ID GSDMD_MOUSE Reviewed; 487 AA. AC Q9D8T2; Q3TBD9; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 11-DEC-2019, entry version 118. DE RecName: Full=Gasdermin-D; DE AltName: Full=Gasdermin domain-containing protein 1; DE Contains: DE RecName: Full=Gasdermin-D, N-terminal; DE Short=GSDMD-NT {ECO:0000303|PubMed:27383986}; DE Contains: DE RecName: Full=Gasdermin-D, C-terminal; DE Short=GSDMD-CT {ECO:0000303|PubMed:27383986}; GN Name=Gsdmdc1; Synonyms=Gsdmd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Pancreas; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 11-44; 84-125; 139-152 AND 204-218, FUNCTION, RP ASSOCIATION WITH NLRP3 INFLAMMASOME, SUBCELLULAR LOCATION, MASS RP SPECTROMETRY, MUTAGENESIS OF ASP-276, AND CLEAVAGE BY CASP1. RX PubMed=26611636; DOI=10.1038/cr.2015.139; RA He W.T., Wan H., Hu L., Chen P., Wang X., Huang Z., Yang Z.H., Zhong C.Q., RA Han J.; RT "Gasdermin D is an executor of pyroptosis and required for interleukin- RT 1beta secretion."; RL Cell Res. 25:1285-1298(2015). RN [4] RP PROTEIN SEQUENCE OF 277-288, FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF RP ILE-105 AND ASP-276, AND CLEAVAGE BY CASP1 AND CASP4. RX PubMed=26375259; DOI=10.1038/nature15541; RA Kayagaki N., Stowe I.B., Lee B.L., O'Rourke K., Anderson K., Warming S., RA Cuellar T., Haley B., Roose-Girma M., Phung Q.T., Liu P.S., Lill J.R., RA Li H., Wu J., Kummerfeld S., Zhang J., Lee W.P., Snipas S.J., RA Salvesen G.S., Morris L.X., Fitzgerald L., Zhang Y., Bertram E.M., RA Goodnow C.C., Dixit V.M.; RT "Caspase-11 cleaves gasdermin D for non-canonical inflammasome RT signalling."; RL Nature 526:666-671(2015). RN [5] RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=18693275; DOI=10.1002/dvg.20412; RA Fujii T., Tamura M., Tanaka S., Kato Y., Yamamoto H., Mizushina Y., RA Shiroishi T.; RT "Gasdermin D (Gsdmd) is dispensable for mouse intestinal epithelium RT development."; RL Genesis 46:418-423(2008). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, AND AUTOINHIBITION. RX PubMed=26375003; DOI=10.1038/nature15514; RA Shi J., Zhao Y., Wang K., Shi X., Wang Y., Huang H., Zhuang Y., Cai T., RA Wang F., Shao F.; RT "Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell RT death."; RL Nature 526:660-665(2015). RN [8] RP FUNCTION (GASDERMIN-D, N-TERMINAL), SUBCELLULAR LOCATION, AND ACTIVATION RP WITH NLRC4 INFLAMMASOME. RX PubMed=27418190; DOI=10.15252/embj.201694696; RA Sborgi L., Ruehl S., Mulvihill E., Pipercevic J., Heilig R., Stahlberg H., RA Farady C.J., Mueller D.J., Broz P., Hiller S.; RT "GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell RT death."; RL EMBO J. 35:1766-1778(2016). RN [9] RP FUNCTION. RX PubMed=27385778; DOI=10.4049/jimmunol.1600699; RA Russo H.M., Rathkey J., Boyd-Tressler A., Katsnelson M.A., Abbott D.W., RA Dubyak G.R.; RT "Active caspase-1 induces plasma membrane pores that precede pyroptotic RT lysis and are blocked by lanthanides."; RL J. Immunol. 197:1353-1367(2016). RN [10] RP FUNCTION (GASDERMIN-D, N-TERMINAL), CLEAVAGE BY CASP4, LIPID-BINDING, RP HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-39; RP CYS-57; CYS-77; CYS-122; ARG-138; LYS-146; ARG-152; ARG-154; CYS-192; RP LYS-237; ARG-239; ARG-248; LYS-249 AND CYS-265. RX PubMed=27383986; DOI=10.1038/nature18629; RA Liu X., Zhang Z., Ruan J., Pan Y., Magupalli V.G., Wu H., Lieberman J.; RT "Inflammasome-activated gasdermin D causes pyroptosis by forming membrane RT pores."; RL Nature 535:153-158(2016). CC -!- FUNCTION: [Gasdermin-D, N-terminal]: Promotes pyroptosis in response to CC microbial infection and danger signals. Produced by the cleavage of CC gasdermin-D by inflammatory caspases CASP1 or CASP4 in response to CC canonical, as well as non-canonical (such as cytosolic LPS) CC inflammasome activators (PubMed:26611636, PubMed:26375259, CC PubMed:26375003, PubMed:27418190, PubMed:27385778, PubMed:27383986). CC After cleavage, moves to the plasma membrane where it strongly binds to CC membrane inner leaflet lipids, including monophosphorylated CC phosphatidylinositols, such as phosphatidylinositol 4-phosphate, CC bisphosphorylated phosphatidylinositols, such as phosphatidylinositol CC (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)- CC trisphosphate, and