ID GSDC3_MOUSE Reviewed; 480 AA. AC Q8CB12; E9QJY6; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 10-FEB-2021, entry version 100. DE RecName: Full=Gasdermin-C3 {ECO:0000303|PubMed:17350798}; DE Contains: DE RecName: Full=Gasdermin-C3, N-terminal {ECO:0000305}; DE Short=GSDMC3-NT {ECO:0000305}; DE Contains: DE RecName: Full=Gasdermin-C3, C-terminal {ECO:0000305}; DE Short=GSDMC3-CT {ECO:0000305}; GN Name=Gsdmc3 {ECO:0000303|PubMed:17350798, ECO:0000312|MGI:MGI:3580656}; 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] {ECO:0000312|EMBL:BAC29694.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29694.1}; RC TISSUE=Vagina {ECO:0000312|EMBL:BAC29694.1}; 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 GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0000305} RP IDENTIFICATION. RX PubMed=17350798; DOI=10.1016/j.ygeno.2007.01.003; RA Tamura M., Tanaka S., Fujii T., Aoki A., Komiyama H., Ezawa K., RA Sumiyama K., Sagai T., Shiroishi T.; RT "Members of a novel gene family, Gsdm, are expressed exclusively in the RT epithelium of the skin and gastrointestinal tract in a highly tissue- RT specific manner."; RL Genomics 89:618-629(2007). CC -!- FUNCTION: [Gasdermin-C3]: This form constitutes the precursor of the CC pore-forming protein: upon cleavage, the released N-terminal moiety CC (Gasdermin-C3, N-terminal) binds to membranes and forms pores, CC triggering cell death. {ECO:0000250|UniProtKB:Q96QA5}. CC -!- FUNCTION: [Gasdermin-C3, N-terminal]: Pore-forming protein that causes CC membrane permeabilization and pyroptosis (By similarity). Released upon CC cleavage and binds to membrane inner leaflet lipids. Homooligomerizes CC within the membrane and forms pores of 10-15 nanometers (nm) of inner CC diameter, triggering pyroptosis (By similarity). The functional CC mechanisms and physiological proteases that cleave and activate this CC pore-forming protein are unknown (By similarity). CC {ECO:0000250|UniProtKB:Q96QA5, ECO:0000250|UniProtKB:Q9BYG8}. CC -!- ACTIVITY REGULATION: [Gasdermin-C3]: The full-length protein before CC cleavage is inactive: intramolecular interactions between N- and C- CC terminal domains mediate autoinhibition in the absence of activation CC signal. The intrinsic pyroptosis-inducing activity is carried by the CC released N-terminal moiety (Gasdermin-C3, N-terminal). CC {ECO:0000250|UniProtKB:Q5Y4Y6}. CC -!- SUBUNIT: [Gasdermin-C3, N-terminal]: Homooligomer; homooligomeric ring- CC shaped pore complex containing 27-28 subunits when inserted in the CC membrane. {ECO:0000250|UniProtKB:Q5Y4Y6}. CC -!- SUBCELLULAR LOCATION: [Gasdermin-C3]: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9BYG8}. CC -!- SUBCELLULAR LOCATION: [Gasdermin-C3, N-terminal]: Cell membrane CC {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q5Y4Y6}. CC -!- DOMAIN: Intramolecular interactions between N- and C-terminal domains CC are important for autoinhibition in the absence of activation signal. CC The intrinsic pyroptosis-inducing activity is carried by the N-terminal CC domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. CC -!- PTM: Cleavage relieves autoinhibition by releasing the N-terminal CC moiety (Gasdermin-C, N-terminal) that initiates pyroptosis. CC {ECO:0000250|UniProtKB:P57764}. 