ID UROK_HUMAN Reviewed; 431 AA. AC P00749; B4DPZ2; Q15844; Q16618; Q53XS3; Q5SWW9; Q969W6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 2. DT 13-FEB-2019, entry version 238. DE RecName: Full=Urokinase-type plasminogen activator; DE Short=U-plasminogen activator; DE Short=uPA; DE EC=3.4.21.73; DE Contains: DE RecName: Full=Urokinase-type plasminogen activator long chain A; DE Contains: DE RecName: Full=Urokinase-type plasminogen activator short chain A; DE Contains: DE RecName: Full=Urokinase-type plasminogen activator chain B; DE Flags: Precursor; GN Name=PLAU; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Holmes W.E., Pennica D., Blaber M., Rey M.W., Guenzler W.A., RA Steffens G.J., Heyneker H.L.; RT "Cloning and expression of the gene for pro-urokinase in Escherichia RT coli."; RL Biotechnology (N.Y.) 3:923-929(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3888571; DOI=10.1089/dna.1985.4.139; RA Jacobs P., Cravador A., Loriau R., Brockly F., Colau B., Chuchana P., RA van Elsen A., Herzog A., Bollen A.; RT "Molecular cloning, sequencing, and expression in Escherichia coli of RT human preprourokinase cDNA."; RL DNA 4:139-146(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2415429; DOI=10.1016/0378-1119(85)90084-8; RA Nagai M., Hiramatsu R., Kaneda T., Hayasuke N., Arimura H., RA Nishida M., Suyama T.; RT "Molecular cloning of cDNA coding for human preprourokinase."; RL Gene 36:183-188(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-214. RX PubMed=2987867; DOI=10.1093/nar/13.8.2759; RA Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F.; RT "The human urokinase-plasminogen activator gene and its promoter."; RL Nucleic Acids Res. 13:2759-2771(1985). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) System Donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Mesangial cell; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-15; LEU-141 AND RP GLN-231. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-141. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-431, AND VARIANT LEU-141. RX PubMed=8652631; RA Yoshimoto M., Ushiyama Y., Sakai M., Tamaki S., Hara H., Takahashi K., RA Sawasaki Y., Hanada K.; RT "Characterization of single chain urokinase-type plasminogen activator RT with a novel amino-acid substitution in the kringle structure."; RL Biochim. Biophys. Acta 1293:83-89(1996). RN [12] RP PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=2023947; DOI=10.1073/pnas.88.9.3992; RA Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R., RA Sarin V.K.; RT "Characterization of a posttranslational fucosylation in the growth RT factor domain of urinary plasminogen activator."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431, AND VARIANT RP MET-214. RX PubMed=6589620; DOI=10.1073/pnas.81.15.4727; RA Verde P., Stoppelli M.P., Galeffi P., di Nocera P., Blasi F.; RT "Identification and primary sequence of an unspliced human urokinase RT poly(A)+ RNA."