| IED ID | IndEnz0002009592 |
| Enzyme Type ID | protease009592 |
| Protein Name |
Tryptase alpha/beta-1 Tryptase-1 EC 3.4.21.59 Tryptase I Tryptase alpha-1 |
| Gene Name | TPSAB1 TPS1 TPS2 TPSB1 |
| 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 | MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP |
| Enzyme Length | 275 |
| Uniprot Accession Number | Q15661 |
| Absorption | |
| Active Site | ACT_SITE 74; /note=Charge relay system; ACT_SITE 121; /note=Charge relay system; ACT_SITE 224; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.; EC=3.4.21.59; |
| DNA Binding | |
| EC Number | 3.4.21.59 |
| Enzyme Function | FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315). {ECO:0000250, ECO:0000250|UniProtKB:P21845, ECO:0000269|PubMed:18854315}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (16); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (5); Natural variant (28); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | P16333; P27986; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Note=Released from the secretory granules upon mast cell activation. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (17) |
| Cross Reference PDB | 1LTO; 2F9N; 2F9O; 2F9P; 2ZEB; 2ZEC; 4A6L; 4MPU; 4MPV; 4MPW; 4MPX; 4MQA; 5F03; 5WI6; 6O1F; 6P0P; 6VVU; |
| Mapped Pubmed ID | 11792624; 11876641; 11906611; 12397176; 12742661; 15567416; 15638376; 16027150; 16414069; 16517749; 17146627; 17205215; 17449330; 17474147; 17635650; 17655281; 18079491; 18272363; 18359288; 18790994; 19100407; 19250736; 19535787; 19625657; 20087660; 20540319; 20718781; 21493897; 21707711; 2176865; 21791437; 22102069; 22192588; 22194960; 22363824; 22613992; 23018683; 23330964; 23559352; 23991686; 24054365; 24155887; 24237068; 24372627; 24507159; 24565497; 24726923; 24806698; 24915568; 25797204; 25957593; 26044856; 26089601; 26878596; 27288661; 27545065; 28049209; 29661938; 30128075; 30134249; 30641266; 31209239; 31337736; 31585081; 32057241; 32709152; 32717252; 32777817; 33353951; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,515 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.59; |