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 31-JUL-2019, entry version 115. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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., RA Zhong C.Q., Han J.; RT "Gasdermin D is an executor of pyroptosis and required for RT interleukin-1beta secretion."; RL Cell Res. 25:1285-1298(2015). RN [4] RP PROTEIN SEQUENCE OF 277-288, FUNCTION, DISRUPTION PHENOTYPE, RP MUTAGENESIS OF 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., RA Warming S., Cuellar T., Haley B., Roose-Girma M., Phung Q.T., RA Liu P.S., Lill J.R., Li H., Wu J., Kummerfeld S., Zhang J., Lee W.P., RA Snipas S.J., Salvesen G.S., Morris L.X., Fitzgerald L., Zhang Y., RA Bertram E.M., 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 RT 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., RA Cai T., 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 RP ACTIVATION WITH NLRC4 INFLAMMASOME. RX PubMed=27418190; DOI=10.15252/embj.201694696; RA Sborgi L., Ruehl S., Mulvihill E., Pipercevic J., Heilig R., RA Stahlberg H., Farady C.J., Mueller D.J., Broz P., Hiller S.; RT "GSDMD membrane pore formation constitutes the mechanism of pyroptotic RT cell 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., RA Abbott D.W., Dubyak G.R.; RT "Active caspase-1 induces plasma membrane pores that precede RT pyroptotic 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., RA Lieberman J.; RT "Inflammasome-activated gasdermin D causes pyroptosis by forming RT membrane pores."; RL Nature 535:153-158(2016). CC -!- FUNCTION: Gasdermin-D, N-terminal: Promotes pyroptosis in response CC to microbial infection and danger signals. Produced by the CC cleavage of gasdermin-D by inflammatory caspases CASP1 or CASP4 in CC response to canonical, as well as non-canonical (such as cytosolic CC LPS) inflammasome activators (PubMed:26611636, PubMed:26375259, CC PubMed:26375003, PubMed:27418190, PubMed:27385778, CC PubMed:27383986). After cleavage, moves to the plasma membrane CC where it strongly binds to membrane inner leaflet lipids, CC including monophosphorylated phosphatidylinositols, such as CC phosphatidylinositol 4-phosphate, bisphosphorylated CC phosphatidylinositols, such as phosphatidylinositol (4,5)- CC 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 CC bactericidal activity. Gasdermin-D, N-terminal released from CC pyroptotic cells into the extracellular milieu rapidly binds to CC and kills both Gram-negative and Gram-positive bacteria, without CC harming neighboring mammalian cells, as it does not disrupt the CC plasma membrane from the outside due to lipid-binding specificity. CC Under cell culture conditions, also active against intracellular CC bacteria, such as Listeria monocytogenes. Strongly binds to CC bacterial and mitochondrial lipids, including cardiolipin. Does CC not bind to phosphatidylethanolamine or phosphatidylcholine CC (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 CC to that of uncleaved CASP1 precursor. Although this recruitment is CC also observed in the absence of PYCARD, it is more efficient in CC its presence (PubMed:26611636). Gasdermin-D, N-terminal forms CC disulfide-linked homooligomers (16-mers) in a Ca(+2)-independent CC manner. Oligomerization occurs in the presence of membranes; CC remains monomeric in the cytosol (PubMed:27383986). CC {ECO:0000269|PubMed:26611636, 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 CC NLRP3 inflammasone with similar kinetics to that of uncleaved CC CASP1 precursor. {ECO:0000269|PubMed:26611636}. CC -!- SUBCELLULAR LOCATION: Gasdermin-D, N-terminal: Cell membrane CC {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. CC Secreted {ECO:0000269|PubMed:27383986}. Note=Released in the CC extracellular milieu following pyroptosis. CC {ECO:0000269|PubMed:27383986}. CC -!- DEVELOPMENTAL STAGE: Expression starts at 8.5 dpc and increases CC from 13.5 dpc on. Still detected after birth. CC {ECO:0000269|PubMed:18693275}. CC -!- DOMAIN: Intramolecular interactions between N- and C-terminal CC domains may be important for autoinhibition in the absence of CC cleavage by inflammatory caspases CASP1 or CASP4. The intrinsic CC pyroptosis-inducing activity is carried by gasdermin-D, N- CC terminal, that is released upon cleavage by inflammatory caspases. CC {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, CC 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 CC initiate pyroptosis (PubMed:26375259, PubMed:26611636). Cleavage CC at Asp-88 by 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 CC Mendelian rate and do not exhibit any overt phenotype in normal CC housing conditions. The gastrointestinal tract develops normally. CC They are however resistant to LPS-induced lethal septic shock. CC Primary bone marrow-derived macrophages fail to undergo pyroptosis CC in response to canonical (acting via CASP1), as well as to non- CC canonical (acting via CASP4) inflammasome activators. CASP1- CC mediated IL1B release is also impaired, but not CASP1 CC autoprocessing, nor IL1B maturation. {ECO:0000269|PubMed:18693275, CC ECO:0000269|PubMed:26375003, 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; QGPTCAL; -. 