EC 3.4.22.61: Caspase-8
Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala)
Systematic name:
-
Alternative Name(s):
- Apoptotic cysteine protease
- Apoptotic protease Mch-5
- CAP4
- CASP-8
- FADD-homologous ICE/CED-3-like protease
- FADD-like ICE
- FLICE
- ICE-like apoptotic protease 5
- MACH
- MORT1-associated CED-3 homolog
- Mammalian Ced-3 homolog 5
- Mch5
GO terms
Biochemical function:
- scaffold protein binding
- protein-containing complex binding
- identical protein binding
- death effector domain binding
- ubiquitin protein ligase binding
- cysteine-type peptidase activity
- peptidase activity
- protein binding
- tumor necrosis factor receptor binding
- death receptor binding
- cysteine-type endopeptidase activity
Biological process:
- self proteolysis
- execution phase of apoptosis
- extrinsic apoptotic signaling pathway
- apoptotic signaling pathway
- response to anesthetic
- obsolete cellular response to organic cyclic compound
- cellular response to mechanical stimulus
- pyroptotic inflammatory response
- syncytiotrophoblast cell differentiation involved in labyrinthine layer development
- negative regulation of necroptotic process
- protein maturation
- proteolysis involved in protein catabolic process
- positive regulation of proteolysis
- positive regulation of macrophage differentiation
- response to ethanol
- regulation of innate immune response
- positive regulation of neuron apoptotic process
- negative regulation of canonical NF-kappaB signal transduction
- positive regulation of canonical NF-kappaB signal transduction
- positive regulation of apoptotic process
- B cell activation
- T cell activation
- TRAIL-activated apoptotic signaling pathway
- response to tumor necrosis factor
- positive regulation of interleukin-1 beta production
- response to lipopolysaccharide
- response to estradiol
- response to cobalt ion
- positive regulation of cell migration
- macrophage differentiation
- natural killer cell activation
- protein processing
- regulation of tumor necrosis factor-mediated signaling pathway
- extrinsic apoptotic signaling pathway via death domain receptors
- heart development
- apoptotic process
- proteolysis
- regulation of cytokine production
- angiogenesis
Protein families (Pfam)![The deposited structure of PDB entry 8ynm contains 16 copies of Pfam domain PF01335 (Death effector domain) in CASP8 and FADD-like apoptosis regulator subunit p43. Showing 2 copies in chain I [auth G].](https://www.ebi.ac.uk/pdbe/static/entry/8ynm_1_G_Pfam_PF01335_image-200x200.png "The deposited structure of PDB entry <span class='highlight'>8ynm</span> contains 16 copies of Pfam domain <span class='highlight'>PF01335 (Death effector domain)</span> in <span class='highlight'>CASP8 and FADD-like apoptosis regulator subunit p43</span>. Showing 2 copies in chain <span class='highlight'>I [auth G]</span>.")
![The deposited structure of PDB entry 8ynm contains 6 copies of Pfam domain PF01335 (Death effector domain) in Caspase-8. Showing 2 copies in chain B [auth A].](https://www.ebi.ac.uk/pdbe/static/entry/8ynm_2_A_Pfam_PF01335_image-200x200.png "The deposited structure of PDB entry <span class='highlight'>8ynm</span> contains 6 copies of Pfam domain <span class='highlight'>PF01335 (Death effector domain)</span> in <span class='highlight'>Caspase-8</span>. Showing 2 copies in chain <span class='highlight'>B [auth A]</span>.")
![The deposited structure of PDB entry 8ynm contains 3 copies of Pfam domain PF00656 (Caspase domain) in Caspase-8. Showing 1 copy in chain B [auth A] (this domain is out of the observed residue ranges!).](https://www.ebi.ac.uk/pdbe/static/entry/8ynm_2_A_Pfam_PF00656_image-200x200.png "The deposited structure of PDB entry <span class='highlight'>8ynm</span> contains 3 copies of Pfam domain <span class='highlight'>PF00656 (Caspase domain)</span> in <span class='highlight'>Caspase-8</span>. Showing 1 copy in chain <span class='highlight'>B [auth A]</span> (this domain is out of the observed residue ranges!).")