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4727-4731(1984). RN [14] RP PROTEIN SEQUENCE OF 21-177. RX PubMed=6754569; RA Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E., RA Flohe L.; RT "The primary structure of high molecular mass urokinase from human RT urine. The complete amino acid sequence of the A chain."; RL Hoppe-Seyler's Z. Physiol. Chem. 363:1155-1165(1982). RN [15] RP PROTEIN SEQUENCE OF 156-176 AND 179-224. RX PubMed=6749491; DOI=10.1111/j.1432-1033.1982.tb06676.x; RA Schaller J., Nick H., Rickli E.E., Gillessen D., Lergier W., RA Studer R.O.; RT "Human low-molecular-weight urinary urokinase. Partial RT characterization and preliminary sequence data of the two polypeptide RT chains."; RL Eur. J. Biochem. 125:251-257(1982). RN [16] RP PROTEIN SEQUENCE OF 158-410. RX PubMed=6754572; RA Steffens G.J., Gunzler W.A., Otting F., Frankus E., Flohe L.; RT "The complete amino acid sequence of low molecular mass urokinase from RT human urine."; RL Hoppe-Seyler's Z. Physiol. Chem. 363:1043-1058(1982). RN [17] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=3501295; RA Stief T.W., Radtke K.P., Heimburger N.; RT "Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for RT identity of PCI and plasminogen activator inhibitor 3."; RL Biol. Chem. Hoppe-Seyler 368:1427-1433(1987). RN [18] RP PHOSPHORYLATION AT SER-158 AND SER-323, AND MUTAGENESIS OF SER-158 AND RP SER-323. RX PubMed=9151681; DOI=10.1083/jcb.137.3.779; RA Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C., RA Mastronicola M.R., Nolli M.L., Stoppelli M.P.; RT "Phosphorylation of human pro-urokinase on Ser138/303 impairs its RT receptor-dependent ability to promote myelomonocytic adherence and RT motility."; RL J. Cell Biol. 137:779-791(1997). RN [19] RP HETERODIMER WITH SERPINA5. RX PubMed=10340997; DOI=10.1093/molehr/5.6.513; RA He S., Lin Y.L., Liu Y.X.; RT "Functionally inactive protein C inhibitor in seminal plasma may be RT associated with infertility."; RL Mol. Hum. Reprod. 5:513-519(1999). RN [20] RP INTERACTION WITH MRC2. RX PubMed=10636902; DOI=10.1074/jbc.275.3.1993; RA Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., RA Danoe K.; RT "A urokinase receptor-associated protein with specific collagen RT binding properties."; RL J. Biol. Chem. 275:1993-2002(2000). RN [21] RP INTERACTION WITH LRP1B. RX PubMed=11384978; DOI=10.1074/jbc.M102727200; RA Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.; RT "The putative tumor suppressor LRP1B, a novel member of the low RT density lipoprotein (LDL) receptor family, exhibits both overlapping RT and distinct properties with the LDL receptor-related protein."; RL J. Biol. Chem. 276:28889-28896(2001). RN [22] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=14696115; DOI=10.1002/ijc.11594; RA Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., RA Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.; RT "Regulation of carcinoma cell invasion by protein C inhibitor whose RT expression is decreased in renal cell carcinoma."; RL Int. J. Cancer 108:516-523(2004). RN [23] RP TISSUE SPECIFICITY. RX PubMed=15988036; DOI=10.1128/MCB.25.14.6279-6288.2005; RA Ustach C.V., Kim H.