| IED ID | IndEnz0002002443 |
| Enzyme Type ID | protease002443 |
| Protein Name |
Granzyme H EC 3.4.21.- CCP-X Cathepsin G-like 2 CTSGL2 Cytotoxic T-lymphocyte proteinase Cytotoxic serine protease C CSP-C |
| Gene Name | GZMH CGL2 CTSGL2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MQPFLLLLAFLLTPGAGTEEIIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHCQGSSINVTLGAHNIKEQERTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDCQCERLFHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQGILSYGNKKGTPPGVYIKVSHFLPWIKRTMKRL |
| Enzyme Length | 246 |
| Uniprot Accession Number | P20718 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 108; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 202; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINB1. {ECO:0000269|PubMed:23269243}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication. {ECO:0000269|PubMed:22156497, ECO:0000269|PubMed:23269243}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (15); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Helix (4); Natural variant (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Alternative splicing;Cytolysis;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytolytic granule {ECO:0000269|PubMed:23269243}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3TJU; 3TJV; 3TK9; 4GAW; |
| Mapped Pubmed ID | 10512690; 10521426; 12515723; 15069086; 17363894; 17409270; 17765974; 17766182; 19039329; 20889553; 22156339; 23352961; 33737344; 6807977; 9570564; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,315 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B59; |