ID CASP1_HUMAN Reviewed; 404 AA.
AC P29466; B5MDZ1; Q53EY6; Q6DMQ1; Q6GSS3; Q6PI75; Q9UCN3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 01-MAY-2013, entry version 153.
DE RecName: Full=Caspase-1;
DE Short=CASP-1;
DE EC=3.4.22.36;
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;
DE Contains:
DE RecName: Full=Caspase-1 subunit p10;
DE Flags: Precursor;
GN Name=CASP1; Synonyms=IL1BC, IL1BCE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PARTIAL PROTEIN SEQUENCE,
RP AND ACTIVE SITE.
RX PubMed=1574116; DOI=10.1038/356768a0;
RA Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D.,
RA Kostura M.J., Miller D.K., Molineaux S.M., Weidner J.R., Aunins J.,
RA Elliston K.O., Ayala J.M., Casano F.J., Chin J., Ding G.J.-F.,
RA Egger L.A., Gaffney E.P., Limjuco G., Palyha O.C., Raju M.,
RA Rolando A.M., Salley J.P., Yamin T.-T., Lee T.D., Shively J.E.,
RA McCross M., Mumford R.A., Schmidt J.A., Tocci M.J.;
RT "A novel heterodimeric cysteine protease is required for interleukin-1
RT beta processing in monocytes.";
RL Nature 356:768-774(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND PROTEIN SEQUENCE OF
RP 120-142.
RX PubMed=1373520; DOI=10.1126/science.1373520;
RA Cerretti D.P., Kozlosky C.J., Mosley B., Nelson N., van Ness K.,
RA Greenstreet T.A., March C.J., Kronheim S.R., Druck T.,
RA Cannizzaro L.A., Huebner K., Black R.A.;
RT "Molecular cloning of the interleukin-1 beta converting enzyme.";
RL Science 256:97-100(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; DELTA; EPSILON AND GAMMA),
RP ALTERNATIVE SPLICING, AND FUNCTION.
RX PubMed=7876192; DOI=10.1074/jbc.270.9.4312;
RA Alnemri E.S., Fernandes-Alnemri T., Litwack G.;
RT "Cloning and expression of four novel isoforms of human interleukin-1
RT beta converting enzyme with different apoptotic activities.";
RL J. Biol. Chem. 270:4312-4317(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 4-404 (ISOFORM BETA).
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-404 (ISOFORM ALPHA), FUNCTION,
RP MUTAGENESIS OF CYS-285, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=15498465; DOI=10.1016/j.ygeno.2004.06.005;
RA Feng Q., Li P., Leung P.C.K., Auersperg N.;
RT "Caspase-1 zeta, a new splice variant of caspase-1 gene.";
RL Genomics 84:587-591(2004).
RN [8]
RP PROTEIN SEQUENCE OF 120-142.
RX PubMed=1321594; DOI=10.1016/0003-9861(92)90629-B;
RA Kronheim S.R., Mumma A., Greenstreet T., Glackin P.J., Van Ness K.,
RA March C.J., Black R.A.;
RT "Purification of interleukin-1 beta converting enzyme, the protease
RT that cleaves the interleukin-1 beta precursor.";
RL Arch. Biochem. Biophys. 296:698-703(1992).
RN [9]
RP INTERACTION WITH CARD18.
RX PubMed=11051551; DOI=10.1016/S0092-8674(00)00108-2;
RA Humke E.W., Shriver S.K., Starovasnik M.A., Fairbrother W.J.,
RA Dixit V.M.;
RT "ICEBERG: a novel inhibitor of interleukin-1beta generation.";
RL Cell 103:99-111(2000).
RN [10]
RP COMPONENT OF THE INFLAMMASOME.
RX PubMed=15030775; DOI=10.1016/S1074-7613(04)00046-9;
RA Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N.,
RA Tschopp J.;
RT "NALP3 forms an IL-1beta-processing inflammasome with increased
RT activity in Muckle-Wells autoinflammatory disorder.";
RL Immunity 20:319-325(2004).
RN [11]
RP INTERACTION WITH CARD17.
