viruses such as Sendai virus, adenovirus, and influenza virus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| inflammatory response | The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. |
| innate immune response | Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| regulation of apoptotic process | Any process that modulates the occurrence or rate of cell death by apoptotic process. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGIPTSSVSE | EQESSEGQDS | GDICSEENQI | VSSYASKVCF | EIEQDYKNRQ | FLGPEGNVDV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELIDKSTNTY | SVRFPTAGWY | LWPATGLGFL | VRDVVTLTIG | FGSWNQHLAL | DLQHHEQWLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GGPLFDITAE | PEEAVAEIHL | PHFISLQAGE | VDVSWFLIAH | FKNEGMVLEH | PARVEPFYAV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LEKPSFSLMG | ILLRIASGTR | LSIPITSNTL | IYYHPHPEDI | KFHLYLVPSD | ALLTKMIDDE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EDRFCGVRLQ | TSPPVEPLNF | GARYIVSNSA | HLEIIPTELK | LSYRSPGEIQ | HFSKFYAGQM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEPIQLEITE | KRHETLVWKT | VVKPVDIQLG | AASAPPAFSG | AAFVKENHRQ | LQARMGDLKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLDDLQDNEV | LTENEKELVE | QAKTRQSKND | TLLTMVEKKG | DRALELLFRS | ISERDPYLVS |
| YLRQQSL |