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CASP1_MOUSE
ID   CASP1_MOUSE             Reviewed;         402 AA.
AC   P29452;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 205.
DE   RecName: Full=Caspase-1;
DE            Short=CASP-1;
DE            EC=3.4.22.36 {ECO:0000269|PubMed:21147462};
DE   AltName: Full=Interleukin-1 beta convertase;
DE            Short=IL-1BC;
DE   AltName: Full=Interleukin-1 beta-converting enzyme;
DE            Short=ICE;
DE            Short=IL-1 beta-converting enzyme;
DE   AltName: Full=p45;
DE   Contains:
DE     RecName: Full=Caspase-1 subunit p20 {ECO:0000305|PubMed:32109412};
DE   Contains:
DE     RecName: Full=Caspase-1 subunit p10 {ECO:0000305|PubMed:32109412};
DE   Flags: Precursor;
GN   Name=Casp1; Synonyms=Il1bc;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=1431103;
RA   Nett-Fiordalisi M.A., Cerretti D.P., Berson D.R., Gilbert D.J.,
RA   Jenkins N.A., Copeland N.G., Black R.A., Chaplin D.D.;
RT   "Molecular cloning of the murine IL-1 beta converting enzyme cDNA.";
RL   J. Immunol. 149:3254-3259(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8446594; DOI=10.1073/pnas.90.5.1809;
RA   Molineaux S.M., Casano F.J., Rolando A.M., Peterson E.P., Limjuco G.,
RA   Chin J., Griffin P.R., Calaycay J.R., Ding G.J.-F., Yamin T.-T.,
RA   Palyha O.C., Luell S., Fletcher D., Miller D.K., Howard A.D.,
RA   Thornberry N.A., Kostura M.J.;
RT   "Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a
RT   structurally conserved homologue of human IL-1 beta converting enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1809-1813(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=8034321; DOI=10.1006/geno.1994.1203;
RA   Casano F.J., Rolando A.M., Mudgett J.S., Molineaux S.M.;
RT   "The structure and complete nucleotide sequence of the murine gene encoding
RT   interleukin-1 beta converting enzyme (ICE).";
RL   Genomics 20:474-481(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [5]
RP   CHARACTERIZATION.
RC   STRAIN=C3H/An;
RX   PubMed=9038361; DOI=10.1016/s0014-5793(97)00026-4;
RA   van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
RA   van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
RA   Fiers W.;
RT   "Characterization of seven murine caspase family members.";
RL   FEBS Lett. 403:61-69(1997).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE,
RP   ACTIVE SITE, AND MUTAGENESIS OF ASP-103; ASP-122; CYS-284;
RP   296-ASP--ASP-314; ASP-296 AND 313-ASP-ASP-314.
RX   PubMed=21147462; DOI=10.1016/j.chom.2010.11.007;
RA   Broz P., von Moltke J., Jones J.W., Vance R.E., Monack D.M.;
RT   "Differential requirement for Caspase-1 autoproteolysis in pathogen-induced
RT   cell death and cytokine processing.";
RL   Cell Host Microbe 8:471-483(2010).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-343, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
RA   Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J., Fang R.,
RA   Meng G., Su X., Jiang Z.;
RT   "Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to
RT   regulate responses to DNA virus infection.";
RL   Immunity 46:393-404(2017).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH SERPINB1A; SERPINB1B AND SERPINB1C.
RX   PubMed=30692621; DOI=10.1038/s41590-018-0303-z;
RA   Choi Y.J., Kim S., Choi Y., Nielsen T.B., Yan J., Lu A., Ruan J., Lee H.R.,
RA   Wu H., Spellberg B., Jung J.U.;
RT   "SERPINB1-mediated checkpoint of inflammatory caspase activation.";
RL   Nat. Immunol. 20:276-287(2019).
RN   [11]
RP   FUNCTION, SUBUNIT, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
RP   102-GLU--ASP-122 AND ILE-316.
