Q8CB12 · GSDC3_MOUSE
- ProteinGasdermin-C3
- GeneGsdmc3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids480 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Gasdermin-C3
This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C3, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Gasdermin-C3, N-terminal
Pore-forming protein that causes membrane permeabilization and pyroptosis. Produced by the cleavage of gasdermin-C3 by caspase CASP8 in response to death signals (By similarity).
After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (By similarity).
After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (By similarity).
Activity regulation
Gasdermin-C3
The full-length protein before cleavage is inactive: intramolecular interactions between N- and C-terminal domains mediate autoinhibition in the absence of activation signal (By similarity).
The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-C3, N-terminal) following cleavage by caspase CASP8 (By similarity).
The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-C3, N-terminal) following cleavage by caspase CASP8 (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Molecular Function | phosphatidylinositol-4-phosphate binding | |
Molecular Function | phosphatidylserine binding | |
Biological Process | defense response to bacterium | |
Biological Process | programmed cell death | |
Biological Process | pyroptotic inflammatory response |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameGasdermin-C3
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CB12
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Gasdermin-C3
Gasdermin-C3, N-terminal
Cell membrane ; Multi-pass membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451681 | ?-480 | Gasdermin-C3, C-terminal | |||
Sequence: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDKLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLLVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIEPIGRIQEPAHLDFKCLQYEVSEQTRLLPELSKDVQEVVLSSFLSMLYEGDRNVLHDLMKMLELSQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLARSVEMRLLPHQVELVTSILQPNFKYPWNIPFTVQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLQKANSSFKPSLRPGYI | ||||||
Chain | PRO_0000451680 | 1-? | Gasdermin-C3, N-terminal | |||
Chain | PRO_0000347332 | 1-480 | Gasdermin-C3 | |||
Sequence: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDKLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLLVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIEPIGRIQEPAHLDFKCLQYEVSEQTRLLPELSKDVQEVVLSSFLSMLYEGDRNVLHDLMKMLELSQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLARSVEMRLLPHQVELVTSILQPNFKYPWNIPFTVQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLQKANSSFKPSLRPGYI |
Post-translational modification
Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C3, N-terminal) that initiates pyroptosis.
Palmitoylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Gasdermin-C3, N-terminal
Homooligomer; homooligomeric ring-shaped pore complex containing 27-28 subunits when inserted in the membrane.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-226 | Triggers pyroptosis | ||||
Sequence: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDKLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLLVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATK |
Domain
Intramolecular interactions between N- and C-terminal domains are important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain.
Sequence similarities
Belongs to the gasdermin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length480
- Mass (Da)54,188
- Last updated2011-07-27 v2
- ChecksumBEA95A9F8FFEEA6A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 383 | in Ref. 1; BAC29694 | ||||
Sequence: P → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK037079 EMBL· GenBank· DDBJ | BAC29694.1 EMBL· GenBank· DDBJ | mRNA | ||
AC140673 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |