Detail Information for IndEnz0002001087
IED ID IndEnz0002001087
Enzyme Type ID protease001087
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 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 MRVWLASLFLCALVANSEGGSELEASDESNCGCQNGGVCVSYKYFSSIRRCSCPKKFKGEHCEIDTSKTCYHGNGQSYRGKANTDTKGRPCLAWNSPAVLQQTYNAHRSDALSLGLGKHNYCRNPDNQRRPWCYVQIGLKQFVQECMVQDCSLSKKPSSTVDQQGFQCGQKALRPRFKIVGGEFTVVENQPWFAAIYLKNKGGSPPSFKCGGSLISPCWVASATHCFVNQPKKEEYVVYLGQSKRNSYNPGEMKFEVEQLILHEDFSDETLAFHNDIALLKIRTSTGQCAQPSRTIQTICLPPRFGDAPFGSDCEITGFGQESATDYFYPKDLKMSVVKIISHEQCKQPHYYGSEINYKMLCAADPEWKTDSCSGDSGGPLICNIDGRPTLSGIVSWGSGCAEKNKPGVYTRVSYFLNWIQSHIGEENGLAF
Enzyme Length 432
Uniprot Accession Number P29598
Absorption
Active Site ACT_SITE 225; /note=Charge relay system; ACT_SITE 276; /note=Charge relay system; ACT_SITE 377; /note=Charge relay system
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); Modified residue (1); Region (2); Sequence conflict (3); Signal peptide (1)
Keywords Disulfide bond;EGF-like domain;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 158; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00749
Post Translational Modification 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..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10727258; 12524078; 12919869; 15019809; 15322501; 15506291; 15854129; 16456094; 16899994; 17040480; 17587687; 17651644; 17712486; 17939964; 17953365; 18022622; 18052026; 18467699; 18716863; 18718505; 18998460; 19010488; 19099788; 19137075; 19166201; 19184369; 19490965; 19500378; 19527776; 19587273; 19615318; 19663807; 19834131; 19952306; 20016209; 20035854; 20731662; 20798533; 20952728; 21151668; 21375013; 21473829; 21779364; 21843593; 22160250; 22300381; 22592543; 23018346; 23324284; 23327706; 2509088; 9315743;
Motif
Gene Encoded By
Mass 47,957
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda