| IED ID | IndEnz0002001086 |
| Enzyme Type ID | protease001086 |
| Protein Name |
Urokinase-type plasminogen activator U-plasminogen activator uPA EC 3.4.21.73 Cleaved into: Urokinase-type plasminogen activator long chain A; Urokinase-type plasminogen activator short chain A; Urokinase-type plasminogen activator chain B |
| Gene Name | PLAU |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MRVLLVCLLLCALVVSDSEGSHELHGVSDASNCGCLNGGTCVTYKYFSNIWRCNCPKKFQGEHCEIDTLKTCYHGDGHSYRGKANTDIMDRPCLAWNSANVLTKTYHAHRPDALQLGLGKHNYCRNPDHQRRPWCYVQVGLKQLIQECKVHDCSSGKKPALPPGKLEFQCGQKALRPRFKIIGGEFTIIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINHQKKEDYIVYLGRSRLNSMTPGEMKFEVEQLILHEGYRADTLAHHNDIALLKILSNNGQCAQPSRSIQTICLPPWNADPNFGTSCEITGFGKENSTDYLYPEQLKMTVVKLVSYQECQQPHYYGSEVTTKMLCAADPQWETDSCQGDSGGPLVCSVQGRMTLTGIVSWGRGCALKNKPGVYTRVSRFLPWIRSHIGEENGLAL |
| Enzyme Length | 433 |
| Uniprot Accession Number | Q8MHY7 |
| Absorption | |
| Active Site | ACT_SITE 226; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 277; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 378; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250|UniProtKB:P00749}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.73; |
| DNA Binding | |
| EC Number | 3.4.21.73 |
| Enzyme Function | FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. {ECO:0000250|UniProtKB:P00749}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (4); Disulfide bond (12); Domain (3); Glycosylation (1); Modified residue (1); Region (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Kringle;Phosphoprotein;Plasminogen activation;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00749}. |
| Modified Residue | MOD_RES 325; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00749 |
| Post Translational Modification | PTM: Phosphorylation of Ser-325 abolishes proadhesive ability but does not interfere with receptor binding. {ECO:0000250}.; PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4. {ECO:0000250|UniProtKB:P00749}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,444 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |