GSDMC_MOUSE
ID GSDMC_MOUSE Reviewed; 468 AA.
AC Q99NB5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Gasdermin-C {ECO:0000303|PubMed:17350798};
DE AltName: Full=Gasdermin-C1 {ECO:0000303|PubMed:17350798};
DE AltName: Full=Melanoma-derived leucine zipper-containing extranuclear factor {ECO:0000303|PubMed:11223543};
DE Short=mMLZE {ECO:0000303|PubMed:11223543};
DE Contains:
DE RecName: Full=Gasdermin-C, N-terminal {ECO:0000305};
DE Short=GSDMC-NT {ECO:0000305};
DE Contains:
DE RecName: Full=Gasdermin-C, C-terminal {ECO:0000305};
DE Short=GSDMC-CT {ECO:0000305};
GN Name=Gsdmc {ECO:0000303|PubMed:17350798, ECO:0000312|MGI:MGI:1933176};
GN Synonyms=Gsdmc1 {ECO:0000303|PubMed:17350798},
GN Mlze {ECO:0000303|PubMed:11223543};
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:BAB40332.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Melanoma {ECO:0000269|PubMed:11223543};
RX PubMed=11223543; DOI=10.1111/j.1349-7006.2001.tb01076.x;
RA Watabe K., Ito A., Asada H., Endo Y., Kobayashi T., Nakamoto K., Itami S.,
RA Takao S., Shinomura Y., Aikou T., Yoshikawa K., Matsuzawa Y., Kitamura Y.,
RA Nojima H.;
RT "Structure, expression and chromosome mapping of MLZE, a novel gene which
RT is preferentially expressed in metastatic melanoma cells.";
RL Jpn. J. Cancer Res. 92:140-151(2001).
RN [2] {ECO:0000312|EMBL:BAE23451.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23451.1};
RC TISSUE=Vagina {ECO:0000312|EMBL:BAE23451.1};
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 [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-C]: This form constitutes the precursor of the
CC pore-forming protein: upon cleavage, the released N-terminal moiety
CC (Gasdermin-C, N-terminal) binds to membranes and forms pores,
CC triggering cell death. {ECO:0000250|UniProtKB:Q96QA5}.
CC -!- FUNCTION: [Gasdermin-C, 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-C]: 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-C, N-terminal).
CC {ECO:0000250|UniProtKB:Q5Y4Y6}.
CC -!- SUBUNIT: [Gasdermin-C, 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-C]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BYG8}.
CC -!- SUBCELLULAR LOCATION: [Gasdermin-C, 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 -!- CAUTION: Despite its name, does not contains a functional leucine
CC zipper. {ECO:0000305|PubMed:11223543}.
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DR EMBL; AB042406; BAB40332.1; -; mRNA.
DR EMBL; AK137662; BAE23451.1; -; mRNA.
DR CCDS; CCDS37086.1; -.
DR RefSeq; NP_113555.1; NM_031378.3.
DR AlphaFoldDB; Q99NB5; -.
DR SMR; Q99NB5; -.
DR STRING; 10090.ENSMUSP00000105752; -.
DR iPTMnet; Q99NB5; -.
DR PhosphoSitePlus; Q99NB5; -.
DR PaxDb; Q99NB5; -.
DR PRIDE; Q99NB5; -.
DR ProteomicsDB; 269842; -.
DR DNASU; 83492; -.
DR Ensembl; ENSMUST00000110125; ENSMUSP00000105752; ENSMUSG00000079025.
DR GeneID; 83492; -.
DR KEGG; mmu:83492; -.
DR UCSC; uc007vyt.1; mouse.
DR CTD; 56169; -.
DR MGI; MGI:1933176; Gsdmc.
DR VEuPathDB; HostDB:ENSMUSG00000079025; -.
DR eggNOG; ENOG502S0IQ; Eukaryota.
DR GeneTree; ENSGT00950000183140; -.
DR HOGENOM; CLU_040752_2_0_1; -.
DR InParanoid; Q99NB5; -.
DR OMA; ISLWITY; -.
DR OrthoDB; 1067854at2759; -.
DR PhylomeDB; Q99NB5; -.
DR TreeFam; TF331886; -.
DR BioGRID-ORCS; 83492; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gsdmc; mouse.
DR PRO; PR:Q99NB5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99NB5; protein.
DR Bgee; ENSMUSG00000079025; Expressed in left colon and 61 other tissues.
DR ExpressionAtlas; Q99NB5; baseline and differential.
DR Genevisible; Q99NB5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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..468
FT /note="Gasdermin-C"
FT /id="PRO_0000349129"
FT CHAIN 1..?
FT /note="Gasdermin-C, N-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451676"
FT CHAIN ?..468
FT /note="Gasdermin-C, C-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451677"
FT REGION 1..230
FT /note="Triggers pyroptosis"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG8"
SQ SEQUENCE 468 AA; 52743 MW; 95691D85F4C57168 CRC64;
MSYTFDWLSK DVVKKLQGRD LRPVKCLSDA TKFCLFNILQ ETSSRLALKT EYIPVGFTLL
HLLEPNIPVP EPEVSAPIPL KHTISQKLKA DLDVETIAGG EAGFVKSCGY DIEVQSKSIP
NPKLESLQNR KLLDQLPTFM KTCWKDGKNL YVVTEAYEVT KDTVLEGTSN SKFAIKGIIN
QLVKVGGSGQ WQTEKTDSIP IQKGSVLAYK KQQLVIEDNT CVILTSANTK KKMTFPMRFV
GMSGHLRYQD LVIETGSWIN DIDPIGTIKE PTHLDFMCLQ NEVSEQTRLL AELSKDVQEV
VFSSFLHMLC DRDVLYDLMK MLELNQLGHM DGPGGKILDE LRKDSSLSWI NLKDLILYLL
QALMVLSDTQ LCLLALSVEM RLLPHQVELV KSILQPNFKY PWNIPFTLQP QLLAPLQGEG
LAITYELLEE CGLKMELNNP RSTWDLEAKM PLSALYGSLS FLQQLSEA