RX   PubMed=32109412; DOI=10.1016/j.cell.2020.02.002;
RA   Wang K., Sun Q., Zhong X., Zeng M., Zeng H., Shi X., Li Z., Wang Y.,
RA   Zhao Q., Shao F., Ding J.;
RT   "Structural mechanism for GSDMD targeting by autoprocessed caspases in
RT   pyroptosis.";
RL   Cell 180:941-955(2020).
RN   [12]
RP   IDENTIFICATION IN THE AIM2 PANOPTOSOME COMPLEX.
RX   PubMed=34471287; DOI=10.1038/s41586-021-03875-8;
RA   Lee S., Karki R., Wang Y., Nguyen L.N., Kalathur R.C., Kanneganti T.D.;
RT   "AIM2 forms a complex with pyrin and ZBP1 to drive PANoptosis and host
RT   defence.";
RL   Nature 597:415-419(2021).
CC   -!- FUNCTION: Thiol protease involved in a variety of inflammatory
CC       processes by proteolytically cleaving other proteins, such as the
CC       precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and
CC       interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D
CC       (GSDMD), into active mature peptides (PubMed:21147462,
CC       PubMed:32109412). Plays a key role in cell immunity as an inflammatory
CC       response initiator: once activated through formation of an inflammasome
CC       complex, it initiates a pro-inflammatory response through the cleavage
CC       of the two inflammatory cytokines IL1B and IL18, releasing the mature
CC       cytokines which are involved in a variety of inflammatory processes
CC       (PubMed:21147462). Cleaves a tetrapeptide after an Asp residue at
CC       position P1 (PubMed:21147462). Also initiates pyroptosis, a programmed
CC       lytic cell death pathway, through cleavage of GSDMD (PubMed:32109412).
CC       In contrast to cleavage of interleukins IL1B and IL1B, recognition and
CC       cleavage of GSDMD is not strictly dependent on the consensus cleavage
CC       site but depends on an exosite interface on CASP1 that recognizes and
CC       binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32109412).
CC       Upon inflammasome activation, during DNA virus infection but not RNA
CC       virus challenge, controls antiviral immunity through the cleavage of
CC       CGAS, rendering it inactive (PubMed:28314590). In apoptotic cells,
CC       cleaves SPHK2 which is released from cells and remains enzymatically
CC       active extracellularly (By similarity). {ECO:0000250|UniProtKB:P29466,
CC       ECO:0000269|PubMed:21147462, ECO:0000269|PubMed:28314590,
CC       ECO:0000269|PubMed:32109412}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Strict requirement for an Asp residue at position P1 and has a
CC         preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.; EC=3.4.22.36;
CC         Evidence={ECO:0000269|PubMed:21147462};
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC       heterodimers, each one formed by a 20 kDa (Caspase-1 subunit p20) and a
CC       10 kDa (Caspase-1 subunit p10) subunit (PubMed:32109412). May be a
CC       component of the inflammasome, a protein complex which also includes
CC       PYCARD, CARD8 and NLRP2 and whose function would be the activation of
CC       pro-inflammatory caspases (By similarity). Component of the AIM2
CC       PANoptosome complex, a multiprotein complex that drives inflammatory
CC       cell death (PANoptosis) (PubMed:34471287). Both the p10 and p20
CC       subunits interact with MEFV (By similarity). Interacts with CARD17/INCA
CC       and CARD18 (By similarity). Interacts with SERPINB1; this interaction
CC       regulates CASP1 activity (By similarity).
CC       {ECO:0000250|UniProtKB:P29466, ECO:0000269|PubMed:32109412,
CC       ECO:0000269|PubMed:34471287}.
CC   -!- SUBUNIT: [Caspase-1 subunit p20]: Heterotetramer that consists of two
CC       anti-parallel arranged heterodimers, each one formed by a 20 kDa
CC       (Caspase-1 subunit p20) and a 10 kDa (Caspase-1 subunit p10) subunit.
CC       {ECO:0000269|PubMed:32109412}.
