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
	Human	Mouse
Entrez	834	12362
Ensembl	n/a	ENSMUSG00000025888
Uniprot	n/a	P29452
Refseq	NM_001223 (mRNA) NP_001214 (protein)	NM_009807 (mRNA) 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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