-R.C.; RT "Platelet-derived growth factor D is activated by urokinase RT plasminogen activator in prostate carcinoma cells."; RL Mol. Cell. Biol. 25:6279-6288(2005). RN [24] RP INVOLVEMENT IN QPD. RX PubMed=20007542; DOI=10.1182/blood-2009-07-233965; RA Paterson A.D., Rommens J.M., Bharaj B., Blavignac J., Wong I., RA Diamandis M., Waye J.S., Rivard G.E., Hayward C.P.; RT "Persons with Quebec platelet disorder have a tandem duplication of RT PLAU, the urokinase plasminogen activator gene."; RL Blood 115:1264-1266(2010). RN [25] RP STRUCTURE BY NMR. RX PubMed=2536903; DOI=10.1038/337579a0; RA Oswald R.E., Bogusky M.J., Bamberger M., Smith R.A.G., Dobson C.M.; RT "Dynamics of the multidomain fibrinolytic protein urokinase from two- RT dimensional NMR."; RL Nature 337:579-582(1989). RN [26] RP STRUCTURE BY NMR OF 67-155. RX PubMed=1327118; DOI=10.1021/bi00155a008; RA Li X., Smith R.A.G., Dobson C.M.; RT "Sequential 1H NMR assignments and secondary structure of the kringle RT domain from urokinase."; RL Biochemistry 31:9562-9571(1992). RN [27] RP STRUCTURE BY NMR OF 67-155. RX PubMed=8107091; DOI=10.1006/jmbi.1994.1106; RA Li X., Bokman A.M., Llinas M., Smith R.A.G., Dobson C.M.; RT "Solution structure of the kringle domain from urokinase-type RT plasminogen activator."; RL J. Mol. Biol. 235:1548-1559(1994). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8591045; DOI=10.1016/S0969-2126(01)00203-9; RA Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D., RA Dobson C.M., Stuart D.I., Jones E.Y.; RT "The crystal structure of the catalytic domain of human urokinase-type RT plasminogen activator."; RL Structure 3:681-691(1995). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411. RX PubMed=10805774; DOI=10.1073/pnas.97.10.5113; RA Sperl S., Jacob U., Arroyo de Prada N., Sturzebecher J., Wilhelm O.G., RA Bode W., Magdolen V., Huber R., Moroder L.; RT "(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly RT selective inhibitors of human urokinase."; RL Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-152 IN COMPLEX WITH PLAUR. RX PubMed=16456079; DOI=10.1126/science.1121143; RA Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J., RA Li Y., Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B., RA Huang M.; RT "Structure of human urokinase plasminogen activator in complex with RT its receptor."; RL Science 311:656-659(2006). RN [31] RP VARIANT LEU-141. RX PubMed=9065988; RA Conne B., Berczy M., Belin D.; RT "Detection of polymorphisms in the human urokinase-type plasminogen RT activator gene."; RL Thromb. Haemost. 77:434-435(1997). RN [32] RP ERRATUM. RA Conne B., Berczy M., Belin D.; RL Thromb. Haemost. 78:973-973(1997). RN [33] RP VARIANT LEU-141. RX PubMed=9194591; DOI=10.1002/elps.1150180505; RA Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., RA Creutzburg S., Graeff H., Magdolen V.; RT "Mutational analysis of the genes encoding urokinase-type plasminogen RT activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer."; RL Electrophoresis 18:686-689(1997). RN [34] RP VARIANT [LARGE SCALE ANALYSIS] LEU-141. RX PubMed=18987736; DOI=10.1038/nature07485; RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., RA Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., RA Graubert T.A., DiPersio J.F., Wilson R.K.; RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia RT genome."; RL Nature 456:66-72(2008). CC -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the CC active enzyme plasmin. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to CC form plasmin.; EC=3.4.21.73; CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. CC {ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:3501295}. CC -!- SUBUNIT: Found in high and low molecular mass forms. Each consists CC of two chains, A and B. The high molecular mass form contains a CC long chain A which is cleaved to yield a short chain A. Forms CC heterodimer with SERPINA5. Binds LRP1B; binding is followed by CC internalization and degradation. Interacts with MRC2. Interacts CC with PLAUR. {ECO:0000269|PubMed:10636902, CC ECO:0000269|PubMed:11384978, ECO:0000269|PubMed:16456079}. CC -!- INTERACTION: CC Q03405-1:PLAUR; NbExp=2; IntAct=EBI-3905042, EBI-15695188; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P00749-1; Sequence=Displayed; CC Name=2; CC IsoId=P00749-2; Sequence=VSP_038368; CC -!- TISSUE SPECIFICITY: Expressed in the prostate gland and prostate CC cancers. {ECO:0000269|PubMed:15988036}. CC -!- PTM: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive CC ability but does not interfere with receptor binding. CC {ECO:0000269|PubMed:9151681}. CC -!- DISEASE: Quebec platelet disorder (QPD) [MIM:601709]: An autosomal CC dominant bleeding disorder due to a gain-of-function defect in CC fibrinolysis. Although affected individuals do not exhibit CC systemic fibrinolysis, they show delayed onset bleeding after CC challenge, such as surgery. The hallmark of the disorder is CC markedly increased PLAU levels within platelets, which causes CC intraplatelet plasmin generation and secondary degradation of CC alpha-granule proteins. {ECO:0000269|PubMed:20007542}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- PHARMACEUTICAL: Available under the name Abbokinase (Abbott). Used CC in Pulmonary Embolism (PE) to initiate fibrinolysis. Clinically CC used for therapy of thrombolytic disorders. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Urokinase entry; CC URL="https://en.wikipedia.org/wiki/Urokinase"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/plau/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M15476; AAA61253.1; -; mRNA. DR EMBL; X02760; CAA26535.1; -; mRNA. DR EMBL; D00244; BAA00175.1; -; mRNA. DR EMBL; K03226; AAC97138.1; -; mRNA. DR EMBL; X02419; CAA26268.1; -; Genomic_DNA. DR EMBL; AF377330; AAK53822.1; -; Genomic_DNA. DR EMBL; BT007391; AAP36055.1; -; mRNA. DR EMBL; AK298560; BAG60754.1; -; mRNA. DR EMBL; AL596247; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54544.1; -; Genomic_DNA. DR EMBL; BC013575; AAH13575.1; -; mRNA. DR EMBL; D11143; BAA01919.1; -; mRNA. DR EMBL; K02286; AAA61252.1; -; Genomic_DNA. DR CCDS; CCDS44442.1; -. [P00749-2] DR CCDS; CCDS7339.1; -. [P00749-1] DR PIR; A00931; UKHU. DR RefSeq; NP_001138503.1; NM_001145031.2. [P00749-2] DR RefSeq; NP_001306120.1; NM_001319191.1. DR RefSeq; NP_002649.1; NM_002658.4. [P00749-1] DR UniGene; Hs.77274; -. DR PDB; 1C5W; X-ray; 1.94 A; A=156-178, B=179-431. DR PDB; 1C5X; X-ray; 1.75 A; A=156-178, B=179-431. DR PDB; 1C5Y; X-ray; 1.65 A; A=156-178, B=179-431. DR PDB; 1C5Z; X-ray; 1.85 A; A=156-178, B=179-431. DR PDB; 1EJN; X-ray; 1.80 A; A=179-431. DR PDB; 1F5K; X-ray; 1.80 A; U=179-431. DR PDB; 1F5L; X-ray; 2.10 A; A=179-431. DR PDB; 1F92; X-ray; 2.60 A; A=179-431. DR PDB; 1FV9; X-ray; 3.00 A; A=179-423. DR