CC   -!- SUBUNIT: [Caspase-1 subunit p10]: Heterotetramer that consists of two
CC       anti-parallel arranged heterodimers, each one formed by a 20 kDa
CC       (Caspase-1 subunit p20) and a 10 kDa (Caspase-1 subunit p10) subunit.
CC       {ECO:0000269|PubMed:32109412}.
CC   -!- INTERACTION:
CC       P29452; Q3UP24: Nlrc4; NbExp=2; IntAct=EBI-489700, EBI-16006652;
CC       P29452; Q9EPB4: Pycard; NbExp=2; IntAct=EBI-489700, EBI-6253348;
CC       P29452; P18011: ipaB; Xeno; NbExp=3; IntAct=EBI-489700, EBI-490239;
CC       P29452; Q56134: sipB; Xeno; NbExp=2; IntAct=EBI-489700, EBI-489689;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21147462}. Cell
CC       membrane {ECO:0000250|UniProtKB:P29466}.
CC   -!- TISSUE SPECIFICITY: High level expression seen in spleen and lung, low
CC       level expression seen in brain, heart, liver, kidney, testis and
CC       skeletal muscle. {ECO:0000269|PubMed:1431103}.
CC   -!- PTM: The two subunits are derived from the precursor sequence by an
CC       autocatalytic mechanism. {ECO:0000269|PubMed:21147462,
CC       ECO:0000269|PubMed:32109412}.
CC   -!- PTM: Ubiquitinated via 'Lys-11'-linked polyubiquitination.
CC       Deubiquitinated by USP8. {ECO:0000250|UniProtKB:P29466}.
CC   -!- DISRUPTION PHENOTYPE: Mutants are resitant to vaccinia virus (VACV) but
CC       not vesicular somatitis virus (VSV) infection. They show lower viral
CC       loads in the lungs compared to wild type mice, they produce higher
CC       levels of type I IFN, IL6 and RSAD2/Viperin after VCAV INFECTION.
CC       {ECO:0000269|PubMed:28314590}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR   EMBL; L03799; AAA39306.1; -; mRNA.
DR   EMBL; L28095; AAA20209.1; -; mRNA.
DR   EMBL; U04269; AAA56992.1; -; Genomic_DNA.
DR   EMBL; BC008152; AAH08152.1; -; mRNA.
DR   CCDS; CCDS22798.1; -.
DR   PIR; A46495; A46495.
DR   RefSeq; NP_033937.2; NM_009807.2.
DR   AlphaFoldDB; P29452; -.
DR   SMR; P29452; -.
DR   BioGRID; 198492; 4.
DR   ComplexPortal; CPX-4241; NLRP3 inflammasome.
DR   ComplexPortal; CPX-4242; Caspase-1 complex.
DR   ComplexPortal; CPX-4243; AIM2 inflammasome.
DR   ComplexPortal; CPX-4244; Pyrin inflammasome.
DR   ComplexPortal; CPX-4261; NLRP1b inflammasome, allele-1 variant.
DR   ComplexPortal; CPX-4266; NLRP1b inflammasome, allele-2 variant.
DR   ComplexPortal; CPX-4269; NLRP1b inflammasome, allele-3 variant.
DR   ComplexPortal; CPX-4270; NLRP1b inflammasome, allele-5 variant.
DR   ComplexPortal; CPX-4271; NLRP1a inflammasome.
DR   CORUM; P29452; -.
DR   DIP; DIP-34659N; -.
DR   IntAct; P29452; 7.
DR   MINT; P29452; -.
DR   STRING; 10090.ENSMUSP00000027015; -.
DR   BindingDB; P29452; -.
DR   ChEMBL; CHEMBL4800; -.
DR   MEROPS; C14.001; -.
DR   iPTMnet; P29452; -.
DR   PhosphoSitePlus; P29452; -.
DR   SwissPalm; P29452; -.
DR   EPD; P29452; -.
DR   MaxQB; P29452; -.
DR   PaxDb; P29452; -.