more weakly to phosphatidic acid and CC phosphatidylserine. Homooligomerizes within the membrane and forms CC pores of 10 - 15 nanometers (nm) of inner diameter, allowing the CC release of mature IL1B and triggering pyroptosis. Exhibits bactericidal CC activity. Gasdermin-D, N-terminal released from pyroptotic cells into CC the extracellular milieu rapidly binds to and kills both Gram-negative CC and Gram-positive bacteria, without harming neighboring mammalian CC cells, as it does not disrupt the plasma membrane from the outside due CC to lipid-binding specificity. Under cell culture conditions, also CC active against intracellular bacteria, such as Listeria monocytogenes. CC Strongly binds to bacterial and mitochondrial lipids, including CC cardiolipin. Does not bind to phosphatidylethanolamine or CC phosphatidylcholine (PubMed:27383986). {ECO:0000269|PubMed:26375003, CC ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, CC ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27385778, CC ECO:0000269|PubMed:27418190}. CC -!- SUBUNIT: In response to a canonical inflammasome stimulus, such as CC nigericin, recruited to NLRP3 inflammasone with similar kinetics to CC that of uncleaved CASP1 precursor. Although this recruitment is also CC observed in the absence of PYCARD, it is more efficient in its presence CC (PubMed:26611636). Gasdermin-D, N-terminal forms disulfide-linked CC homooligomers (16-mers) in a Ca(+2)-independent manner. Oligomerization CC occurs in the presence of membranes; remains monomeric in the cytosol CC (PubMed:27383986). {ECO:0000269|PubMed:26611636, CC ECO:0000269|PubMed:27383986}. CC -!- SUBCELLULAR LOCATION: [Gasdermin-D]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. CC Inflammasome {ECO:0000269|PubMed:26611636}. Note=In response to a CC canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 CC inflammasone with similar kinetics to that of uncleaved CASP1 CC precursor. {ECO:0000269|PubMed:26611636}. CC -!- SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cell membrane CC {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. Secreted CC {ECO:0000269|PubMed:27383986}. Note=Released in the extracellular CC milieu following pyroptosis. {ECO:0000269|PubMed:27383986}. CC -!- DEVELOPMENTAL STAGE: Expression starts at 8.5 dpc and increases from CC 13.5 dpc on. Still detected after birth. {ECO:0000269|PubMed:18693275}. CC -!- DOMAIN: Intramolecular interactions between N- and C-terminal domains CC may be important for autoinhibition in the absence of cleavage by CC inflammatory caspases CASP1 or CASP4. The intrinsic pyroptosis-inducing CC activity is carried by gasdermin-D, N-terminal, that is released upon CC cleavage by inflammatory caspases. {ECO:0000269|PubMed:26375003, CC ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636}. CC -!- PTM: Cleavage at Asp-276 by CASP1 (mature and uncleaved precursor CC forms) or CASP4 relieves autoinhibition and is sufficient to initiate CC pyroptosis (PubMed:26375259, PubMed:26611636). Cleavage at Asp-88 by CC CASP3 (By similarity). {ECO:0000250|UniProtKB:P57764, CC ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636}. CC -!- DISRUPTION PHENOTYPE: Knockout mice are born at the expected Mendelian CC rate and do not exhibit any overt phenotype in normal housing CC conditions. The gastrointestinal tract develops normally. They are CC however resistant to LPS-induced lethal septic shock. Primary bone CC marrow-derived macrophages fail to undergo pyroptosis in response to CC canonical (acting via CASP1), as well as to non-canonical (acting via CC CASP4) inflammasome activators. CASP1-mediated IL1B release is also CC impaired, but not CASP1 autoprocessing, nor IL1B maturation. CC {ECO:0000269|PubMed:18693275, ECO:0000269|PubMed:26375003, CC ECO:0000269|PubMed:26375259}. CC -!