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; AK037079; BAC29694.1; -; mRNA. DR EMBL; AC140673; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS37088.1; -. DR RefSeq; NP_899017.2; NM_183194.3. DR RefSeq; XP_006521088.1; XM_006521025.3. DR RefSeq; XP_011243950.1; XM_011245648.2. DR RefSeq; XP_017172127.1; XM_017316638.1. DR RefSeq; XP_017172128.1; XM_017316639.1. DR RefSeq; XP_017172129.1; XM_017316640.1. DR RefSeq; XP_017172130.1; XM_017316641.1. DR RefSeq; XP_017172131.1; XM_017316642.1. DR RefSeq; XP_017172132.1; XM_017316643.1. DR RefSeq; XP_017172133.1; XM_017316644.1. DR RefSeq; XP_017172134.1; XM_017316645.1. DR RefSeq; XP_017172135.1; XM_017316646.1. DR RefSeq; XP_017172136.1; XM_017316647.1. DR RefSeq; XP_017172137.1; XM_017316648.1. DR RefSeq; XP_017172138.1; XM_017316649.1. DR RefSeq; XP_017172139.1; XM_017316650.1. DR RefSeq; XP_017172140.1; XM_017316651.1. DR RefSeq; XP_017172141.1; XM_017316652.1. DR RefSeq; XP_017172142.1; XM_017316653.1. DR SMR; Q8CB12; -. DR iPTMnet; Q8CB12; -. DR PhosphoSitePlus; Q8CB12; -. DR MaxQB; Q8CB12; -. DR PaxDb; Q8CB12; -. DR PRIDE; Q8CB12; -. DR Ensembl; ENSMUST00000089894; ENSMUSP00000087339; ENSMUSG00000055827. DR Ensembl; ENSMUST00000185526; ENSMUSP00000140272; ENSMUSG00000055827. DR Ensembl; ENSMUST00000190682; ENSMUSP00000139472; ENSMUSG00000055827. DR GeneID; 270328; -. DR KEGG; mmu:270328; -. DR UCSC; uc007vza.2; mouse. DR CTD; 270328; -. DR MGI; MGI:3580656; Gsdmc3. DR eggNOG; ENOG502S0IQ; Eukaryota. DR GeneTree; ENSGT00950000183140; -. DR HOGENOM; CLU_040752_2_0_1; -. DR InParanoid; Q8CB12; -. DR OMA; WINDIEP; -. DR OrthoDB; 1067854at2759; -. DR TreeFam; TF331886; -. DR BioGRID-ORCS; 270328; 0 hits in 17 CRISPR screens. DR ChiTaRS; Gsdmc3; mouse. DR PRO; PR:Q8CB12; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q8CB12; protein. DR Bgee; ENSMUSG00000055827; Expressed in ileum and 26 other tissues. DR GO; GO:0034451; C:centriolar satellite; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IBA:GO_Central. DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central. DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central. DR GO; GO:0070269; P:pyroptosis; IBA:GO_Central. 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 2: Evidence at transcript level; KW Cell membrane; Cytoplasm; Membrane; Necrosis; Reference proteome; KW Transmembrane; Transmembrane beta strand. FT CHAIN 1..480 FT /note="Gasdermin-C3" FT /id="PRO_0000347332" FT CHAIN 1..? FT /note="Gasdermin-C3, N-terminal" FT /evidence="ECO:0000305" FT /id="PRO_0000451680" FT CHAIN ?..480 FT /note="Gasdermin-C3, C-terminal" FT /evidence="ECO:0000305" FT /id="PRO_0000451681" FT REGION 1..226 FT /note="Triggers pyroptosis" FT /evidence="ECO:0000250|UniProtKB:Q9BYG8" FT CONFLICT 383 FT /note="P -> T (in Ref. 1; BAC29694)" FT /evidence="ECO:0000305" SQ SEQUENCE 480 AA; 54188 MW; BEA95A9F8FFEEA6A CRC64; MGYSFDRASK DVVKKLQGRD LRPVECLSDA TKFRLFHILQ ETPRSGWETE DIPVGFTLLD LLEPNFPVPE PEVSAPKPFI HVQSTDLEAN LNVADIARGG VGYVGYGGYN IEVQSTSIPN PKLEILQNRK LLDKLPTFMK FCRMERKNLY VVTEAYEVSK DTMLTGLSSV NLLVKGFFKQ LFKVRGKAGR SEKYSIPIPK GSVLAYKKQQ LVIENNTCVI LPSATKKKMT FPGTPKYASA SEPTEIYRTE LQGLWINDIE PIGRIQEPAH LDFKCLQYEV SEQTRLLPEL SKDVQEVVLS SFLSMLYEGD RNVLHDLMKM LELSQLGHMD GPGGKILDEL RKDSSNPCVD LKDLILYLLQ ALMVLSDSQL NLLARSVEMR LLPHQVELVT SILQPNFKYP WNIPFTVQPQ LLAPLQGEGL AITYELLEEC GLKMELNNPR STWDLEAKMP LSALYGSLSF LQQLQKANSS FKPSLRPGYI //