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Database: UniProt
Entry: P29466
LinkDB: P29466
Original site: P29466 
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   29-OCT-2014, entry version 169.
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   INTERACTION WITH MEFV.
RX   PubMed=16785446; DOI=10.1073/pnas.0602081103;
RA   Chae J.J., Wood G., Masters S.L., Richard K., Park G., Smith B.J.,
RA   Kastner D.L.;
RT   "The B30.2 domain of pyrin, the familial Mediterranean fever protein,
RT   interacts directly with caspase-1 to modulate IL-1beta production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9982-9987(2006).
RN   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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       {ECO:0000269|PubMed:15498465, ECO:0000269|PubMed:7876192}.
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. Both the p10 and p20
CC       subunits interact with MEFV. Interacts with CARD17/INCA and
CC       CARD18. {ECO:0000269|PubMed:11051551, ECO:0000269|PubMed:15383541,
CC       ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:8044845,
CC       ECO:0000269|PubMed:9987822}.
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. {ECO:0000269|PubMed:15498465}.
CC   -!- PTM: The two subunits are derived from the precursor sequence by
CC       an autocatalytic mechanism.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 CARD domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00046}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT72297.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAT72297.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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   CCDS; CCDS53704.1; -. [P29466-3]
DR   CCDS; CCDS8329.1; -. [P29466-2]
DR   CCDS; CCDS8330.1; -. [P29466-1]
DR   CCDS; CCDS8331.1; -. [P29466-4]
DR   CCDS; CCDS8332.1; -. [P29466-5]
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. [P29466-2]
DR   RefSeq; NP_001244047.1; NM_001257118.2. [P29466-1]
DR   RefSeq; NP_001244048.1; NM_001257119.2. [P29466-2]
DR   RefSeq; NP_150634.1; NM_033292.3. [P29466-1]
DR   RefSeq; NP_150635.1; NM_033293.3. [P29466-3]
DR   RefSeq; NP_150636.1; NM_033294.3. [P29466-4]
DR   RefSeq; NP_150637.1; NM_033295.3. [P29466-5]
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   SMR; P29466; 2-89, 125-404.
DR   BioGrid; 107284; 30.
DR   DIP; DIP-175N; -.
DR   IntAct; P29466; 6.
DR   MINT; MINT-201196; -.
DR   STRING; 9606.ENSP00000410076; -.
DR   BindingDB; P29466; -.
DR   ChEMBL; CHEMBL4801; -.
DR   DrugBank; DB01017; Minocycline.
DR   GuidetoPHARMACOLOGY; 1617; -.
DR   MEROPS; C14.001; -.
DR   PhosphoSite; P29466; -.
DR   DMDM; 266321; -.
DR   MaxQB; P29466; -.
DR   PaxDb; P29466; -.
DR   PRIDE; P29466; -.
DR   DNASU; 834; -.
DR   Ensembl; ENST00000353247; ENSP00000344132; ENSG00000137752. [P29466-5]
DR   Ensembl; ENST00000436863; ENSP00000410076; ENSG00000137752. [P29466-1]
DR   Ensembl; ENST00000446369; ENSP00000403260; ENSG00000137752. [P29466-4]
DR   Ensembl; ENST00000525825; ENSP00000434779; ENSG00000137752. [P29466-2]
DR   Ensembl; ENST00000526568; ENSP00000434250; ENSG00000137752. [P29466-3]
DR   Ensembl; ENST00000531166; ENSP00000434303; ENSG00000137752. [P29466-5]
DR   Ensembl; ENST00000533400; ENSP00000433138; ENSG00000137752. [P29466-1]
DR   Ensembl; ENST00000534497; ENSP00000436875; ENSG00000137752. [P29466-4]
DR   GeneID; 834; -.
DR   KEGG; hsa:834; -.
DR   UCSC; uc001pig.4; human. [P29466-3]
DR   UCSC; uc001pim.5; human. [P29466-1]
DR   UCSC; uc009yxi.4; human. [P29466-2]
DR   UCSC; uc021qpr.2; human. [P29466-4]
DR   UCSC; uc021qps.2; human. [P29466-5]
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   GeneTree; ENSGT00760000118912; -.