RX PubMed=15383541; DOI=10.1074/jbc.M407891200;
RA Lamkanfi M., Denecker G., Kalai M., D'hondt K., Meeus A., Declercq W.,
RA Saelens X., Vandenabeele P.;
RT "INCA, a novel human caspase recruitment domain protein that inhibits
RT interleukin-1beta generation.";
RL J. Biol. Chem. 279:51729-51738(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=8044845; DOI=10.1016/0092-8674(94)90303-4;
RA Walker N.P.C., Talanian R.V., Brady K.D., Dang L.C., Bump N.J.,
RA Ferenz C.R., Franklin S., Ghayur T., Hackett M.C., Hammill L.D.,
RA Herzog L., Hugunin M., Houy W., Mankovich J.A., McGuiness L.,
RA Orlewicz E., Paskind M., Pratt C.A., Reis P., Summani A.,
RA Terranova M., Welch J.P., Xiong L., Moeller A., Tracey D.E., Kamen R.,
RA Wong W.W.;
RT "Crystal structure of the cysteine protease interleukin-1 beta-
RT converting enzyme: a (p20/p10)2 homodimer.";
RL Cell 78:343-352(1994).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS).
RX PubMed=9190289; DOI=10.1016/S1074-5521(97)90258-1;
RA Rano T.A., Timkey T., Peterson E.P., Rotonda J., Nicholson D.W.,
RA Becker J.W., Chapman K.T., Thornberry N.A.;
RT "A combinatorial approach for determining protease specificities:
RT application to interleukin-1beta converting enzyme (ICE).";
RL Chem. Biol. 4:149-155(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=9987822;
RA Okamoto Y., Anan H., Nakai E., Morihira K., Yonetoku Y., Kurihara H.,
RA Sakashita H., Terai Y., Takeuchi M., Shibanuma T., Isomura Y.;
RT "Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors:
RT synthesis, structure activity relationships and crystallographic study
RT of the ICE-inhibitor complex.";
RL Chem. Pharm. Bull. 47:11-21(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 120-404 OF MUTANT ALA-285.
RX PubMed=15296730; DOI=10.1016/j.str.2004.05.010;
RA Romanowski M.J., Scheer J.M., O'Brien T., McDowell R.S.;
RT "Crystal structures of a ligand-free and malonate-bound human caspase-
RT 1: implications for the mechanism of substrate binding.";
RL Structure 12:1361-1371(2004).
CC -!- FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and
CC an Ala, releasing the mature cytokine which is involved in a
CC variety of inflammatory processes. Important for defense against
CC pathogens. Cleaves and activates sterol regulatory element binding
CC proteins (SREBPs). Can also promote apoptosis.
CC -!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
CC position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-
CC Asp-|-.
CC -!- ENZYME REGULATION: Specifically inhibited by the cowpox virus Crma
CC protein.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel
CC arranged heterodimers, each one formed by a 20 kDa (p20) and a 10
CC kDa (p10) subunit. The p20 subunit can also form a heterodimer
CC with the epsilon isoform which then has an inhibitory effect. May
CC be a component of the inflammasome, a protein complex which also
CC includes PYCARD, CARD8 and NALP2 and whose function would be the
CC activation of proinflammatory caspases. Interacts with CARD17/INCA
CC and CARD18.
CC -!- INTERACTION:
CC P09038:FGF2; NbExp=2; IntAct=EBI-516667, EBI-977447;
CC P01583:IL1A; NbExp=3; IntAct=EBI-516667, EBI-1749782;
CC Q9NPP4:NLRC4; NbExp=4; IntAct=EBI-516667, EBI-1222527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist;
CC Name=Alpha;
CC IsoId=P29466-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P29466-2; Sequence=VSP_000798;
CC Name=Gamma;
CC IsoId=P29466-3; Sequence=VSP_000799;
CC Name=Delta;
CC IsoId=P29466-4; Sequence=VSP_000799, VSP_000800;
CC Note=Apoptosis inactive;
CC Name=Epsilon;
CC IsoId=P29466-5; Sequence=VSP_000797;
CC Note=Apoptosis inactive;
CC -!- TISSUE SPECIFICITY: Expressed in larger amounts in spleen and
CC lung. Detected in liver, heart, small intestine, colon, thymus,
CC prostate, skeletal muscle, peripheral blood leukocytes, kidney and
CC testis. No expression in the brain.
CC -!- PTM: The two subunits are derived from the precursor sequence by
CC an autocatalytic mechanism.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC -!- SIMILARITY: Contains 1 CARD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT72297.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAT72297.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CASP1ID145ch11q22.html";
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DR EMBL; X65019; CAA46153.1; -; mRNA.
