Caspase 1

Caspase 1, apoptosis-related cysteine peptidase (interleukin 1 beta convertase)
PDB rendering based on 1bmq.
Available structures
1bmq, 1ibc, 1ice, 1rwk, 1rwm, 1rwn, 1rwo, 1rwp, 1rwv, 1rww, 1rwx, 1sc1, 1sc3, 1sc4, 2fqq, 2h48, 2hbq, 2hbr, 2hby, 2hbz
Identifiers
Symbols	CASP1; ICE; IL1BC; P45
External IDs	OMIM: 147678 MGI: 96544 HomoloGene: 7653
Gene ontology Molecular function • signal transducer activity • protein binding • cysteine-type peptidase activity • caspase activator activity • caspase activity Cellular component • intracellular Biological process • proteolysis • signal transduction • regulation of apoptosis • positive regulation of I-kappaB kinase/NF-kappaB cascade
Orthologs
Species	Human	Mouse
Entrez	834	12362
Ensembl	n/a	ENSMUSG00000025888
UniProt	n/a	P29452
RefSeq	NM_001223 (mRNA)	NM_009807 (mRNA)
	NP_001214 (protein)	NP_033937 (protein)
Location	n/a	Chr 9: 5.3 - 5.31 Mb
PubMed search	[1]	[2]

Caspase 1 is an enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory cytokines interleukin 1-β and interleukin 18, into active mature peptides.^[1] It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue. Caspase 1 is produced as a zymogen that is cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active caspase 1 contains two heterodimers of p20 and p10. It interacts with another CARD domain containing protein called PYCARD (or ASC) and is involved in inflammasome formation and activation of inflammatory processes.^[2]

Caspase 1 has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington's disease. Alternative splicing of the gene results in five transcript variants encoding distinct isoforms.^[3]

Interactions

Caspase 1 has been shown to interact with NLRC4.^[4][5]

References

1. ^ Thornberry N, Bull H, Calaycay J, Chapman K, Howard A, Kostura M, Miller D, Molineaux S, Weidner J, Aunins J (1992). "A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes". Nature 356 (6372): 768–74. doi:10.1038/356768a0. PMID 1574116. 
2. ^ Mariathasan S, Newton K, Monack D, Vucic D, French D, Lee W, Roose-Girma M, Erickson S, Dixit V (2004). "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf". Nature 430 (6996): 213–8. doi:10.1038/nature02664. PMID 15190255. 
3. ^ "Entrez Gene: CASP1 caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=834. 
4. ^ Damiano, Jason S; Oliveira Vasco, Welsh Kate, Reed John C (Jul. 2004). "Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses". Biochem. J. (England) 381 (Pt 1): 213–9. doi:10.1042/BJ20031506. PMID 15107016. 
5. ^ Damiano, J S; Stehlik C, Pio F, Godzik A, Reed J C (Jul. 2001). "CLAN, a novel human CED-4-like gene". Genomics (United States) 75 (1-3): 77–83. doi:10.1006/geno.2001.6579. ISSN 0888-7543. PMID 11472070. 

See also

• The Proteolysis Map

v • d • e PDB Gallery 1bmq: CRYSTAL STRUCTURE OF THE COMPLEX OF INTERLEUKIN-1BETA CONVERTING ENZYME (ICE) WITH A PEPTIDE BASED INHIBITOR, (3S )-N-METHANESULFONYL-3-({1-[N-(2-NAPHTOYL)-L-VALYL]-L-PROLYL }AMINO)-4-OXOBUTANAMIDE   1ibc: CRYSTAL STRUCTURE OF INHIBITED INTERLEUKIN-1BETA CONVERTING ENZYME   1ice: STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME   1rwk: Crystal structure of human caspase-1 in complex with 3-(2-mercapto-acetylamino)-4-oxo-pentanoic acid   1rwm: Crystal structure of human caspase-1 in complex with 4-oxo-3-[2-(5-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-thiophen-2-yl)-acetylamino]-pentanoic acid   1rwn: Crystal structure of human caspase-1 in complex with 3-{2-ethyl-6-[4-(quinoxalin-2-ylamino)-benzoylamino]-hexanoylamino}-4-oxo-butyric acid   1rwo: Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-ylamino)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-pentanoic acid   1rwp: Crystal structure of human caspase-1 in complex with 3-{6-[(8-hydroxy-quinoline-2-carbonyl)-amino]-2-thiophen-2-yl-hexanoylamino}-4-oxo-butyric acid   1rwv: Crystal structure of human caspase-1 in complex with 5-[5-(1-carboxymethyl-2-oxo-propylcarbamoyl)-5-phenyl-pentylsulfamoyl]-2-hydroxy-benzoic acid   1rww: Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid   1rwx: Crystal structure of human caspase-1 in complex with 4-oxo-3-{6-[4-(quinoxalin-2-yloxy)-benzoylamino]-2-thiophen-2-yl-hexanoylamino}-butyric acid   1sc1: Crystal structure of an active-site ligand-free form of the human caspase-1 C285A mutant   1sc3: Crystal structure of the human caspase-1 C285A mutant in complex with malonate   1sc4: Crystal structure of the human caspase-1 C285A mutant after removal of malonate   2fqq: Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide   2h48: Crystal structure of human caspase-1 (Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)   2hbq: Crystal structure of wildtype human caspase-1 in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)   2hbr: Crystal structure of human caspase-1 (Arg286->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)   2hby: Crystal structure of human caspase-1 (Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)   2hbz: Crystal structure of human caspase-1 (Arg286->Ala, Glu390->Ala) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)

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