DR   HOVERGEN; HBG076981; -.
DR   InParanoid; P29466; -.
DR   KO; K01370; -.
DR   OMA; KSAEIYP; -.
DR   PhylomeDB; P29466; -.
DR   TreeFam; TF102023; -.
DR   BRENDA; 3.4.22.36; 2681.
DR   Reactome; REACT_23950; Interleukin-1 processing.
DR   Reactome; REACT_75776; NOD1/2 Signaling Pathway.
DR   Reactome; REACT_75777; The AIM2 inflammasome.
DR   Reactome; REACT_75808; The NLRP3 inflammasome.
DR   Reactome; REACT_75892; The IPAF inflammasome.
DR   SABIO-RK; P29466; -.
DR   SignaLink; P29466; -.
DR   ChiTaRS; CASP1; human.
DR   EvolutionaryTrace; P29466; -.
DR   GeneWiki; Caspase_1; -.
DR   GenomeRNAi; 834; -.
DR   NextBio; 3460; -.
DR   PMAP-CutDB; P29466; -.
DR   PRO; PR:P29466; -.
DR   Bgee; P29466; -.
DR   CleanEx; HS_CASP1; -.
DR   ExpressionAtlas; P29466; baseline and differential.
DR   Genevestigator; P29466; -.
DR   GO; GO:0097169; C:AIM2 inflammasome complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
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; IBA:RefGenome.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:GOC.
DR   GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
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:0097194; P:execution phase of apoptosis; IBA:RefGenome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0032611; P:interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR   GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
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 signaling; IEP:UniProtKB.
DR   GO; GO:0050717; P:positive regulation of interleukin-1 alpha secretion; IEA:Ensembl.
DR   GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
DR   GO; GO:0097300; P:programmed necrotic cell death; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IBA:RefGenome.
DR   GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.10.533.10; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR029030; Caspase-like_dom.
DR   InterPro; IPR017350; Caspase_ICE-type.
DR   InterPro; IPR011029; DEATH-like_dom.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR015917; Pept_C14A_p45_core.
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; SSF47986; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00046}.
FT   ACT_SITE    237    237       {ECO:0000269|PubMed:1574116}.
FT   ACT_SITE    285    285       {ECO:0000269|PubMed:1574116}.
FT   VAR_SEQ      20    335       Missing (in isoform Epsilon).
FT                                {ECO:0000303|PubMed:7876192}.
FT                                /FTId=VSP_000797.
FT   VAR_SEQ      20    112       Missing (in isoform Gamma and isoform
FT                                Delta). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:7876192}.
FT                                /FTId=VSP_000799.
FT   VAR_SEQ      92    112       Missing (in isoform Beta).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:7876192}.
FT                                /FTId=VSP_000798.
FT   VAR_SEQ     288    335       Missing (in isoform Delta).
FT                                {ECO:0000303|PubMed:7876192}.
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                                {ECO:0000269|PubMed:15498465}.
FT   CONFLICT    319    319       K -> R (in Ref. 4; BAD97223).
FT                                {ECO:0000305}.
FT   CONFLICT    402    402       P -> L (in Ref. 4; BAD97223).
FT                                {ECO:0000305}.
FT   TURN        129    132
FT   HELIX       138    147
FT   STRAND      148    150
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    236
FT   STRAND      242    244
FT   STRAND      250    252
FT   STRAND      255    257
FT   HELIX       258    265
FT   TURN        267    269
FT   HELIX       271    273
FT   STRAND      278    283
FT   STRAND      287    289
FT   STRAND      291    298
FT   HELIX       316    319
FT   STRAND      326    333
FT   STRAND      340    342
FT   TURN        343    345
FT   HELIX       348    360
FT   TURN        361    363
FT   HELIX       366    376
FT   STRAND      381    383
FT   STRAND      388    391
FT   STRAND      395    397
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
//
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