DR   PeptideAtlas; P29452; -.
DR   PRIDE; P29452; -.
DR   ProteomicsDB; 279913; -.
DR   Antibodypedia; 1075; 1138 antibodies from 47 providers.
DR   DNASU; 12362; -.
DR   Ensembl; ENSMUST00000027015; ENSMUSP00000027015; ENSMUSG00000025888.
DR   GeneID; 12362; -.
DR   KEGG; mmu:12362; -.
DR   UCSC; uc009obr.1; mouse.
DR   CTD; 834; -.
DR   MGI; MGI:96544; Casp1.
DR   VEuPathDB; HostDB:ENSMUSG00000025888; -.
DR   eggNOG; KOG3573; Eukaryota.
DR   GeneTree; ENSGT00940000159114; -.
DR   HOGENOM; CLU_036904_0_1_1; -.
DR   InParanoid; P29452; -.
DR   OMA; NTENCKA; -.
DR   OrthoDB; 1327703at2759; -.
DR   PhylomeDB; P29452; -.
DR   TreeFam; TF102023; -.
DR   BRENDA; 3.4.22.36; 3474.
DR   Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-MMU-448706; Interleukin-1 processing.
DR   Reactome; R-MMU-5620971; Pyroptosis.
DR   BioGRID-ORCS; 12362; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Casp1; mouse.
DR   PRO; PR:P29452; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P29452; protein.
DR   Bgee; ENSMUSG00000025888; Expressed in paneth cell and 115 other tissues.
DR   ExpressionAtlas; P29452; baseline and differential.
DR   Genevisible; P29452; MM.
DR   GO; GO:0097169; C:AIM2 inflammasome complex; ISS:UniProtKB.
DR   GO; GO:0008303; C:caspase complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0061702; C:inflammasome complex; ISO:MGI.
DR   GO; GO:0072557; C:IPAF inflammasome complex; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IC:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0072558; C:NLRP1 inflammasome complex; ISS:UniProtKB.
DR   GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097179; C:protease inhibitor complex; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0071310; P:cellular response to organic substance; ISO:MGI.
DR   GO; GO:0140447; P:cytokine precursor processing; ISO:MGI.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:ARUK-UCL.
DR   GO; GO:0051607; P:defense response to virus; IC:ComplexPortal.
DR   GO; GO:0060081; P:membrane hyperpolarization; IMP:MGI.
DR   GO; GO:0007613; P:memory; ISO:MGI.
DR   GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR   GO; GO:0051882; P:mitochondrial depolarization; IMP:MGI.
DR   GO; GO:0007520; P:myoblast fusion; ISO:MGI.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IC:ComplexPortal.
DR   GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA:ComplexPortal.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; ISO:MGI.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IDA:ComplexPortal.
DR   GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IMP:MGI.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:ComplexPortal.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:ComplexPortal.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:ComplexPortal.
DR   GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0097300; P:programmed necrotic cell death; IDA:MGI.
DR   GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0070269; P:pyroptosis; IDA:ComplexPortal.
DR   GO; GO:0010506; P:regulation of autophagy; IMP:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0033198; P:response to ATP; IMP:MGI.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0140448; P:signaling receptor ligand precursor processing; ISO:MGI.
DR   GO; GO:1901998; P:toxin transport; IMP:MGI.
DR   CDD; cd00032; CASc; 1.
DR   Gene3D; 1.10.533.10; -; 1.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR002398; Pept_C14.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR10454; PTHR10454; 1.
DR   Pfam; PF00619; CARD; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00114; CARD; 1.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF52129; SSF52129; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Cell membrane; Cytoplasm; Hydrolase; Membrane; Methylation;
KW   Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation; Zymogen.
