PLAU
| Plasminogen activator, urokinase |
PDB rendering based on 1c5w. |
| Available structures |
| PDB |
1C5W, 1C5X, 1C5Y, 1C5Z, 1EJN, 1F5K, 1F5L, 1F92, 1FV9, 1GI7, 1GI8, 1GI9, 1GJ7, 1GJ8, 1GJ9, 1GJA, 1GJB, 1GJC, 1GJD, 1KDU, 1LMW, 1O3P, 1O5A, 1O5B, 1O5C, 1OWD, 1OWE, 1OWH, 1OWI, 1OWJ, 1OWK, 1SC8, 1SQA, 1SQO, 1SQT, 1U6Q, 1URK, 1VJ9, 1VJA, 1W0Z, 1W10, 1W11, 1W12, 1W13, 1W14, 2FD6, 2I9A, 2I9B, 2NWN, 2O8T, 2O8U, 2O8W, 2R2W, 2VIN, 2VIO, 2VIP, 2VIQ, 2VIV, 2VIW, 2VNT, 3BT1, 3BT2, 3IG6, 3KGP, 3KHV, 3KID, 3M61, 3MHW |
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| Identifiers |
| Symbols |
PLAU; ATF; UPA; URK; u-PA |
| External IDs |
OMIM: 191840 MGI: 97611 HomoloGene: 55670 GeneCards: PLAU Gene |
| EC number |
3.4.21.73 |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
5328 |
18792 |
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| Ensembl |
ENSG00000122861 |
ENSMUSG00000021822 |
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| UniProt |
P00749 |
Q0VBA8 |
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| RefSeq (mRNA) |
NM_001145031.1 |
NM_008873.3 |
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| RefSeq (protein) |
NP_001138503.1 |
NP_032899.1 |
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| Location (UCSC) |
Chr 10:
75.67 – 75.68 Mb |
Chr 14:
21.66 – 21.66 Mb |
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| PubMed search |
[1] |
[2] |
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Urokinase-type plasminogen activator is an enzyme that in humans is encoded by the PLAU gene.[1]
This gene encodes a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. A specific polymorphism in this gene may be associated with late-onset Alzheimer disease and also with decreased affinity for fibrin-binding. The protein encoded by this gene converts plasminogen to plasmin by specific cleavage of an Arg-Val bond in plasminogen. This gene's proprotein is cleaved at a Lys-Ile bond by plasmin to form a two-chain derivative in which a single disulfide bond connects the amino-terminal A-chain to the catalytically active, carboxy-terminal B-chain. This two-chain derivative is also called HMW-uPA (high molecular weight uPA). HMW-uPA can be further processed into LMW-uPA (low molecular weight uPA) by cleavage of chain A into a short chain A (A1) and an amino-terminal fragment. LMW-uPA is proteolytically active but does not bind to the uPA receptor.[2]
Interactions
PLAU has been shown to interact with Protein C inhibitor.[3][4]
References
- ^ Nagai M, Hiramatsu R, Kaneda T, Hayasuke N, Arimura H, Nishida M, Suyama T (Dec 1985). "Molecular cloning of cDNA coding for human preprourokinase". Gene 36 (1-2): 183–8. doi:10.1016/0378-1119(85)90084-8. PMID 2415429.
- ^ "Entrez Gene: PLAU plasminogen activator, urokinase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5328.
- ^ Geiger, M; Huber K, Wojta J, Stingl L, Espana F, Griffin J H, Binder B R (Aug. 1989). "Complex formation between urokinase and plasma protein C inhibitor in vitro and in vivo". Blood (UNITED STATES) 74 (2): 722–8. ISSN 0006-4971. PMID 2752144.
- ^ España, F; Berrettini M, Griffin J H (Aug. 1989). "Purification and characterization of plasma protein C inhibitor". Thromb. Res. (UNITED STATES) 55 (3): 369–84. doi:10.1016/0049-3848(89)90069-8. ISSN 0049-3848. PMID 2551064.
Further reading
- Ploug M, Gårdsvoll H, Jørgensen TJ, et al. (2002). "Structural analysis of the interaction between urokinase-type plasminogen activator and its receptor: a potential target for anti-invasive cancer therapy.". Biochem. Soc. Trans. 30 (2): 177–83. doi:10.1042/BST0300177. PMID 12023847.
- Alfano M, Sidenius N, Blasi F, Poli G (2004). "The role of urokinase-type plasminogen activator (uPA)/uPA receptor in HIV-1 infection.". J. Leukoc. Biol. 74 (5): 750–6. doi:10.1189/jlb.0403176. PMID 12960238.
- Harbeck N, Kates RE, Gauger K, et al. (2004). "Urokinase-type plasminogen activator (uPA) and its inhibitor PAI-I: novel tumor-derived factors with a high prognostic and predictive impact in breast cancer.". Thromb. Haemost. 91 (3): 450–6. doi:10.1160/TH03-12-0798. PMID 14983219.
- Gilabert-Estelles J, Ramon LA, España F, et al. (2006). "Expression of the fibrinolytic components in endometriosis.". Pathophysiol. Haemost. Thromb. 35 (1-2): 136–40. doi:10.1159/000093556. PMID 16855359.
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PDB gallery
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1c5w: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
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1c5x: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
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1c5y: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
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1c5z: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
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1ejn: UROKINASE PLASMINOGEN ACTIVATOR B-CHAIN INHIBITOR COMPLEX
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1f5k: UROKINASE PLASMINOGEN ACTIVATOR B-CHAIN-BENZAMIDINE COMPLEX
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1f5l: UROKINASE PLASMINOGEN ACTIVATOR B-CHAIN-AMILORIDE COMPLEX
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1f92: UROKINASE PLASMINOGEN ACTIVATOR B CHAIN-UKI-1D COMPLEX
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1fv9: Crystal structure of human microurokinase in complex with 2-amino-5-hydroxy-benzimidazole
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1gi7: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
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1gi8: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
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1gi9: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
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1gj7: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gj8: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gj9: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gja: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gjb: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gjc: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1gjd: ENGINEERING INHIBITORS HIGHLY SELECTIVE FOR THE S1 SITES OF SER190 TRYPSIN-LIKE SERINE PROTEASE DRUG TARGETS
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1kdu: SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE
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1lmw: LMW U-PA STRUCTURE COMPLEXED WITH EGRCMK (GLU-GLY-ARG CHLOROMETHYL KETONE)
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1o3p: Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors
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1o5a: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)
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1o5b: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)
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1o5c: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)
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1owd: Substituted 2-Naphthamidine inhibitors of urokinase
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1owe: Substituted 2-Naphthamidine inhibitors of urokinase
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1owh: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1owi: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1owj: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1owk: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1sc8: Urokinase Plasminogen Activator B-Chain-J435 Complex
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1sqa: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1sqo: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1sqt: Substituted 2-Naphthamidine Inhibitors of Urokinase
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1u6q: Substituted 2-Naphthamadine inhibitors of Urokinase
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1urk: SOLUTION STRUCTURE OF THE AMINO TERMINAL FRAGMENT OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR
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1vj9: Urokinase Plasminogen Activator B-Chain-JT464 Complex
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1vja: Urokinase Plasminogen Activator B-Chain-JT464 Complex
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2fd6: Structure of Human Urokinase Plasminogen Activator in Complex with Urokinase Receptor and an anti-upar antibody at 1.9 A
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2i9a: Crystal structure of the free aminoterminal fragment of urokinase type plasminogen activator (ATF)
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2i9b: Crystal structure of ATF-urokinase receptor complex
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