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urokinase; urokinase-type plasminogen activator; U-plasminogen activator; uPA (PLAU)

Function: - proteolytic enzyme produced naturally by the renal parenchymal cells that promotes thrombolysis by converting plasminogen to plasmin - specific cleavage of Arg-|-Val bond in plasminogen to form plasmin - inhibited by SERPINA5 - phosphorylation of Ser-158 & Ser-323 abolishes proadhesive ability but does not interfere with receptor binding - found in high & low molecular mass forms - each consists of two chains, A & B - the high molecular mass form contains a long chain A which is cleaved to yield a short chain A - forms heterodimer with SERPINA5 - binds LRP1B - binding is followed by internalization & degradation - interacts with MRC2 - interacts with PLAUR Structure: - belongs to the peptidase S1 family - contains 1 EGF-like domain - contains 1 kringle domain - contains 1 peptidase S1 domain Compartment: - secreted - normally present in urine Alternative splicing: named isoforms=2 Expression: - secreted by renal parenchymal cells - expressed in the prostate gland & prostate cancers Pathology: - defects in PLAU are the cause of Quebec platelet disorder Pharmacology: - available under the name Abbokinase (Abbott) - used for therapy of venous thrombosis or venous thromboembolism

Interactions

molecular events

Related

urokinase plasminogen activator surface receptor; uPAR; U-PAR; monocyte activation antigen Mo3; CD87 (PLAUR, MO3, UPAR)

Specific

Abbokinase (urokinase) prourokinase; contains: urokinase-type plasminogen activator long chain A; urokinase-type plasminogen activator short chain A; urokinase-type plasminogen activator chain B (PLAU) urokinase A fragment urokinase B fragment Urokinase Parenteral

General

enzymatic agent fibrinolytic agent (thrombolytic agent) glycoprotein multisubunit protein peptide precursor phosphoprotein plasminogen activator

Properties

SIZE: entity length = 431 aa MW = 49 kD MOTIF: signal sequence {1-20} EGF domain {27-63} MOTIF: cysteine residue {C31} MODIFICATION: cysteine residue {C39} cysteine residue {C33} MODIFICATION: cysteine residue {C51} PLAUR binding {34-57} Thr glycosylation site {T38} cysteine residue {C39} MODIFICATION: cysteine residue {C31} cysteine residue {C51} MODIFICATION: cysteine residue {C33} cysteine residue {C53} MODIFICATION: cysteine residue {C62} cysteine residue {C62} MODIFICATION: cysteine residue {C53} Kringle {70-151} MOTIF: cysteine residue {C70} MODIFICATION: cysteine residue {C151} cysteine residue {C91} MODIFICATION: cysteine residue {C133} cysteine residue {C122} MODIFICATION: cysteine residue {C146} cysteine residue {C133} MODIFICATION: cysteine residue {C91} cysteine residue {C146} MODIFICATION: cysteine residue {C122} cysteine residue {C151} MODIFICATION: cysteine residue {C70} Connecting peptide {152-177} MOTIF: Ser phosphorylation site {S158} cysteine residue {C168} MODIFICATION: cysteine residue {C-INTERCHAIN} proteolytic site {177-178} S1 domain {179-424} MOTIF: cysteine residue {C209} MODIFICATION: cysteine residue {C225} cysteine residue {C217} MODIFICATION: cysteine residue {C288} histidine residue {H224} cysteine residue {C225} MODIFICATION: cysteine residue {C209} aspartate residue {D275} cysteine residue {C288} MODIFICATION: cysteine residue {C217} cysteine residue {C313} MODIFICATION: cysteine residue {C382} N-glycosylation site {N322} Ser phosphorylation site {S323} cysteine residue {C345} MODIFICATION: cysteine residue {C361} cysteine residue {C361} MODIFICATION: cysteine residue {C345} cysteine residue {C372} MODIFICATION: cysteine residue {C400} serine residue {S376} cysteine residue {C382} MODIFICATION: cysteine residue {C313} cysteine residue {C400} MODIFICATION: cysteine residue {C372} MISC-INFO: elimination route LIVER KIDNEY 1/2life 10-20 MINUTES

Database Correlations

OMIM correlations MORBIDMAP 191840 UniProt P00749 PFAM correlations Entrez Gene 5328 Kegg hsa:5328 ENZYME 3.4.21.73

References

  1. Clinical Diagnosis and Management by Laboratory Methods, 18th ed, J.B. Henry (ed), W.B. Saunders, Philadelphia, PA, 1991 pg 739
  2. UniProt :accession P00749
  3. Wikipedia; Note: urokinase entry http://en.wikipedia.org/wiki/urokinase
  4. SeattleSNPs http://pga.gs.washington.edu/data/plau/