EC Number   |
General Information |
Reference |
|---|
   3.4.22.64 | evolution |
caspase-11 belongs to the caspase family and is an homologous protein of caspase-1, phylogenetic tree, relationship between caspase-1 and caspase-11 and tertiary structure comparison, overview |
770138 |
| 3.4.22.64 | evolution |
caspase-11 belongs to the inflammatory caspases |
771849 |
| 3.4.22.64 | evolution |
caspase-11 is a member of the caspase family of cysteine proteases |
-, 731616 |
| 3.4.22.64 | evolution |
caspase-11, -4, and -5 belong to a family of aspartate-specific cysteine proteases. Their activation requires oligomerization and autoproteolysis. Caspase-11, -4, and -5 contain an N-terminal death fold named caspase recruitment domain (CARD) and a C-terminal catalytic domain |
770172 |
| 3.4.22.64 | evolution |
caspases-4 and -5 are the human orthologues of murine caspase-11, sharing with it 68% and 47% amino acid sequence identity, respectively |
772221 |
| 3.4.22.64 | evolution |
inflammatory caspases all share a similar prodomain at the N-terminus responsible for protein-protein interactions: the caspase activation and recruitment domain (CARD). The genes of the inflammatory caspases are all located adjacent to the Casp1 gene on the mammalian chromosome (chromosome 9 in mouse), forming an inflammatory gene cluster. The close proximity of these genes and the high degree of similarity in the caspase protein structures might explain that the multiple inflammatory caspases arose from amplification of the Casp1 gene locus in the early stages of mammalian evolution |
731905 |
| 3.4.22.64 | evolution |
the regions surrounding Lys356 and Lys293 in caspase-4, EC 3.4.22.57, which interact with Glu28 and Asp30 in pro-IL-18, are not conserved in caspase-11. Instead, caspase-11 displays non-charged residues (His352 and Leu289) at these sites |
774708 |
| 3.4.22.64 | malfunction |
ADP-riboxanation of the Arg310 in caspase-11 blocks autoprocessing of caspase-11 as well as its recognition and cleavage of gasdermin D (GSDMD). ADP-riboxanation of caspase-11 paralyses pyroptosis-mediated defence in Shigella-infected mice. Mutation of ospC3 stimulates caspase-11- and GSDMD-dependent anti-Shigella humoral immunity, generating a vaccine-like protective effect |
774702 |
| 3.4.22.64 | malfunction |
all Casp1-/- mice also lack caspase-11, due to the generation of the Casp1-/- line in the 129 mouse strain background, which express a mis-spliced and truncated version of the Casp11 messenger RNA |
731611 |
| 3.4.22.64 | malfunction |
all existing caspase-1 deficient mice also lack Caspase-11 due to the backcrossing of a mutant Casp11 allele from 129 into C57BL/6 mice |
-, 732915 |