- SIMILARITY: Belongs to the gasdermin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK007710; BAB25204.1; -; mRNA. DR EMBL; AK165858; BAE38418.1; -; mRNA. DR EMBL; AK171294; BAE42374.1; -; mRNA. DR EMBL; BC029813; AAH29813.1; -; mRNA. DR CCDS; CCDS27551.1; -. DR RefSeq; NP_081236.1; NM_026960.4. DR PDB; 6AO3; X-ray; 1.76 A; A/B/C/D=277-487. DR PDB; 6N9N; X-ray; 3.30 A; A/B=1-487. DR PDBsum; 6AO3; -. DR PDBsum; 6N9N; -. DR SMR; Q9D8T2; -. DR DIP; DIP-61777N; -. DR IntAct; Q9D8T2; 1. DR STRING; 10090.ENSMUSP00000023238; -. DR iPTMnet; Q9D8T2; -. DR PhosphoSitePlus; Q9D8T2; -. DR SwissPalm; Q9D8T2; -. DR EPD; Q9D8T2; -. DR MaxQB; Q9D8T2; -. DR PaxDb; Q9D8T2; -. DR PeptideAtlas; Q9D8T2; -. DR PRIDE; Q9D8T2; -. DR Ensembl; ENSMUST00000023238; ENSMUSP00000023238; ENSMUSG00000022575. DR GeneID; 69146; -. DR KEGG; mmu:69146; -. DR UCSC; uc007whh.1; mouse. DR CTD; 79792; -. DR MGI; MGI:1916396; Gsdmd. DR eggNOG; ENOG410IKA4; Eukaryota. DR eggNOG; ENOG4111D9N; LUCA. DR GeneTree; ENSGT00950000183140; -. DR HOGENOM; HOG000082450; -. DR InParanoid; Q9D8T2; -. DR KO; K20917; -. DR OMA; TSFQPYC; -. DR OrthoDB; 747086at2759; -. DR PhylomeDB; Q9D8T2; -. DR TreeFam; TF331886; -. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR PRO; PR:Q9D8T2; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q9D8T2; protein. DR Bgee; ENSMUSG00000022575; Expressed in 144 organ(s), highest expression level in intestine. DR ExpressionAtlas; Q9D8T2; baseline and differential. DR Genevisible; Q9D8T2; MM. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB. DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI. DR GO; GO:0019835; P:cytolysis; IDA:UniProtKB. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0046931; P:pore complex assembly; IDA:UniProtKB. DR GO; GO:0035915; P:pore formation in membrane of other organism; IDA:UniProtKB. DR GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0070269; P:pyroptosis; IDA:UniProtKB. DR InterPro; IPR007677; Gasdermin. DR InterPro; IPR040460; Gasdermin_pore. DR InterPro; IPR041263; Gasdermin_PUB. DR PANTHER; PTHR16399; PTHR16399; 1. DR Pfam; PF04598; Gasdermin; 1. DR Pfam; PF17708; Gasdermin_C; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Immunity; Inflammasome; Inflammatory response; KW Innate immunity; Membrane; Necrosis; Phosphoprotein; Reference proteome; KW Secreted. FT CHAIN 1..487 FT /note="Gasdermin-D" FT /id="PRO_0000148176" FT CHAIN 1..276 FT /note="Gasdermin-D, N-terminal" FT /evidence="ECO:0000305|PubMed:27383986" FT /id="PRO_0000437528" FT CHAIN 277..487 FT /note="Gasdermin-D, C-terminal" FT /evidence="ECO:0000305|PubMed:27383986" FT /id="PRO_0000437529" FT SITE 88..89 FT /note="Cleavage; by CASP3" FT /evidence="ECO:0000250|UniProtKB:P57764" FT SITE 276..277 FT /note="Cleavage; by inflammatory caspases CASP1 and CASP4" FT /evidence="ECO:0000269|PubMed:26375259" FT MOD_RES 38 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P57764" FT MUTAGEN 39 FT /note="C->A: Loss of oligomerization of Gasdermin-D, N- FT terminal." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 57 FT /note="C->A: No effect on oligomerization." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 77 FT /note="C->A: No effect on oligomerization." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 105 FT /note="I->N: Loss of cytosolic LPS-induced IL1B release and FT pyroptosis in bone marrow-derived macrophages. No effect on FT protein expression. No effect on cleavage by CASP4." FT /evidence="ECO:0000269|PubMed:26375259" FT MUTAGEN 122 FT /note="C->A: No effect on oligomerization." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 138 FT /note="R->A,S: Complete loss of homooligomerization, lipid- FT binding, relocalization of Gasdermin-D, N-terminal to the FT plasma membrane and pyroptosis, as well as loss of FT bactericidal activity; when associated with A-146; A-152 FT and A-154. Partial loss of homooligomerization and FT pyroptosis; when associated with A-146." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 146 FT /note="K->A: Complete loss of homooligomerization, lipid- FT binding, relocalization of Gasdermin-D, N-terminal to the FT plasma membrane and pyroptosis, as well as loss of FT bactericidal activity; when associated with A-138 or with FT S-138; A-152 and A-154. Partial loss of homooligomerization FT and pyroptosis; when associated with A-138, with A-152 or FT with A-152 and A-154." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 152 FT /note="R->A: Complete loss of homooligomerization, lipid- FT binding, relocalization of Gasdermin-D, N-terminal to the FT plasma membrane and pyroptosis, as well as loss of FT bactericidal activity; when associated with A-138 or with FT S-138; A-146 and A-154. Partial loss of homooligomerization FT and pyroptosis; when associated with A-146 or with A-154, FT or with A-146 and A-154." