| IED ID | IndEnz0002015565 |
| Enzyme Type ID | protease015565 |
| Protein Name |
Granzyme B G,H EC 3.4.21.79 CTLA-1 Cytotoxic cell protease 1 CCP1 Fragmentin-2 |
| Gene Name | Gzmb Ctla-1 Ctla1 |
| 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 | MKILLLLLTLSLASRTKAGEIIGGHEVKPHSRPYMALLSIKDQQPEAICGGFLIREDFVLTAAHCEGSIINVTLGAHNIKEQEKTQQVIPMVKCIPHPDYNPKTFSNDIMLLKLKSKAKRTRAVRPLNLPRRNVNVKPGDVCYVAGWGRMAPMGKYSNTLQEVELTVQKDRECESYFKNRYNKTNQICAGDPKTKRASFRGDSGGPLVCKKVAAGIVSYGYKDGSPPRAFTKVSSFLSWIKKTMKSS |
| Enzyme Length | 247 |
| Uniprot Accession Number | P04187 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P18291; ACT_SITE 108; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P18291; ACT_SITE 203; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P18291 |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by the serine protease inhibitor diisopropylfluorophosphate. {ECO:0000250|UniProtKB:P10144}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79; Evidence={ECO:0000250|UniProtKB:P10144}; |
| DNA Binding | |
| EC Number | 3.4.21.79 |
| Enzyme Function | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Asp. Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis. {ECO:0000250|UniProtKB:P10144}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Apoptosis;Cytolysis;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10144}. Cytolytic granule {ECO:0000250|UniProtKB:P10144}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P10144}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10367905; 10570179; 10673337; 10737774; 10820381; 10862355; 11380680; 11497079; 11507223; 11884544; 12039912; 12115618; 12182457; 12355441; 12594834; 12601154; 12847210; 1303276; 1346779; 1351769; 1371498; 1387109; 14499263; 14985351; 15061770; 15084164; 15322178; 15356127; 1544892; 15454490; 15456877; 15534000; 15567431; 15569669; 15699075; 15699103; 15699143; 15749851; 15998831; 16034109; 16116214; 16141072; 16236268; 16280358; 16339537; 16405654; 16436955; 16541469; 16606695; 16618603; 16775321; 16807745; 16869802; 16873683; 16901729; 17005566; 17088087; 17116752; 17125145; 17179148; 17283185; 17283187; 17540585; 17599099; 17661907; 17919943; 18064039; 18096765; 18222115; 18606691; 18788942; 18802078; 18836177; 19119023; 19136373; 19228596; 19414782; 19525394; 19592578; 1971251; 19838298; 19915045; 19915065; 19965675; 20007464; 20018616; 20035050; 20042681; 2007574; 20395300; 20400962; 20424188; 20435891; 20543105; 20585036; 20935160; 21177822; 21248253; 21267068; 21278341; 21296981; 21311565; 21316440; 21450826; 21525386; 21590764; 21606480; 21677750; 21709155; 21853094; 21964027; 22017873; 22031758; 22084442; 22227570; 22236998; 22427643; 22674984; 22792290; 22801574; 22844498; 2293612; 2300587; 2307468; 23264653; 2338144; 23402528; 23568450; 23642129; 23663075; 23744295; 23840635; 23912712; 24113190; 24205352; 24290277; 24414824; 24440757; 24487434; 24625974; 24752302; 24791744; 24906149; 24928990; 25168425; 25205813; 25367158; 25398236; 25428875; 25452549; 25495009; 25502180; 25526309; 25605735; 25750028; 25923440; 25990242; 26390156; 26392464; 26436530; 26610869; 26756195; 26894590; 27365293; 27608599; 27612641; 27716898; 27721430; 27760760; 27806296; 28082402; 28207896; 28537251; 28722018; 28723565; 28798348; 29107333; 29445095; 29743559; 30135490; 30183689; 31241463; 31498925; 3182016; 32407293; 32473350; 32504614; 3257230; 32696761; 32726632; 33436591; 33674611; 34183776; 3485287; 7493755; 7518410; 7566124; 7730612; 7798197; 7906967; 8011213; 8012118; 8018917; 8137431; 8251184; 8453108; 8468056; 8530045; 8626800; 8631895; 8833158; 8917549; 9259590; 9362539; 9558376; 9671732; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,470 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.79; |