Gsdmc2
entrez
331063
canonical
uniprot
Q2KHK6
canonical
ensembl
ENSMUSG00000056293
resolver
ensp
ENSMUSP00000087344
resolver
ensp
ENSMUSP00000140487
resolver
ensp
ENSMUSP00000141066
resolver
enst
ENSMUST00000089900
resolver
enst
ENSMUST00000188404
resolver
enst
ENSMUST00000188691
resolver
genesymbol
Gsdmc2
resolver
uniprot
Q2KHK8
resolver
uniprot
Q8CC94
resolver
uniprot_entry
GSDC2_MOUSE
resolver
uniprot_sec
Q2KHK8
resolver
uniprot_sec
Q8CC94
resolver
activity_regulation
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). {ECO:0000250|UniProtKB:Q9BYG8, ECO:0000269|PubMed:34290141}.
uniprot
proteins
amino_acid_sequence
MGYSFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLEPNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKLEILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFKVRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEPTEIYRTELQGLWINDIVPIGRIQEPAHLDFMCLQNEVYKQTEQLAELSKGVQEVVLSSILSMLYEGDRKVLYDLMNMLELNQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALMVLSDSQLNLLAQSVEMGILPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLRKANSSSKPSLRPGYI
uniprot
proteins
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. {ECO:0000269|PubMed:34290141}.; FUNCTION: [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). {ECO:0000250|UniProtKB:Q9BYG8, ECO:0000269|PubMed:34290141}.
uniprot
proteins
mass_dalton
53952
uniprot
proteins
post_translational_modification
PTM: Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C2, N-terminal) that initiates pyroptosis (PubMed:34290141). {ECO:0000305|PubMed:34290141}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9BYG8}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17350798
uniprot
proteins
pubmed
34290141
uniprot
proteins
sequence_length
480
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-C2]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYG8}.; SUBCELLULAR LOCATION: [Gasdermin-C2, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
uniprot
proteins