DR EMBL; M87507; AAA66942.1; -; mRNA.
DR EMBL; U13697; AAC50107.1; -; mRNA.
DR EMBL; U13698; AAC50108.1; -; mRNA.
DR EMBL; U13699; AAC50109.1; -; mRNA.
DR EMBL; U13700; AAC50110.1; -; mRNA.
DR EMBL; AK223503; BAD97223.1; -; mRNA.
DR EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041689; AAH41689.1; -; mRNA.
DR EMBL; BC062327; AAH62327.1; -; mRNA.
DR EMBL; AY660536; AAT72297.1; ALT_SEQ; mRNA.
DR IPI; IPI00021800; -.
DR IPI; IPI00219307; -.
DR IPI; IPI00219308; -.
DR IPI; IPI00219309; -.
DR IPI; IPI00219310; -.
DR PIR; A54263; A42677.
DR PIR; A56084; A56084.
DR PIR; B56084; B56084.
DR PIR; C56084; C56084.
DR PIR; D56084; D56084.
DR RefSeq; NP_001214.1; NM_001223.4.
DR RefSeq; NP_001244047.1; NM_001257118.1.
DR RefSeq; NP_001244048.1; NM_001257119.1.
DR RefSeq; NP_150634.1; NM_033292.3.
DR RefSeq; NP_150635.1; NM_033293.3.
DR RefSeq; NP_150636.1; NM_033294.3.
DR RefSeq; NP_150637.1; NM_033295.3.
DR UniGene; Hs.2490; -.
DR PDB; 1BMQ; X-ray; 2.50 A; A=131-297, B=317-404.
DR PDB; 1IBC; X-ray; 2.73 A; A=104-297, B=317-404.
DR PDB; 1ICE; X-ray; 2.60 A; A=131-297, B=317-404.
DR PDB; 1RWK; X-ray; 2.30 A; A=120-297, B=317-404.
DR PDB; 1RWM; X-ray; 2.70 A; A=120-297, B=317-404.
DR PDB; 1RWN; X-ray; 2.00 A; A=120-297, B=317-404.
DR PDB; 1RWO; X-ray; 2.10 A; A=120-297, B=317-404.
DR PDB; 1RWP; X-ray; 2.20 A; A=120-297, B=317-404.
DR PDB; 1RWV; X-ray; 2.10 A; A=120-297, B=317-404.
DR PDB; 1RWW; X-ray; 2.80 A; A=120-297, B=317-404.
DR PDB; 1RWX; X-ray; 1.85 A; A=120-297, B=317-404.
DR PDB; 1SC1; X-ray; 2.60 A; A=120-297, B=317-404.
DR PDB; 1SC3; X-ray; 1.80 A; A=120-297, B=317-404.
DR PDB; 1SC4; X-ray; 2.10 A; A=120-297, B=317-404.
DR PDB; 2FQQ; X-ray; 3.30 A; A=120-297, B=317-404.
DR PDB; 2H48; X-ray; 2.20 A; A=120-297, B=317-404.
DR PDB; 2H4W; X-ray; 2.00 A; A=120-297, B=317-404.
DR PDB; 2H4Y; X-ray; 1.90 A; A=120-297, B=317-404.
DR PDB; 2H51; X-ray; 2.10 A; A=120-297, B=317-404.
DR PDB; 2H54; X-ray; 1.80 A; A=120-297, B=317-404.
DR PDB; 2HBQ; X-ray; 1.80 A; A=120-297, B=317-404.
DR PDB; 2HBR; X-ray; 2.20 A; A=120-297, B=317-404.
DR PDB; 2HBY; X-ray; 2.10 A; A=120-297, B=317-404.
DR PDB; 2HBZ; X-ray; 1.90 A; A=120-297, B=317-404.
DR PDB; 3D6F; X-ray; 1.90 A; A=120-297, B=317-404.
DR PDB; 3D6H; X-ray; 2.00 A; A=120-297, B=317-404.
DR PDB; 3D6M; X-ray; 1.80 A; A=120-297, B=317-404.
DR PDB; 3E4C; X-ray; 2.05 A; A/B=104-404.
DR PDB; 3NS7; X-ray; 2.60 A; A=136-297, B=317-404.
DR PDBsum; 1BMQ; -.
DR PDBsum; 1IBC; -.
DR PDBsum; 1ICE; -.
DR PDBsum; 1RWK; -.
