| IED ID | IndEnz0002018953 |
| Enzyme Type ID | protease018953 |
| Protein Name |
Caspase-7 CASP-7 EC 3.4.22.60 Apoptotic protease Mch-3 Cysteine protease LICE2 Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11 |
| Gene Name | Casp7 Lice2 Mch3 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MTDDQDCAAELEKVDSSSEDGVDAKPDRSSIISSILLKKKRNASAGPVRTGRDRVPTYLYRMDFQKMGKCIIINNKNFDKATGMDVRNGTDKDAGALFKCFQNLGFEVTVHNDCSCAKMQDLLRKASEEDHSNSACFACVLLSHGEEDLIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDIDANPRNKIPVEADFLFAYSTVPGYYSWRNPGKGSWFVQALCSILNEHGKDLEIMQILTRVNDRVARHFESQSDDPRFNEKKQIPCMVSMLTKELYFSR |
| Enzyme Length | 303 |
| Uniprot Accession Number | P97864 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence=ECO:0000250; ACT_SITE 186; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60; Evidence={ECO:0000269|PubMed:25231987}; |
| DNA Binding | |
| EC Number | 3.4.22.60 |
| Enzyme Function | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Cleaves and activates sterol regulatory element binding proteins (SREBPs) (By similarity). Overexpression promotes programmed cell death (By similarity). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (PubMed:25231987). 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). {ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:30878284}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (2); Erroneous initiation (1); Modified residue (1); Propeptide (2); Region (1); Sequence conflict (3) |
| Keywords | Acetylation;Apoptosis;Cytoplasm;Hydrolase;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | P11103; P62270 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:17242355 |
| Post Translational Modification | PTM: Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10087912; 10377054; 10578172; 10618441; 10739653; 11259653; 11526440; 11549719; 11829465; 12466851; 12480175; 12717433; 12819136; 14583630; 14686614; 15163632; 15200957; 15231831; 15525783; 15994297; 16141072; 16183742; 16469926; 16932756; 17023557; 17283187; 17371867; 17565040; 17646170; 17893180; 17913437; 18023262; 18631454; 18632667; 18667412; 18723680; 19074731; 19168786; 19325570; 19343209; 19555972; 19759058; 19801895; 19838298; 20019843; 20057499; 20179271; 20802146; 21267068; 21389984; 21666244; 21677750; 21876121; 22195746; 22365665; 22464733; 22807671; 22858065; 23341629; 23384561; 23424201; 23713787; 23834359; 24388981; 24632563; 24664731; 24752940; 25162007; 25525875; 25551609; 25738962; 26038565; 26095253; 26121671; 26253163; 26271098; 26306916; 26504199; 26643564; 26924441; 27121492; 27339879; 27552481; 27643624; 27737018; 27808091; 29563882; 30021146; 30185650; 30381458; 30451870; 30485804; 31723262; 32471877; 32989095; 33278357; 9070890; 9202146; 9654089; 9837723; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,061 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.60; |