Q2KHK6 · GSDC2_MOUSE
- ProteinGasdermin-C2
- GeneGsdmc2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids480 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Gasdermin-C2
This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C2, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Gasdermin-C2, N-terminal
Pore-forming protein that causes membrane permeabilization and pyroptosis in response to type-2 immunity (PubMed:34290141).
Produced by the cleavage of gasdermin-C2 in response to type-2 immunity following worm infection (PubMed:34290141).
After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids (By similarity).
Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis and lytic cell death in enterocytes (PubMed:34290141).
Produced by the cleavage of gasdermin-C2 in response to type-2 immunity following worm infection (PubMed:34290141).
After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids (By similarity).
Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis and lytic cell death in enterocytes (PubMed:34290141).
Activity regulation
Gasdermin-C2
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-C2, N-terminal) following cleavage by caspase CASP8 in response to type-2 immunity following worm infection (PubMed:34290141).
The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-C2, N-terminal) following cleavage by caspase CASP8 in response to type-2 immunity following worm infection (PubMed:34290141).
GO annotations
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 | intestinal epithelial cell development | |
Biological Process | programmed cell death | |
Biological Process | pyroptotic inflammatory response |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameGasdermin-C2
- 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 accessionQ2KHK6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Gasdermin-C2
Gasdermin-C2, 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_0000451679 | ?-480 | Gasdermin-C2, C-terminal | |||
Sequence: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIVPIGRIQEPAHLDFMCLQNEVYKQTEQLAELSKGVQEVVLSSILSMLYEGDRKVLYDLMNMLELNQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLAQSVEMGILPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLRKANSSSKPSLRPGYI | ||||||
Chain | PRO_0000451678 | 1-? | Gasdermin-C2, N-terminal | |||
Chain | PRO_0000347331 | 1-480 | Gasdermin-C2 | |||
Sequence: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIVPIGRIQEPAHLDFMCLQNEVYKQTEQLAELSKGVQEVVLSSILSMLYEGDRKVLYDLMNMLELNQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLAQSVEMGILPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLRKANSSSKPSLRPGYI |
Post-translational modification
Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C2, N-terminal) that initiates pyroptosis (PubMed:34290141).
Palmitoylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By type 2 cytokines in response to type-2 immunity following worm infection.
Gene expression databases
Interaction
Subunit
Gasdermin-C2, 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: MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATK |
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)53,952
- Last updated2008-09-02 v2
- ChecksumC1F78ECDB8D4AAD1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 134 | in Ref. 2; AAI13154 | ||||
Sequence: N → K | ||||||
Sequence conflict | 180 | in Ref. 1; BAC28384 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 363 | in Ref. 2; AAI13154 | ||||
Sequence: M → L | ||||||
Sequence conflict | 368 | in Ref. 2; AAI13154 | ||||
Sequence: S → T | ||||||
Sequence conflict | 371 | in Ref. 2; AAI13154 | ||||
Sequence: N → C | ||||||
Sequence conflict | 378 | in Ref. 2; AAI13154 | ||||
Sequence: E → K | ||||||
Sequence conflict | 381 | in Ref. 2; AAI13154 | ||||
Sequence: I → L | ||||||
Sequence conflict | 395 | in Ref. 2; AAI13154 | ||||
Sequence: P → T | ||||||
Sequence conflict | 400-403 | in Ref. 2; AAI13154 | ||||
Sequence: PWNI → SSNT | ||||||
Sequence conflict | 407 | in Ref. 2; AAI13156 | ||||
Sequence: L → V | ||||||
Sequence conflict | 465 | in Ref. 2; AAI13154 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 476 | in Ref. 2; AAI13154 | ||||
Sequence: R → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK033603 EMBL· GenBank· DDBJ | BAC28384.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113153 EMBL· GenBank· DDBJ | AAI13154.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113155 EMBL· GenBank· DDBJ | AAI13156.1 EMBL· GenBank· DDBJ | mRNA |