DR PDBsum; 1RWM; -.
DR PDBsum; 1RWN; -.
DR PDBsum; 1RWO; -.
DR PDBsum; 1RWP; -.
DR PDBsum; 1RWV; -.
DR PDBsum; 1RWW; -.
DR PDBsum; 1RWX; -.
DR PDBsum; 1SC1; -.
DR PDBsum; 1SC3; -.
DR PDBsum; 1SC4; -.
DR PDBsum; 2FQQ; -.
DR PDBsum; 2H48; -.
DR PDBsum; 2H4W; -.
DR PDBsum; 2H4Y; -.
DR PDBsum; 2H51; -.
DR PDBsum; 2H54; -.
DR PDBsum; 2HBQ; -.
DR PDBsum; 2HBR; -.
DR PDBsum; 2HBY; -.
DR PDBsum; 2HBZ; -.
DR PDBsum; 3D6F; -.
DR PDBsum; 3D6H; -.
DR PDBsum; 3D6M; -.
DR PDBsum; 3E4C; -.
DR PDBsum; 3NS7; -.
DR ProteinModelPortal; P29466; -.
DR DIP; DIP-175N; -.
DR IntAct; P29466; 6.
DR MINT; MINT-201196; -.
DR STRING; 9606.ENSP00000410076; -.
DR MEROPS; C14.001; -.
DR PhosphoSite; P29466; -.
DR DMDM; 266321; -.
DR PaxDb; P29466; -.
DR PRIDE; P29466; -.
DR DNASU; 834; -.
DR Ensembl; ENST00000353247; ENSP00000344132; ENSG00000137752.
DR Ensembl; ENST00000393136; ENSP00000376844; ENSG00000137752.
DR Ensembl; ENST00000415981; ENSP00000408446; ENSG00000137752.
DR Ensembl; ENST00000436863; ENSP00000410076; ENSG00000137752.
DR Ensembl; ENST00000446369; ENSP00000403260; ENSG00000137752.
DR Ensembl; ENST00000525825; ENSP00000434779; ENSG00000137752.
DR Ensembl; ENST00000526568; ENSP00000434250; ENSG00000137752.
DR Ensembl; ENST00000531166; ENSP00000434303; ENSG00000137752.
DR Ensembl; ENST00000533400; ENSP00000433138; ENSG00000137752.
DR Ensembl; ENST00000534497; ENSP00000436875; ENSG00000137752.
DR Ensembl; ENST00000593315; ENSP00000469724; ENSG00000137752.
DR Ensembl; ENST00000594519; ENSP00000472457; ENSG00000137752.
DR Ensembl; ENST00000598974; ENSP00000470811; ENSG00000137752.
DR GeneID; 834; -.
DR KEGG; hsa:834; -.
DR UCSC; uc001pig.3; human.
DR UCSC; uc001pim.4; human.
DR UCSC; uc009yxi.3; human.
DR UCSC; uc010rvh.2; human.
DR UCSC; uc010rvi.2; human.
DR CTD; 834; -.
DR GeneCards; GC11M104898; -.
DR HGNC; HGNC:1499; CASP1.
DR HPA; CAB002685; -.
DR HPA; HPA003056; -.
DR MIM; 147678; gene.
DR neXtProt; NX_P29466; -.
DR PharmGKB; PA26083; -.
DR eggNOG; NOG274219; -.
DR HOVERGEN; HBG076981; -.
DR InParanoid; P29466; -.
DR KO; K01370; -.
DR OMA; KSAEIYP; -.
DR OrthoDB; EOG49W2FS; -.
DR PhylomeDB; P29466; -.
DR BRENDA; 3.4.22.36; 2681.
DR Pathway_Interaction_DB; caspase_pathway; Caspase cascade in apoptosis.
DR Pathway_Interaction_DB; anthraxpathway; Cellular roles of Anthrax toxin.
DR Pathway_Interaction_DB; ifngpathway; IFN-gamma pathway.
DR Pathway_Interaction_DB; il1pathway; IL1-mediated signaling events.
DR Reactome; REACT_6900; Immune System.
DR SABIO-RK; P29466; -.
DR BindingDB; P29466; -.
DR ChEMBL; CHEMBL4801; -.
DR ChiTaRS; CASP1; human.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB00859; Penicillamine.
DR EvolutionaryTrace; P29466; -.
DR GenomeRNAi; 834; -.