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 154 FT /note="R->A: Complete loss of homooligomerization, lipid- FT binding, relocalization of Gasdermin-D, N-terminal to the FT plasma membrane and pyroptosis, as well as loss of FT bactericidal activity; when associated with A-138 or with FT S-138; A-146 and A-152. Partial loss of homooligomerization FT and pyroptosis; when associated with A-152 or with A-146 FT and A-152." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 192 FT /note="C->A: Loss of oligomerization of Gasdermin-D, N- FT terminal." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 237 FT /note="K->A: No effect on pyroptosis; when associated with FT A-239 or with A-239; A-248 and A-249." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 239 FT /note="R->A: No effect on pyroptosis; when associated with FT A-237 or with A-237; A-248 and A-249." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 248 FT /note="R->A: No effect on pyroptosis; when associated with FT A-237; A-239 and A-249." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 249 FT /note="K->A: No effect on pyroptosis; when associated with FT A-237; A-239 and A-248." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 265 FT /note="C->A: No effect on oligomerization." FT /evidence="ECO:0000269|PubMed:27383986" FT MUTAGEN 276 FT /note="D->A,N: Loss of CASP1-induced cleavage, pyroptosis FT and IL1B release." FT /evidence="ECO:0000269|PubMed:26375259, FT ECO:0000269|PubMed:26611636" FT HELIX 6..15 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 19..21 FT /evidence="ECO:0000244|PDB:6N9N" FT HELIX 32..35 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 40..43 FT /evidence="ECO:0000244|PDB:6N9N" FT TURN 63..65 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 66..68 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 87..89 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 119..125 FT /evidence="ECO:0000244|PDB:6N9N" FT HELIX 128..137 FT /evidence="ECO:0000244|PDB:6N9N" FT HELIX 148..152 FT /evidence="ECO:0000244|PDB:6N9N" FT TURN 153..155 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 157..167 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 171..173 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 207..209 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 214..223 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 225..227 FT /evidence="ECO:0000244|PDB:6N9N" FT STRAND 229..233 FT /evidence="ECO:0000244|PDB:6N9N" FT HELIX 289..304 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 308..321 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 325..341 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 350..356 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 357..359 FT /evidence="ECO:0000244|PDB:6AO3" FT STRAND 364..366 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 368..383 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 386..396 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 400..414 FT /evidence="ECO:0000244|PDB:6AO3" FT STRAND 422..424 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 428..431 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 440..446 FT /evidence="ECO:0000244|PDB:6AO3" FT TURN 447..449 FT /evidence="ECO:0000244|PDB:6AO3" FT STRAND 454..457 FT /evidence="ECO:0000244|PDB:6AO3" FT STRAND 459..461 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 463..465 FT /evidence="ECO:0000244|PDB:6AO3" FT HELIX 466..482 FT /evidence="ECO:0000244|PDB:6AO3" SQ SEQUENCE 487 AA; 53238 MW; 6702C95B0F92BC49 CRC64; MPSAFEKVVK NVIKEVSGSR GDLIPVDSLR NSTSFRPYCL LNRKFSSSRF WKPRYSCVNL SIKDILEPSA PEPEPECFGS FKVSDVVDGN IQGRVMLSGM GEGKISGGAA VSDSSSASMN VCILRVTQKT WETMQHERHL QQPENKILQQ LRSRGDDLFV VTEVLQTKEE VQITEVHSQE GSGQFTLPGA LCLKGEGKGH QSRKKMVTIP AGSILAFRVA QLLIGSKWDI LLVSDEKQRT FEPSSGDRKA VGQRHHGLNV LAALCSIGKQ LSLLSDGIDE EELIEAADFQ GLYAEVKACS SELESLEMEL RQQILVNIGK ILQDQPSMEA LEASLGQGLC SGGQVEPLDG PAGCILECLV LDSGELVPEL AAPIFYLLGA LAVLSETQQQ LLAKALETTV LSKQLELVKH VLEQSTPWQE QSSVSLPTVL LGDCWDEKNP TWVLLEECGL RLQVESPQVH WEPTSLIPTS ALYASLFLLS SLGQKPC //