Urokinase-type plasminogen activator

Details

Name
Urokinase-type plasminogen activator
Synonyms
  • 3.4.21.73
  • U-plasminogen activator
Gene Name
PLAU
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037097|Urokinase-type plasminogen activator
MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQ
HCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHN
YCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKII
GGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLG
RSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICL
PSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKML
CAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIR
SHTKEENGLAL
Number of residues
431
Molecular Weight
48507.09
Theoretical pI
8.48
GO Classification
Functions
serine-type endopeptidase activity
Processes
angiogenesis / blood coagulation / cellular response to fluid shear stress / cellular response to glucose stimulus / cellular response to hepatocyte growth factor stimulus / cellular response to hypoxia / cellular response to lipopolysaccharide / cellular response to staurosporine / chemotaxis / embryo implantation / fibrinolysis / neuron death / plasminogen activation / positive regulation of cell proliferation / positive regulation of ovulation / positive regulation of reactive oxygen species metabolic process / positive regulation of smooth muscle cell migration / proteolysis / regulation of cell adhesion mediated by integrin / regulation of hepatocyte proliferation / regulation of receptor activity / regulation of smooth muscle cell migration / regulation of smooth muscle cell-matrix adhesion / regulation of wound healing / response to activity / response to hyperoxia / signal transduction / skeletal muscle tissue regeneration / smooth muscle cell migration / spermatogenesis
Components
cell surface / extracellular exosome / extracellular region / extracellular space / focal adhesion / plasma membrane
General Function
Serine-type endopeptidase activity
Specific Function
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0021654|Urokinase-type plasminogen activator (PLAU)
ATGGTCTTCCATTTGAGAACTAGATACGAACAGGCGAACTGTGACTGTCTAAATGGAGGA
ACATGTGTGTCCAACAAGTACTTCTCCAACATTCACTGGTGCAACTGCCCAAAGAAATTC
GGAGGGCAGCACTGTGAAATAGATAAGTCAAAAACCTGCTATGAGGGGAATGGTCACTTT
TACCGAGGAAAGGCCAGCACTGACACCATGGGCCGGCCCTGCCTGCCCTGGAACTCTGCC
ACTGTCCTTCAGCAAACGTACCATGCCCACAGATCTGATGCTCTTCAGCTGGGCCTGGGG
AAACATAATTACTGCAGGAACCCAGACAACCGGAGGCGACCCTGGTGCTATGTGCAGGTG
GGCCTAAAGCCGCTTGTCCAAGAGTGCATGGTGCATGACTGCGCAGATGGAAAAAAGCCC
TCCTCTCCTCCAGAAGAATTAAAATTTCAGTGTGGCCAAAAGACTCTGAGGCCCCGCTTT
AAGATTATTGGGGGAGAATTCACCACCATCGAGAACCAGCCCTGGTTTGCGGCCATCTAC
AGGAGGCACCGGGGGGGCTCTGTCACCTACGTGTGTGGAGGCAGCCTCATCAGCCCTTGC
TGGGTGATCAGCGCCACACACTGCTTCATTGATTACCCAAAGAAGGAGGACTACATCGTC
TACCTGGGTCGCTCAAGGCTTAACTCCAACACGCAAGGGGAGATGAAGTTTGAGGTGGAA
AACCTCATCCTACACAAGGACTACAGCGCTGACACGCTTGCTCACCACAACGACATTGCC
TTGCTGAAGATCCGTTCCAAGGAGGGCAGGTGTGCGCAGCCATCCCGGACTATACAGACC
ATCTGCCTGCCCTCGATGTATAACGATCCCCAGTTTGGCACAAGCTGTGAGATCACTGGC
TTTGGAAAAGAGAATTCTACCGACTATCTCTATCCGGAGCAGCTGAAAATGACTGTTGTG
AAGCTGATTTCCCACCGGGAGTGTCAGCAGCCCCACTACTACGGCTCTGAAGTCACCACC
AAAATGCTGTGTGCTGCTGACCCACAGTGGAAAACAGATTCCTGCCAGGGAGACTCAGGG
GGACCCCTCGTCTGTTCCCTCCAAGGCCGCATGACTTTGACTGGAATTGTGAGCTGGGGC
CGTGGATGTGCCCTGAAGGACAAGCCAGGCGTCTACACGAGAGTCTCACACTTCTTACCC
TGGATCCGCAGTCACACCAAGGAAGAGAATGGCCTGGCCCTCTGA
Chromosome Location
10
Locus
10q24
External Identifiers
ResourceLink
UniProtKB IDP00749
UniProtKB Entry NameUROK_HUMAN
GenBank Protein ID1834524
GenBank Gene IDX02419
GenAtlas IDPLAU
HGNC IDHGNC:9052
General References
  1. Jacobs P, Cravador A, Loriau R, Brockly F, Colau B, Chuchana P, van Elsen A, Herzog A, Bollen A: Molecular cloning, sequencing, and expression in Escherichia coli of human preprourokinase cDNA. DNA. 1985 Apr;4(2):139-46. [Article]
  2. Nagai M, Hiramatsu R, Kaneda T, Hayasuke N, Arimura H, Nishida M, Suyama T: Molecular cloning of cDNA coding for human preprourokinase. Gene. 1985;36(1-2):183-8. [Article]
  3. Riccio A, Grimaldi G, Verde P, Sebastio G, Boast S, Blasi F: The human urokinase-plasminogen activator gene and its promoter. Nucleic Acids Res. 1985 Apr 25;13(8):2759-71. [Article]
