Gsdme
entrez
54722
canonical
uniprot
Q9Z2D3
canonical
ensembl
ENSMUSG00000029821
resolver
ensp
ENSMUSP00000031845
resolver
ensp
ENSMUSP00000126759
resolver
ensp
ENSMUSP00000130522
resolver
ensp
ENSMUSP00000308488
resolver
enst
ENSMUST00000031845
resolver
enst
ENSMUST00000165099
resolver
enst
ENSMUST00000170142
resolver
genesymbol
Gsdme
resolver
genesymbol_syn
Dfna5
resolver
genesymbol_syn
Dfna5h
resolver
uniprot
E9Q5V3
resolver
uniprot_entry
E9Q5V3_MOUSE
resolver
uniprot_entry
GSDME_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: [Gasdermin-E]: 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-E, N-terminal) following cleavage by CASP3 or granzyme B (GZMB) (By similarity). Activated by NLRP1 in the absence of GSDMD expression: NLRP1 cleaves and activates CASP8, promoting downstream activation of CASP3 and subsequent activation of GSDME (PubMed:33852854). {ECO:0000250|UniProtKB:O60443, ECO:0000269|PubMed:33852854}.
uniprot
proteins
amino_acid_sequence
MFAKATRNFLKEVDAGGDLISVSHLNDSDKLQLLSLVTKKKRYWCWQRPKYQILSATLEDVLTEGHCLSPVVVESDFVKYESKCENHKSGAIGTVVGKVKLNVGGKGVVESHSSFGTLRKQEVDVQQLIQDAVKRTVNMDNLVLQQVLESRNEVLCVLTQKIMTTQKCVISEHVQSEETCGGMVGIQTKTIQVSATEDGTVTTDTNVVLEIPAATTIAYGIMELFVKQDGQFEFCLLQGKHGGFEHERKLDSVYLDPLAYREFAFLDMLDGGQGISSQDGPLRVVKQATLHLERSFHPFAVLPAQQQRALFCVLQKILFDEELLRALEQVCDDVAGGLWSSQAVLAMEELTDSQQQDLTAFLQLVGYRIQGEHPGPQDEVSNQKLFATAYFLVSALAEMPDNATVFLGTCCKLHVISSLCCLLHALSDDSVCDFHNPTLAPLRDTERFGIVQRLFASADIALERMQFSAKATILKDSCIFPLILHITLSGLSTLSKEHEEELCQSGHATGQD
uniprot
proteins
function
FUNCTION: [Gasdermin-E]: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis. {ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:33852854}.; FUNCTION: [Gasdermin-E, N-terminal]: Pore-forming protein produced by cleavage by CASP3 or granzyme B (GZMB), which converts non-inflammatory apoptosis to pyroptosis or promotes granzyme-mediated pyroptosis, respectively (PubMed:32188940). After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukins (IL1B and IL16) and triggering pyroptosis (PubMed:33852854). Binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate (By similarity). Cleavage by CASP3 switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis (PubMed:32188940). Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents (PubMed:28045099). Exhibits bactericidal activity (By similarity). Cleavage by GZMB promotes tumor suppressor activity by triggering robust anti-tumor immunity (PubMed:32188940). Suppresses tumors by mediating granzyme-mediated pyroptosis in target cells of natural killer (NK) cells: cleavage by granzyme B (GZMB), delivered to target cells from NK-cells, triggers pyroptosis of tumor cells and tumor suppression (By similarity). May play a role in the p53/TP53-regulated cellular response to DNA damage (By similarity). {ECO:0000250|UniProtKB:O60443, ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:33852854}.
uniprot
proteins
mass_dalton
56631
uniprot
proteins
post_translational_modification
PTM: Cleavage at Asp-270 by CASP3 (mature and uncleaved precursor forms) or granzyme B (GZMB) relieves autoinhibition and is sufficient to initiate pyroptosis. {ECO:0000250|UniProtKB:O60443}.; PTM: [Gasdermin-E]: Succination by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits processing by caspases, and ability to initiate pyroptosis. Succination modification is catalyzed by a non-enzymatic reaction caused by an accumulation of fumarate. {ECO:0000250|UniProtKB:O60443}.; PTM: [Gasdermin-E]: Ubiquitinated on Lys-120 and Lys-189 via 'Lys-48'-linked polyubiquitin chains, leading to proteasomal degradation. Deubiquitinated by USP48, leading to increased stability. {ECO:0000250|UniProtKB:O60443}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:O60443}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
28045099
uniprot
proteins
pubmed
28459430
uniprot
proteins
pubmed
32188940
uniprot
proteins
pubmed
33852854
uniprot
proteins
pubmed
9771715
uniprot
proteins
sequence_length
512
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-E, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:O60443}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-E]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60443}.
uniprot
proteins