Casp7
entrez
12369
canonical
uniprot
P97864
canonical
ensembl
ENSMUSG00000025076
resolver
ensp
ENSMUSP00000026062
resolver
enst
ENSMUST00000026062
resolver
genesymbol
Casp7
resolver
genesymbol_syn
Lice2
resolver
genesymbol_syn
Mch3
resolver
uniprot
O08669
resolver
uniprot
Q4FJQ4
resolver
uniprot_entry
CASP7_MOUSE
resolver
uniprot_entry
Q4FJQ4_MOUSE
resolver
uniprot_sec
O08669
resolver
activity_regulation
ACTIVITY REGULATION: During activation, the N-terminal disordered prodomain is removed by cleavage (PubMed:18667412). Concomitantly, double cleavage gives rise to a large Caspase-7 subunit p20 and a small Caspase-7 subunit p11 (PubMed:18667412). The two large and two small subunits then assemble to form the active CASP7 complex (PubMed:18667412). Can be cleaved and activated by different caspases, depending on the context (PubMed:18667412, PubMed:35705808). Cleaved and activated by initiator caspases (CASP8 and/or CASP9), leading to execution phase of apoptosis (By similarity). Cleavage and maturation by GZMB regulates granzyme-mediated programmed cell death (PubMed:35705808). Cleavage and maturation by CASP1 regulates pyroptosis (PubMed:18667412, PubMed:35705808). Inhibited by XIAP, which directly binds to the active site pocket and obstructs substrate entry (By similarity). Phosphorylation at Ser-30 and Ser-239 by PAK2 inhibits its activity (By similarity). Inhibited by BIRC6; following inhibition of BIRC6-caspase binding by DIABLO/SMAC, BIRC6 is subjected to caspase cleavage, leading to an increase in active caspases (By similarity). {ECO:0000250|UniProtKB:P42574, ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:18667412, ECO:0000269|PubMed:35705808}.
uniprot
proteins
amino_acid_sequence
MTDDQDCAAELEKVDSSSEDGVDAKPDRSSIISSILLKKKRNASAGPVRTGRDRVPTYLYRMDFQKMGKCIIINNKNFDKATGMDVRNGTDKDAGALFKCFQNLGFEVTVHNDCSCAKMQDLLRKASEEDHSNSACFACVLLSHGEEDLIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDIDANPRNKIPVEADFLFAYSTVPGYYSWRNPGKGSWFVQALCSILNEHGKDLEIMQILTRVNDRVARHFESQSDDPRFNEKKQIPCMVSMLTKELYFSR
uniprot
proteins
ec_number
3.4.22.60
uniprot
proteins
function
FUNCTION: Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins (PubMed:16469926, PubMed:19168786). Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (PubMed:25231987). Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (PubMed:18667412, PubMed:35705808). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8 and/or CASP9), mediates execution of apoptosis by catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and YY1 (PubMed:16469926). Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins (PubMed:16469926). Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair (PubMed:35705808). Regulates pyroptosis in intestinal epithelial cells: cleaved and activated by CASP1 in response to S.typhimurium infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of gasdermin-D (GSDMD) pores (PubMed:22807671, PubMed:35705808). Regulates granzyme-mediated programmed cell death in hepatocytes: cleaved and activated by granzyme B (GZMB) in response to bacterial infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of perforin (PRF1) pores (PubMed:35705808). Following cleavage by CASP1 in response to inflammasome activation, catalyzes processing and inactivation of PARP1, alleviating the transcription repressor activity of PARP1 (PubMed:22464733). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Cleaves and activates sterol regulatory element binding proteins (SREBPs) (By similarity). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (PubMed:25231987). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity). {ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:16469926, ECO:0000269|PubMed:18667412, ECO:0000269|PubMed:19168786, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:22807671, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:30878284, ECO:0000269|PubMed:35705808}.
uniprot
proteins
mass_dalton
34061
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="D->A: Abolished cleavage and activation; when associated with A-198."; /evidence="ECO:0000269|PubMed:18667412"; MUTAGEN 198; /note="D->A: Abolished cleavage and activation; when associated with A-23."; /evidence="ECO:0000269|PubMed:18667412
uniprot
proteins
post_translational_modification
PTM: Cleavage by different proteases, such as granzyme B (GZMB), caspase-1 (CASP1), caspase-8 (CASP8) or caspase-9 (CASP9) generate the two active subunits (PubMed:18667412, PubMed:22807671, PubMed:31251782, PubMed:35705808). Its involvement in different programmed cell death processes is probably specified by the protease that activates CASP7 (PubMed:35705808). Cleaved and activated by initiator caspases (CASP8 and/or CASP9), leading to execution phase of apoptosis (By similarity). Cleavage and maturation by GZMB regulates granzyme-mediated programmed cell death (PubMed:35705808). Cleaved and activated by CASP1 in response to bacterial infection (PubMed:18667412, PubMed:31251782, PubMed:35705808). Propeptide domains can also be cleaved efficiently by CASP3 (By similarity). Active heterodimers between the small subunit of caspase-7 and the large subunit of CASP3, and vice versa, also occur (By similarity). Also cleaved at the N-terminus at alternative sites by CAPN1, leading to its activation (By similarity). {ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:18667412, ECO:0000269|PubMed:22807671, ECO:0000269|PubMed:31251782, ECO:0000269|PubMed:35705808}.; PTM: Phosphorylation at Ser-30 and Ser-239 by PAK2 inhibits its activity (By similarity). Phosphorylation at Ser-30 prevents cleavage and activation by initiator caspase CASP9, while phosphorylation at Ser-239 prevents thiol protease activity by preventing substrate-binding (By similarity). {ECO:0000250|UniProtKB:P55210}.; PTM: Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC. {ECO:0000250|UniProtKB:P42574}.
uniprot
proteins
protein_family
Peptidase C14A family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16469926
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18667412
uniprot
proteins
pubmed
19168786
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22464733
uniprot
proteins
pubmed
22807671
uniprot
proteins
pubmed
25231987
uniprot
proteins
pubmed
30878284
uniprot
proteins
pubmed
31251782
uniprot
proteins
pubmed
35705808
uniprot
proteins
pubmed
9038361
uniprot
proteins
pubmed
9070923
uniprot
proteins
pubmed
9125129
uniprot
proteins
sequence_length
303
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55210}. Nucleus {ECO:0000250|UniProtKB:P55210}. Secreted, extracellular space {ECO:0000269|PubMed:35705808}. Note=Following cleavage and activation by CASP1 or granzyme B (GZMB), secreted into the extracellular milieu by passing through the gasdermin-D (GSDMD) pores or perforin (PRF1) pore, respectively. {ECO:0000269|PubMed:35705808}.
uniprot
proteins