FT   PROPEP          1..?118
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004525"
FT   CHAIN           ?119..296
FT                   /note="Caspase-1 subunit p20"
FT                   /evidence="ECO:0000305|PubMed:32109412"
FT                   /id="PRO_0000004526"
FT   PROPEP          297..314
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004527"
FT   CHAIN           315..402
FT                   /note="Caspase-1 subunit p10"
FT                   /evidence="ECO:0000305|PubMed:32109412"
FT                   /id="PRO_0000004528"
FT   DOMAIN          1..91
FT                   /note="CARD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT   REGION          98..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000305|PubMed:21147462"
FT   SITE            103..104
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000305|PubMed:21147462"
FT   SITE            122..123
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000305|PubMed:21147462"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         343
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MUTAGEN         102..122
FT                   /note="EDSKGGHPSSSETKEEQNKED->AASKGGHPSSSATKAAQNKAA:
FT                   Prevents autoprocessing."
FT                   /evidence="ECO:0000269|PubMed:32109412"
FT   MUTAGEN         103
FT                   /note="D->N: In C71 mutant; abolished cleavage and ability
FT                   to generate caspase-1 subunits; abolished ability to
FT                   process inflammatory cytokine interleukin-1 beta (IL1B) and
FT                   ability to induce programmed cell death; when associated
FT                   with N-122 and 296-N--N-314."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         122
FT                   /note="D->N: In C71 mutant; abolished cleavage and ability
FT                   to generate caspase-1 subunits; abolished ability to
FT                   process inflammatory cytokine interleukin-1 beta (IL1B) and
FT                   ability to induce programmed cell death; when associated
FT                   with N-103 and 296-N--N-314."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         284
FT                   /note="C->A: Loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         296..314
FT                   /note="DSVRDSEEDFLTDAIFEDD->NSVRDSEEDFLTNAIFENN: In C71
FT                   mutant; abolished cleavage and ability to generate caspase-
FT                   1 subunits; abolished ability to process inflammatory
FT                   cytokine interleukin-1 beta (IL1B) and ability to induce
FT                   programmed cell death; when associated with N-103 and N-
FT                   122."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         296..314
FT                   /note="DSVRDSEEDFLTDAIFEDD->NSVRNSEENFLTNAIFENN: In C60
FT                   mutant; impaired cleavage and ability to generate caspase-1
FT                   subunits p10 and p20; abolished ability to process
FT                   inflammatory cytokine interleukin-1 beta (IL1B) without
FT                   affecting ability to induce programmed cell death."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         296
FT                   /note="D->N: In C47 mutant; does not affect ability to
FT                   mediate inflammatory response; when associated with 313-N-
FT                   N-314."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         313..314
FT                   /note="DD->NN: In C47 mutant; does not affect ability to
FT                   mediate inflammatory response and cell death; when
FT                   associated with N-296."
FT                   /evidence="ECO:0000269|PubMed:21147462"
FT   MUTAGEN         316
FT                   /note="I->N: Mediates autoprocessing but are unable to
FT                   mediate cleavage of Gasdermin-D (GSDMD)."
FT                   /evidence="ECO:0000269|PubMed:32109412"
FT   CONFLICT        3..6
FT                   /note="DKIL -> V (in Ref. 3; AAA56992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  45640 MW;  3BEBCEFA67C69B03 CRC64;
     MADKILRAKR KQFINSVSIG TINGLLDELL EKRVLNQEEM DKIKLANITA MDKARDLCDH
     VSKKGPQASQ IFITYICNED CYLAGILELQ SAPSAETFVA TEDSKGGHPS SSETKEEQNK
     EDGTFPGLTG TLKFCPLEKA QKLWKENPSE IYPIMNTTTR TRLALIICNT EFQHLSPRVG
     AQVDLREMKL LLEDLGYTVK VKENLTALEM VKEVKEFAAC PEHKTSDSTF LVFMSHGIQE
     GICGTTYSNE VSDILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVRD
     SEEDFLTDAI FEDDGIKKAH IEKDFIAFCS STPDNVSWRH PVRGSLFIES LIKHMKEYAW
     SCDLEDIFRK VRFSFEQPEF RLQMPTADRV TLTKRFYLFP GH
 
 
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