Gsdma
entrez
57911
canonical
uniprot
Q9EST1
canonical
ensembl
ENSMUSG00000017204
resolver
ensp
ENSMUSP00000017348
resolver
enst
ENSMUST00000017348
resolver
genesymbol
Gsdma
resolver
genesymbol_syn
Gsdm
resolver
genesymbol_syn
Gsdm1
resolver
genesymbol_syn
Gsdma1
resolver
uniprot
A3KFN3
resolver
uniprot_entry
GSDMA_MOUSE
resolver
uniprot_sec
A3KFN3
resolver
activity_regulation
ACTIVITY REGULATION: [Gasdermin-A]: 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-A, N-terminal) following cleavage by bacterial effector protein SpeB (PubMed:35110732). {ECO:0000250|UniProtKB:Q5Y4Y6, ECO:0000269|PubMed:35110732}.
uniprot
proteins
amino_acid_sequence
MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVHTDYTLLDVLEPGSSPSDPTDSGNFSFKNMLDARVEGDVDVPKTVKVKGTAGLSRSSTLEVQTLSVAPTALENLHKERKLSADHPFLKEMRERGENLYVVMEVVETLQEVTLERAGKAEGCFSLPFFAPLGLQGSVNHKEAVTIPKGCVLAYRVRQLMVNGKDEWGIPHICNDSMQTFPPGEKPGEGKFILIQASDVGEMHEDFKTLKEEVQRETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQTLEGALDKGHEVTLEALPKDVLLSKDAMDAILYFLGALTVLSEAQQKLLVKSLEKKILPVQLKLVESTMEKNFLQDKEGVFPLQPDLLSSLGEEELILTEALVGLSGLEVQRSGPQYTWDPDTLPHLCALYAGLSLLQLLSKNS
uniprot
proteins
function
FUNCTION: [Gasdermin-A]: This form constitutes the precursor of the pore-forming protein and acts as a sensor of bacterial infection: upon infection, specifically cleaved by bacterial effector protein SpeB in epithelial cells, releasing the N-terminal moiety (Gasdermin-A, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. {ECO:0000269|PubMed:35110732}.; FUNCTION: [Gasdermin-A, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis (PubMed:35110732). Released upon cleavage by bacterial effector protein SpeB, and binds to membrane inner leaflet lipids (PubMed:35110732). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (By similarity). Pyroptosis triggers the elimination of the infected skin cell, depriving the pathogen of its protective niche, while inducing an inflammatory response (PubMed:35110732, PubMed:35545676). This ultimately prevents bacterial penetration of the epithelial barrier and a subsequent systemic dissemination of the pathogen (PubMed:35110732, PubMed:35545676). Binds to cardiolipin and other acidic phospholipids, such as phosphatidylserine, which mediate its targeting to the inner leaflet membrane (By similarity). {ECO:0000250|UniProtKB:Q96QA5, ECO:0000269|PubMed:35110732, ECO:0000269|PubMed:35545676}.
uniprot
proteins
mass_dalton
49593
uniprot
proteins
mutagenesis
MUTAGEN 247..248; /note="QA->NE: Abolished cleavage by bacterial effector protein SpeB, preventing pyroptosis."; /evidence="ECO:0000269|PubMed:35110732
uniprot
proteins
post_translational_modification
PTM: Cleavage by bacterial SpeB relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-A, N-terminal) that initiates pyroptosis. {ECO:0000269|PubMed:35110732}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q96QA5}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
10967128
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17350798
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
35110732
uniprot
proteins
pubmed
35545676
uniprot
proteins
sequence_length
446
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-A]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-A, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
uniprot
proteins
transmembrane_region
TRANSMEM 78..95; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6"; TRANSMEM 99..120; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6"; TRANSMEM 164..180; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6"; TRANSMEM 184..198; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6
uniprot
proteins