GSDC2_MOUSE
ID GSDC2_MOUSE Reviewed; 480 AA.
AC Q2KHK6; Q2KHK8; Q8CC94;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Gasdermin-C2 {ECO:0000303|PubMed:17350798};
DE Contains:
DE RecName: Full=Gasdermin-C2, N-terminal {ECO:0000305};
DE Short=GSDMC2-NT {ECO:0000305};
DE Contains:
DE RecName: Full=Gasdermin-C2, C-terminal {ECO:0000305};
DE Short=GSDMC2-CT {ECO:0000305};
GN Name=Gsdmc2 {ECO:0000303|PubMed:17350798, ECO:0000312|MGI:MGI:2146102};
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:BAC28384.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28384.1};
RC TISSUE=Cecum {ECO:0000312|EMBL:BAC28384.1};
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] {ECO:0000312|EMBL:AAI13156.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {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-C2]: This form constitutes the precursor of the
CC pore-forming protein: upon cleavage, the released N-terminal moiety
CC (Gasdermin-C2, N-terminal) binds to membranes and forms pores,
CC triggering cell death. {ECO:0000250|UniProtKB:Q96QA5}.
CC -!- FUNCTION: [Gasdermin-C2, 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-C2]: 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-C2, N-terminal).
CC {ECO:0000250|UniProtKB:Q5Y4Y6}.
CC -!- SUBUNIT: [Gasdermin-C2, 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-C2]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BYG8}.
CC -!- SUBCELLULAR LOCATION: [Gasdermin-C2, 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}.
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DR EMBL; AK033603; BAC28384.1; -; mRNA.
DR EMBL; BC113153; AAI13154.1; -; mRNA.
DR EMBL; BC113155; AAI13156.1; -; mRNA.
DR CCDS; CCDS37087.1; -.
DR RefSeq; NP_001161746.1; NM_001168274.1.
DR RefSeq; NP_808580.2; NM_177912.4.
DR RefSeq; XP_006521159.1; XM_006521096.3.
DR RefSeq; XP_006521160.1; XM_006521097.3.
DR RefSeq; XP_006521161.1; XM_006521098.3.
DR RefSeq; XP_011243969.1; XM_011245667.2.
DR RefSeq; XP_011243970.1; XM_011245668.2.
DR RefSeq; XP_011243971.1; XM_011245669.2.
DR RefSeq; XP_011243972.1; XM_011245670.2.
DR RefSeq; XP_011243973.1; XM_011245671.2.
DR RefSeq; XP_011243974.1; XM_011245672.2.
DR RefSeq; XP_011243975.1; XM_011245673.2.
DR RefSeq; XP_011243976.1; XM_011245674.2.
DR RefSeq; XP_011243977.1; XM_011245675.2.
DR RefSeq; XP_011243978.1; XM_011245676.2.
DR RefSeq; XP_011243979.1; XM_011245677.2.
DR AlphaFoldDB; Q2KHK6; -.
DR SMR; Q2KHK6; -.
DR STRING; 10090.ENSMUSP00000140487; -.
DR MaxQB; Q2KHK6; -.
DR PaxDb; Q2KHK6; -.
DR PRIDE; Q2KHK6; -.
DR ProteomicsDB; 271173; -.
DR DNASU; 331063; -.
DR Ensembl; ENSMUST00000089900; ENSMUSP00000087344; ENSMUSG00000056293.
DR Ensembl; ENSMUST00000188404; ENSMUSP00000141066; ENSMUSG00000056293.
DR Ensembl; ENSMUST00000188691; ENSMUSP00000140487; ENSMUSG00000056293.
DR GeneID; 331063; -.
DR KEGG; mmu:331063; -.
DR UCSC; uc007vyu.1; mouse.
DR CTD; 331063; -.
DR MGI; MGI:2146102; Gsdmc2.
DR VEuPathDB; HostDB:ENSMUSG00000056293; -.
DR eggNOG; ENOG502S0IQ; Eukaryota.
DR GeneTree; ENSGT00950000183140; -.
DR HOGENOM; CLU_040752_2_0_1; -.
DR InParanoid; Q2KHK6; -.
DR OMA; WDLEAKV; -.
DR OrthoDB; 1067854at2759; -.
DR PhylomeDB; Q2KHK6; -.
DR TreeFam; TF331886; -.
DR BioGRID-ORCS; 331063; 0 hits in 40 CRISPR screens.
DR PRO; PR:Q2KHK6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q2KHK6; protein.
DR Bgee; ENSMUSG00000056293; Expressed in renal medulla collecting duct and 51 other tissues.
DR Genevisible; Q2KHK6; MM.
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: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:0060576; P:intestinal epithelial cell development; IEP:UniProtKB.
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-C2"
FT /id="PRO_0000347331"
FT CHAIN 1..?
FT /note="Gasdermin-C2, N-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451678"
FT CHAIN ?..480
FT /note="Gasdermin-C2, C-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451679"
FT REGION 1..226
FT /note="Triggers pyroptosis"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG8"
FT CONFLICT 134
FT /note="N -> K (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="Q -> H (in Ref. 1; BAC28384)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="M -> L (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="S -> T (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="N -> C (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="E -> K (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="I -> L (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="P -> T (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..403
FT /note="PWNI -> SSNT (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="L -> V (in Ref. 2; AAI13156)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> Q (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="R -> S (in Ref. 2; AAI13154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 53952 MW; C1F78ECDB8D4AAD1 CRC64;
MGYSFDRASK DVVKKLQGRD LRPVECLSDA TKFRLFHILQ ETPRSGWETE DIPVGFTLLD
LLEPNFPVPE PEVSAPKPFI HVQSTDLEAN LNVADIARGG VGYVGYGGYN IEVQSTSIPN
PKLEILQNRK LLDNLPTFMK FCRMERKNLY VVTEAYEVSK DTMLTGLSSV NLSVKGFFKQ
LFKVRGKAGR SEKYSIPIPK GSVLAYKKQQ LVIENNTCVI LPSATKKKMT FPGTPKYASA
SEPTEIYRTE LQGLWINDIV PIGRIQEPAH LDFMCLQNEV YKQTEQLAEL SKGVQEVVLS
SILSMLYEGD RKVLYDLMNM LELNQLGHMD GPGGKILDEL RKDSSNPCVD LKDLILYLLQ
ALMVLSDSQL NLLAQSVEMG ILPHQVELVK SILQPNFKYP WNIPFTLQPQ LLAPLQGEGL
AITYELLEEC GLKMELNNPR STWDLEAKMP LSALYGSLSF LQQLRKANSS SKPSLRPGYI
