| IED ID | IndEnz0002010163 |
| Enzyme Type ID | protease010163 |
| Protein Name |
Tissue-type plasminogen activator t-PA t-plasminogen activator tPA EC 3.4.21.68 Cleaved into: Tissue-type plasminogen activator chain A; Tissue-type plasminogen activator chain B |
| Gene Name | Plat |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MKGELLCVLLLCGVAFTLPDQGIHRRFRRGARSYRATCRDEQTQTTYQQHQSWLRPMLRGNRVEYCRCNSGLAQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPDGFVGKRCDIDTRATCFEGQGITYRGTWSTAENGAECINWNSSALSQKPYSARRPNAIKLGLGNHNYCRNPDRDVKPWCYVFKAGKYTTEFCSTPACPKGPTEDCYVGKGVTYRGTHSFTTSKASCLPWNSMILIGKTYTAWRANSQALGLGRHNYCRNPDGDAKPWCHVMKDRKLTWEYCDMSPCSTCGLRQYKQPQFRIKGGLFTDITSHPWQAAIFVKNKRSPGERFLCGGVLISSCWVLSAAHCFVERFPPHHLKVVLGRTYRVVPGEEEQTFEIEKYIVHKEFDDDTYDNDIALLQLRSDSSQCAQESSSVGTACLPDPDVQLPDWTECELSGYGKHEASSPFFSDRLKEAHVRLYPSSRCTSQHLFNKTITSNMLCAGDTRTGGNQDVHDACQGDSGGPLVCMIDKRMTLLGIISWGLGCGQKDVPGIYTKVTNYLNWIQDNMKQ |
| Enzyme Length | 559 |
| Uniprot Accession Number | P19637 |
| Absorption | |
| Active Site | ACT_SITE 355; /note=Charge relay system; ACT_SITE 404; /note=Charge relay system; ACT_SITE 510; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.68; |
| DNA Binding | |
| EC Number | 3.4.21.68 |
| Enzyme Function | FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (PubMed:1515147). {ECO:0000269|PubMed:1515147}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (17); Domain (5); Glycosylation (2); Propeptide (2); Region (1); Sequence conflict (1); Signal peptide (1); Site (3) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Kringle;Plasminogen activation;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-308 catalyzed by plasmin, tissue kallikrein or factor Xa. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10727258; 10899350; 12000738; 12070304; 12220690; 12524078; 1425827; 14512838; 14614217; 14693179; 15223382; 15496678; 15882815; 16555239; 16977483; 17040480; 18467699; 18716863; 18718505; 19279110; 19935650; 20035854; 21976424; 25325345; 25423126; 25676919; 3017447; 3102470; 3137452; 3891762; 8343497; 9405184; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,903 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.68; |