GSDMC_RAT
ID GSDMC_RAT Reviewed; 474 AA.
AC P85967;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Gasdermin-C;
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:0000312|RGD:1308989};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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}.
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DR EMBL; AABR03055675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P85967; -.
DR SMR; P85967; -.
DR STRING; 10116.ENSRNOP00000041988; -.
DR PaxDb; P85967; -.
DR UCSC; RGD:1308989; rat.
DR RGD; 1308989; Gsdmc.
DR eggNOG; ENOG502S0IQ; Eukaryota.
DR InParanoid; P85967; -.
DR PhylomeDB; P85967; -.
DR TreeFam; TF331886; -.
DR PRO; PR:P85967; -.
DR Proteomes; UP000002494; Unplaced.
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 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Membrane; Necrosis; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..474
FT /note="Gasdermin-C"
FT /id="PRO_0000349130"
FT CHAIN 1..?
FT /note="Gasdermin-C, N-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451684"
FT CHAIN ?..474
FT /note="Gasdermin-C, C-terminal"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451685"
FT REGION 1..237
FT /note="Triggers pyroptosis"
FT /evidence="ECO:0000250|UniProtKB:Q9BYG8"
SQ SEQUENCE 474 AA; 53252 MW; 1338F7E3DEEE99F5 CRC64;
MLYTFDQVSK DVVKKLQGKD LRPVRCLSDA TKFRQFDILQ KTPQSLFFKS EDTPVGYSLL
QILEPNFPVP ETEVSAPMPL KHITSQKWKA DVDVKATIAD GGASAEFVQS CGYDIEVQSR
SIPDSKLESL QNRQGPWGKL LDKKLSFVTD CQMGRNNLYV VTEVFEVTKD TVVQGSSSID
LSGKALVSQL VKGEAQGQWQ RETTDLVPIP KGAVLAYKKK QLVIENNTCA ILLSANAKKK
TFPGIFNFGM SSRSQTMEIV NSSWIDYIPP IGRIEEPVHL DFKYLEKEVF LRKEQLAMLS
KDVQDVVFSN LLPMLSDSDV LFDLINMLEL DQLGHMDGPA GLILDELRKN SSTPWIDLKG
LILYLLQALM VLSDTQLDLL AQSMEMRILL QQRELVRSIL EPNFKYPWNI PFTLQPQLLA
PLQGEGLAIT YELLKGCGLK MEPNSPRSTW DLEAKMPLSA LYGILSCLQQ LVEA
