Gsdma2
entrez
76758
canonical
uniprot
Q32M21
canonical
ensembl
ENSMUSG00000017211
resolver
ensp
ENSMUSP00000017355
resolver
ensp
ENSMUSP00000091470
resolver
genesymbol
Gsdma2
resolver
genesymbol_syn
Gsdm2
resolver
uniprot
Q8CF01
resolver
uniprot
Q9D810
resolver
uniprot_entry
GSDA2_MOUSE
resolver
uniprot_sec
Q8CF01
resolver
uniprot_sec
Q9D810
resolver
activity_regulation
ACTIVITY REGULATION: [Gasdermin-A2]: The full-length protein before cleavage is inactive: intramolecular interactions between N- and C-terminal domains mediate autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-A2, N-terminal). {ECO:0000250|UniProtKB:Q5Y4Y6}.
uniprot
proteins
amino_acid_sequence
MSMFEDVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTLLGNFSFKNMLDVRVEGDVEVPTMMKVKGTVGLSQSSTLEVQMLSVAPTALENLHMERKLSADHPFLKEMREYKQNLYVVMEVVKAKQEVTLKRASNAISKFSLNLPSLGLQGSVNHKEAVTIPKGCVLAYRVRQLIIYGKDEWGIPYICTDNMPTFNPLCVLQRQGSTVQMISGEMHEDFKTLKKEVQQETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQMLEGALDKGHEVTLEALPKDVLLLKDAMDAILYFLGALTELSEEQLKILVKSLENKVLPVQLKLVESILEQNFLQDKEDVFPLRPDLLSSLGEEDQILTEALVGLSGLEVQRSGPQYTWNPDTCHNLCALYAGLSLLHLLSRDS
uniprot
proteins
function
FUNCTION: [Gasdermin-A2]: This form constitutes the precursor of the pore-forming protein and acts as a sensor of infection: upon bacterial infection, specifically cleaved by some bacterial effector protein, releasing the N-terminal moiety (Gasdermin-A2, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. {ECO:0000250|UniProtKB:Q9EST1}.; FUNCTION: [Gasdermin-A2, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage of Gasdermin-A2, and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, such as phosphatidylinositol (4,5)-bisphosphate. {ECO:0000250|UniProtKB:Q96QA5}.
uniprot
proteins
mass_dalton
49844
uniprot
proteins
post_translational_modification
PTM: Cleavage relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-A2, N-terminal) that initiates pyroptosis (By similarity). In contrast to Gsdma, not cleaved by bacterial effector protein SpeB (PubMed:35110732). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:35110732}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q96QA5}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17350798
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
35110732
uniprot
proteins
pubmed
35545676
uniprot
proteins
sequence_length
443
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-A2]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-A2, 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..179; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6"; TRANSMEM 183..197; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q5Y4Y6
uniprot
proteins