DR NextBio; 3460; -.
DR PMAP-CutDB; P29466; -.
DR ArrayExpress; P29466; -.
DR Bgee; P29466; -.
DR CleanEx; HS_CASP1; -.
DR Genevestigator; P29466; -.
DR GermOnline; ENSG00000137752; Homo sapiens.
DR GO; GO:0097169; C:AIM2 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:Compara.
DR GO; GO:0072557; C:IPAF inflammasome complex; ISS:UniProtKB.
DR GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; TAS:ProtInc.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0006917; P:induction of apoptosis; IEA:Compara.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0032611; P:interleukin-1 beta production; IEA:Compara.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEP:UniProtKB.
DR GO; GO:0050717; P:positive regulation of interleukin-1 alpha secretion; IEA:Compara.
DR GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Compara.
DR GO; GO:0016485; P:protein processing; IEA:Compara.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0033198; P:response to ATP; IEA:Compara.
DR GO; GO:0001666; P:response to hypoxia; IEA:Compara.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR017350; Caspase_IL-1_beta.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR011600; Pept_C14_cat.
DR InterPro; IPR001309; Pept_C14_ICE_p20.
DR InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR002398; Pept_C14_p45.
DR InterPro; IPR015917; Pept_C14_p45_core.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PIRSF; PIRSF038001; Caspase_ICE; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF47986; DEATH_like; 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 3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Polymorphism;
KW Protease; Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1 119
FT /FTId=PRO_0000004521.
FT CHAIN 120 297 Caspase-1 subunit p20.
FT /FTId=PRO_0000004522.
FT PROPEP 298 316
FT /FTId=PRO_0000004523.
FT CHAIN 317 404 Caspase-1 subunit p10.
FT /FTId=PRO_0000004524.
FT DOMAIN 1 91 CARD.
FT ACT_SITE 237 237
FT ACT_SITE 285 285
FT VAR_SEQ 20 335 Missing (in isoform Epsilon).
FT /FTId=VSP_000797.
FT VAR_SEQ 20 112 Missing (in isoform Gamma and isoform
FT Delta).
FT /FTId=VSP_000799.
FT VAR_SEQ 92 112 Missing (in isoform Beta).
FT /FTId=VSP_000798.
FT VAR_SEQ 288 335 Missing (in isoform Delta).
FT /FTId=VSP_000800.
FT VARIANT 15 15 R -> H (in dbSNP:rs1042743).
FT /FTId=VAR_048615.
FT MUTAGEN 285 285 C->A,S: Loss of activity.
FT CONFLICT 319 319 K -> R (in Ref. 4; BAD97223).
FT CONFLICT 402 402 P -> L (in Ref. 4; BAD97223).
FT TURN 129 132
FT HELIX 138 148
FT HELIX 149 151
FT TURN 158 160
FT STRAND 164 169
FT STRAND 174 176
FT HELIX 182 195
FT STRAND 199 205
FT HELIX 208 219
FT HELIX 222 226
FT STRAND 230 239
FT STRAND 242 244
FT STRAND 250 252
FT HELIX 258 264
FT TURN 267 269
FT HELIX 271 273
FT STRAND 278 285
FT STRAND 287 289
FT STRAND 291 298
FT HELIX 316 319
FT STRAND 326 332
FT STRAND 340 342
FT HELIX 348 360
FT TURN 361 363
FT HELIX 366 376
FT STRAND 388 390
SQ SEQUENCE 404 AA; 45159 MW; ABF33CF33CC71584 CRC64;
MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV MDKTRALIDS
VIPKGAQACQ ICITYICEED SYLAGTLGLS ADQTSGNYLN MQDSQGVLSS FPAPQAVQDN
PAMPTSSGSE GNVKLCSLEE AQRIWKQKSA EIYPIMDKSS RTRLALIICN EEFDSIPRRT
GAEVDITGMT MLLQNLGYSV DVKKNLTASD MTTELEAFAH RPEHKTSDST FLVFMSHGIR
EGICGKKHSE QVPDILQLNA IFNMLNTKNC PSLKDKPKVI IIQACRGDSP GVVWFKDSVG
VSGNLSLPTT EEFEDDAIKK AHIEKDFIAF CSSTPDNVSW RHPTMGSVFI GRLIEHMQEY
ACSCDVEEIF RKVRFSFEQP DGRAQMPTTE RVTLTRCFYL FPGH
//
