Q2KHK6 · GSDC2_MOUSE

  • Protein
    Gasdermin-C2
  • Gene
    Gsdmc2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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).

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).

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentplasma membrane
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Molecular Functionphosphatidylinositol-4-phosphate binding
Molecular Functionphosphatidylserine binding
Biological Processdefense response to bacterium
Biological Processintestinal epithelial cell development
Biological Processprogrammed cell death
Biological Processpyroptotic inflammatory response

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      Gsdmc2

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q2KHK6
  • Secondary accessions
    • Q2KHK8
    • Q8CC94

Proteomes

Organism-specific databases

Subcellular Location

Gasdermin-C2

Cytoplasm, cytosol

Gasdermin-C2, N-terminal

Cell membrane
; Multi-pass membrane protein

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_0000451679?-480Gasdermin-C2, C-terminal
ChainPRO_00004516781-?Gasdermin-C2, N-terminal
ChainPRO_00003473311-480Gasdermin-C2

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

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.

TypeIDPosition(s)Description
Region1-226Triggers pyroptosis

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    480
  • Mass (Da)
    53,952
  • Last updated
    2008-09-02 v2
  • Checksum
    C1F78ECDB8D4AAD1
MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIVPIGRIQEPAHLDFMCLQNEVYKQTEQLAELSKGVQEVVLSSILSMLYEGDRKVLYDLMNMLELNQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLAQSVEMGILPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLRKANSSSKPSLRPGYI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict134in Ref. 2; AAI13154
Sequence conflict180in Ref. 1; BAC28384
Sequence conflict363in Ref. 2; AAI13154
Sequence conflict368in Ref. 2; AAI13154
Sequence conflict371in Ref. 2; AAI13154
Sequence conflict378in Ref. 2; AAI13154
Sequence conflict381in Ref. 2; AAI13154
Sequence conflict395in Ref. 2; AAI13154
Sequence conflict400-403in Ref. 2; AAI13154
Sequence conflict407in Ref. 2; AAI13156
Sequence conflict465in Ref. 2; AAI13154
Sequence conflict476in Ref. 2; AAI13154

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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