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 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Immunity; Inflammasome; KW Inflammatory response; Innate immunity; Membrane; Necrosis; KW Phosphoprotein; Reference proteome; Secreted. FT CHAIN 1 487 Gasdermin-D. FT /FTId=PRO_0000148176. FT CHAIN 1 276 Gasdermin-D, N-terminal. FT {ECO:0000305|PubMed:27383986}. FT /FTId=PRO_0000437528. FT CHAIN 277 487 Gasdermin-D, C-terminal. FT {ECO:0000305|PubMed:27383986}. FT /FTId=PRO_0000437529. FT SITE 88 89 Cleavage; by CASP3. FT {ECO:0000250|UniProtKB:P57764}. FT SITE 276 277 Cleavage; by inflammatory caspases CASP1 FT and CASP4. {ECO:0000269|PubMed:26375259}. FT MOD_RES 38 38 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P57764}. FT MUTAGEN 39 39 C->A: Loss of oligomerization of FT Gasdermin-D, N-terminal. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 57 57 C->A: No effect on oligomerization. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 77 77 C->A: No effect on oligomerization. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 105 105 I->N: Loss of cytosolic LPS-induced IL1B FT release and pyroptosis in bone marrow- FT derived macrophages. No effect on protein FT expression. No effect on cleavage by FT CASP4. {ECO:0000269|PubMed:26375259}. FT MUTAGEN 122 122 C->A: No effect on oligomerization. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 138 138 R->A,S: Complete loss of FT homooligomerization, lipid-binding, FT relocalization of Gasdermin-D, N-terminal FT to the plasma membrane and pyroptosis, as FT well as loss of bactericidal activity; FT when associated with A-146; A-152 and A- FT 154. Partial loss of homooligomerization FT and pyroptosis; when associated with A- FT 146. {ECO:0000269|PubMed:27383986}. FT MUTAGEN 146 146 K->A: Complete loss of FT homooligomerization, lipid-binding, FT relocalization of Gasdermin-D, N-terminal FT to the plasma membrane and pyroptosis, as FT well as loss of bactericidal activity; FT when associated with A-138 or with S-138; FT A-152 and A-154. Partial loss of FT homooligomerization and pyroptosis; when FT associated with A-138, with A-152 or with FT A-152 and A-154. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 152 152 R->A: Complete loss of FT homooligomerization, lipid-binding, FT relocalization of Gasdermin-D, N-terminal FT to the plasma membrane and pyroptosis, as FT well as loss of bactericidal activity; FT when associated with A-138 or with S-138; FT A-146 and A-154. Partial loss of FT homooligomerization and pyroptosis; when FT associated with A-146 or with A-154, or FT with A-146 and A-154. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 154 154 R->A: Complete loss of FT homooligomerization, lipid-binding, FT relocalization of Gasdermin-D, N-terminal FT to the plasma membrane and pyroptosis, as FT well as loss of bactericidal activity; FT when associated with A-138 or with S-138; FT A-146 and A-152. Partial loss of FT homooligomerization and pyroptosis; when FT associated with A-152 or with A-146 and FT A-152. {ECO:0000269|PubMed:27383986}. FT MUTAGEN 192 192 C->A: Loss of oligomerization of FT Gasdermin-D, N-terminal. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 237 237 K->A: No effect on pyroptosis; when FT associated with A-239 or with A-239; A- FT 248 and A-249. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 239 239 R->A: No effect on pyroptosis; when FT associated with A-237 or with A-237; A- FT 248 and A-249. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 248 248 R->A: No effect on pyroptosis; when FT associated with A-237; A-239 and A-249. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 249 249 K->A: No effect on pyroptosis; when FT associated with A-237; A-239 and A-248. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 265 265 C->A: No effect on oligomerization. FT {ECO:0000269|PubMed:27383986}. FT MUTAGEN 276 276 D->A,N: Loss of CASP1-induced cleavage, FT pyroptosis and IL1B release. FT {ECO:0000269|PubMed:26375259, FT ECO:0000269|PubMed:26611636}. FT HELIX 289 304 {ECO:0000244|PDB:6AO3}. FT HELIX 308 321 {ECO:0000244|PDB:6AO3}. FT HELIX 325 341 {ECO:0000244|PDB:6AO3}. FT HELIX 350 356 {ECO:0000244|PDB:6AO3}. FT HELIX 357 359 {ECO:0000244|PDB:6AO3}. FT STRAND 364 366 {ECO:0000244|PDB:6AO3}. FT HELIX 368 383 {ECO:0000244|PDB:6AO3}. FT HELIX 386 396 {ECO:0000244|PDB:6AO3}. FT HELIX 400 414 {ECO:0000244|PDB:6AO3}. FT STRAND 422 424 {ECO:0000244|PDB:6AO3}. FT HELIX 428 431 {ECO:0000244|PDB:6AO3}. FT HELIX 440 446 {ECO:0000244|PDB:6AO3}. FT TURN 447 449 {ECO:0000244|PDB:6AO3}. FT STRAND 454 457 {ECO:0000244|PDB:6AO3}. FT STRAND 459 461 {ECO:0000244|PDB:6AO3}. FT HELIX 463 465 {ECO:0000244|PDB:6AO3}. FT HELIX 466 482 {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 //