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  7. Yoshimoto M, Ushiyama Y, Sakai M, Tamaki S, Hara H, Takahashi K, Sawasaki Y, Hanada K: Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure. Biochim Biophys Acta. 1996 Mar 7;1293(1):83-9. [Article]
  8. Buko AM, Kentzer EJ, Petros A, Menon G, Zuiderweg ER, Sarin VK: Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3992-6. [Article]
  9. Verde P, Stoppelli MP, Galeffi P, Di Nocera P, Blasi F: Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4727-31. [Article]
  10. Gunzler WA, Steffens GJ, Otting F, Kim SM, Frankus E, Flohe L: The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. Hoppe Seylers Z Physiol Chem. 1982 Oct;363(10):1155-65. [Article]
  11. Schaller J, Nick H, Rickli EE, Gillessen D, Lergier W, Studer RO: Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains. Eur J Biochem. 1982 Jul;125(2):251-7. [Article]
  12. Steffens GJ, Gunzler WA, Otting F, Frankus E, Flohe L: The complete amino acid sequence of low molecular mass urokinase from human urine. Hoppe Seylers Z Physiol Chem. 1982 Sep;363(9):1043-58. [Article]
  13. Stief TW, Radtke KP, Heimburger N: Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for identity of PCI and plasminogen activator inhibitor 3. Biol Chem Hoppe Seyler. 1987 Oct;368(10):1427-33. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00594AmilorideapprovedunknowninhibitorDetails
DB019776-(N-Phenylcarbamyl)-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB023986-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB024736-[N-(1-Isopropyl-3,4-Dihydro-7-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB025516-[N-(4-Ethyl-1,2,3,4-Tetrahydro-6-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB027056-[N-(1-Isopropyl-1,2,3,4-Tetrahydro-7-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB030467-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-CarboximidamideexperimentalunknownDetails
DB030826-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-NaphthamideexperimentalunknownDetails
DB03127BenzamidineexperimentalunknownDetails
DB03476Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-CarboxamidineexperimentalunknownDetails
DB037292-Amino-1H-benzimidazol-5-olexperimentalunknownDetails
DB03782N-(1-adamantyl)-N'-(4-guanidinobenzyl)ureaexperimentalunknownDetails
DB040598-(Pyrimidin-2-Ylamino)Naphthalene-2-CarboximidamideexperimentalunknownDetails
DB04172[2,4,6-Triisopropyl-Phenylsulfonyl-L-[3-Amidino-Phenylalanine]]-Piperazine-N'-Beta-AlanineexperimentalunknownDetails
DB05254FibrinolysininvestigationalunknownDetails
DB019052-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-CarboxamidineexperimentalunknownDetails
DB017252-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamideexperimentalunknownDetails
DB038656-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-CarboxamidineexperimentalunknownDetails
DB068556-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidineexperimentalunknownDetails
DB068566-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINEexperimentalunknownDetails
DB06857N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDEexperimentalunknownDetails
DB070766-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDEexperimentalunknownDetails
DB071221-[4-(2-oxo-2-phenylethyl)phenyl]guanidineexperimentalunknownDetails
DB07129(2R)-1-(2,6-dimethylphenoxy)propan-2-amineexperimentalunknownDetails
DB02526CRA_10655experimentalunknownDetails
DB03159CRA_8696experimentalunknownDetails
DB022872-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidineexperimentalunknownDetails
DB076254-(2-aminoethoxy)-N-(2,5-diethoxyphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails
DB076264-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails
DB031364-Iodobenzo[B]Thiophene-2-CarboxamidineexperimentalunknownDetails
DB03876Thieno[2,3-B]Pyridine-2-CarboxamidineexperimentalunknownDetails
DB080724-(2-AMINOETHOXY)-3,5-DICHLORO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDEexperimentalunknownDetails
DB086974-(2-aminoethoxy)-N-(3-chloro-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails
DB16701PlasminogenapprovedunknownsubstrateDetails