Protein Domain : IPR015917

Type:  Domain Name:  Peptidase C14A, caspase precursor p45, core
Description:  This group of sequences represent the core of p45 (45 kDa) precursor of caspases, which can be processed to produce the active p20 (20 kDa) and p10 (10 kDa) subunits. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family, clan CD) based on the architecture of their catalytic dyad or triad []. Caspases are tightly regulated proteins that require zymogen activation to become active, and once active can be regulated by caspase inhibitors. Activated caspases act as cysteine proteases, using the sulphydryl group of a cysteine side chain for catalysing peptide bond cleavage at aspartyl residues in their substrates. The catalytic cysteine and histidine residues are on the p20 subunit after cleavage of the p45 precursor.Caspases are mainly involved in mediating cell death (apoptosis) [, , ]. They have two main roles within the apoptosis cascade: as initiators that trigger the cell death process, and as effectors of the process itself. Caspase-mediated apoptosis follows two main pathways, one extrinsic and the other intrinsic or mitochondrial-mediated. The extrinsic pathway involves the stimulation of various TNF (tumour necrosis factor) cell surface receptors on cells targeted to die by various TNF cytokines that are produced by cells such as cytotoxic T cells. The activated receptor transmits the signal to the cytoplasm by recruiting FADD, which forms a death-inducing signalling complex (DISC) with caspase-8. The subsequent activation of caspase-8 initiates the apoptosis cascade involving caspases 3, 4, 6, 7, 9 and 10. The intrinsic pathway arises from signals that originate within the cell as a consequence of cellular stress or DNA damage. The stimulation or inhibition of different Bcl-2 family receptors results in the leakage of cytochrome c from the mitochondria, and the formation of an apoptosome composed of cytochrome c, Apaf1 and caspase-9. The subsequent activation of caspase-9 initiates the apoptosis cascade involving caspases 3 and 7, among others. At the end of the cascade, caspases act on a variety of signal transduction proteins, cytoskeletal and nuclear proteins, chromatin-modifying proteins, DNA repair proteins and endonucleases that destroy the cell by disintegrating its contents, including its DNA. The different caspases have different domain architectures depending upon where they fit into the apoptosis cascades, however they all carry the catalytic p10 and p20 subunits.Caspases can have roles other than in apoptosis, such as caspase-1 (interleukin-1 beta convertase) (), which is involved in the inflammatory process. The activation of apoptosis can sometimes lead to caspase-1 activation, providing a link between apoptosis and inflammation, such as during the targeting of infected cells. Caspases may also be involved in cell differentiation []. Short Name:  Pept_C14A_p45_core
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0 Child Features

3 Contains

DB identifier Type Name
IPR001309 Domain Peptidase C14, ICE, catalytic subunit p20
IPR002138 Domain Peptidase C14, caspase non-catalytic subunit p10
IPR016129 Active_site Peptidase C14, ICE, catalytic subunit p20, active site

2 Cross Referencess

Identifier
PR00376
SM00115

2 Found Ins

DB identifier Type Name
IPR015470 Family Caspase-3
IPR017350 Family Caspase, interleukin-1 beta convertase-type

2 GO Annotations

GO Term Gene Name
GO:0008234 IPR015917
GO:0006915 IPR015917

2 Ontology Annotations

GO Term Gene Name
GO:0008234 IPR015917
GO:0006915 IPR015917

1 Parent Features

DB identifier Type Name
IPR011600 Domain Peptidase C14, caspase domain

7 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Mapoly0052s0114.1.p A0A2R6WWW4 PAC:33026716 Marchantia polymorpha 807  
Mapoly0108s0037.1.p A0A2R6WCW2 PAC:33021780 Marchantia polymorpha 807  
CepurR40.5G008800.1.p PAC:43020773 Ceratodon purpureus R40 1147  
CepurR40.5G008700.1.p PAC:43019727 Ceratodon purpureus R40 1508  
CepurGG1.5G009900.1.p PAC:43038693 Ceratodon purpureus GG1 1856  
CepurGG1.5G009700.1.p PAC:43040203 Ceratodon purpureus GG1 1149  
CepurGG1.5G009500.1.p PAC:43040443 Ceratodon purpureus GG1 1385  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11517925
            15077141
            15066636
            10578171
            10872455