PDB; 1GI7; X-ray; 1.79 A; A=156-178, B=179-423. DR PDB; 1GI8; X-ray; 1.75 A; A=156-178, B=179-423. DR PDB; 1GI9; X-ray; 1.80 A; A=156-178, B=179-423. DR PDB; 1GJ7; X-ray; 1.50 A; A=156-178, B=179-431. DR PDB; 1GJ8; X-ray; 1.64 A; A=156-178, B=179-431. DR PDB; 1GJ9; X-ray; 1.80 A; A=156-178, B=179-431. DR PDB; 1GJA; X-ray; 1.56 A; A=156-178, B=179-431. DR PDB; 1GJB; X-ray; 1.90 A; A=156-178, B=179-431. DR PDB; 1GJC; X-ray; 1.73 A; A=156-178, B=179-431. DR PDB; 1GJD; X-ray; 1.75 A; A=156-178, B=179-431. DR PDB; 1KDU; NMR; -; A=69-153. DR PDB; 1LMW; X-ray; 2.50 A; A/C=156-178, B/D=179-431. DR PDB; 1O3P; X-ray; 1.81 A; A=156-178, B=179-431. DR PDB; 1O5A; X-ray; 1.68 A; A=156-178, B=179-431. DR PDB; 1O5B; X-ray; 1.85 A; A=156-178, B=179-431. DR PDB; 1O5C; X-ray; 1.63 A; A=156-178, B=179-431. DR PDB; 1OWD; X-ray; 2.32 A; A=179-423. DR PDB; 1OWE; X-ray; 1.60 A; A=179-423. DR PDB; 1OWH; X-ray; 1.61 A; A=179-423. DR PDB; 1OWI; X-ray; 2.93 A; A=179-423. DR PDB; 1OWJ; X-ray; 3.10 A; A=179-423. DR PDB; 1OWK; X-ray; 2.80 A; A=179-423. DR PDB; 1SC8; X-ray; 2.40 A; U=164-425. DR PDB; 1SQA; X-ray; 2.00 A; A=179-423. DR PDB; 1SQO; X-ray; 1.84 A; A=179-423. DR PDB; 1SQT; X-ray; 1.90 A; A=179-423. DR PDB; 1U6Q; X-ray; 2.02 A; A=179-423. DR PDB; 1URK; NMR; -; A=26-155. DR PDB; 1VJ9; X-ray; 2.40 A; U=164-425. DR PDB; 1VJA; X-ray; 2.00 A; U=164-425. DR PDB; 1W0Z; X-ray; 1.90 A; U=179-425. DR PDB; 1W10; X-ray; 2.00 A; U=179-425. DR PDB; 1W11; X-ray; 2.00 A; U=179-425. DR PDB; 1W12; X-ray; 2.40 A; U=179-425. DR PDB; 1W13; X-ray; 2.00 A; U=179-425. DR PDB; 1W14; X-ray; 2.20 A; U=179-425. DR PDB; 2FD6; X-ray; 1.90 A; A=31-152. DR PDB; 2I9A; X-ray; 1.90 A; A/B/C/D=21-163. DR PDB; 2I9B; X-ray; 2.80 A; A/B/C/D=21-163. DR PDB; 2NWN; X-ray; 2.15 A; A=179-431. DR PDB; 2O8T; X-ray; 1.45 A; A=179-431. DR PDB; 2O8U; X-ray; 1.70 A; A=179-431. DR PDB; 2O8W; X-ray; 1.86 A; A=179-431. DR PDB; 2R2W; X-ray; 2.01 A; U=179-431. DR PDB; 2VIN; X-ray; 1.90 A; A=179-431. DR PDB; 2VIO; X-ray; 1.80 A; A=179-431. DR PDB; 2VIP; X-ray; 1.72 A; A=179-431. DR PDB; 2VIQ; X-ray; 2.00 A; A=179-431. DR PDB; 2VIV; X-ray; 1.72 A; A=179-431. DR PDB; 2VIW; X-ray; 2.05 A; A=179-431. DR PDB; 2VNT; X-ray; 2.20 A; A/B/C/D/E/F=156-431. DR PDB; 3BT1; X-ray; 2.80 A; A=21-153. DR PDB; 3BT2; X-ray; 2.50 A; A=21-153. DR PDB; 3IG6; X-ray; 1.83 A; A/C=156-178, B/D=179-431. DR PDB; 3KGP; X-ray; 2.35 A; A=179-431. DR PDB; 3KHV; X-ray; 2.35 A; A=179-431. DR PDB; 3KID; X-ray; 2.71 A; U=179-431. DR PDB; 3M61; X-ray; 1.68 A; U=179-431. DR PDB; 3MHW; X-ray; 1.45 A; U=179-425. DR PDB; 3MWI; X-ray; 2.03 A; U=179-424. DR PDB; 3OX7; X-ray; 1.58 A; U=179-431. DR PDB; 3OY5; X-ray; 2.31 A; U=179-431. DR PDB; 3OY6; X-ray; 2.31 A; U=179-431. DR PDB; 3PB1; X-ray; 2.30 A; E=179-431. DR PDB; 3QN7; X-ray; 1.90 A; A=179-431. DR PDB; 3U73; X-ray; 3.19 A; A=21-152. DR PDB; 4DVA; X-ray; 1.94 A; U=179-424. DR PDB; 4DW2; X-ray; 2.97 A; U=179-424. DR PDB; 4FU7; X-ray; 2.00 A; A=179-424. DR PDB; 4FU8; X-ray; 2.20 A; A=179-424. DR PDB; 4FU9; X-ray; 1.60 A; A=179-424. DR PDB; 4FUB; X-ray; 1.90 A; A=179-424. DR PDB; 4FUC; X-ray; 1.72 A; A=179-424. DR PDB; 4FUD; X-ray; 2.00 A; A=179-424. DR PDB; 4FUE; X-ray; 2.00 A; A=179-424. DR PDB; 4FUF; X-ray; 2.00 A; A=179-424. DR PDB; 4FUG; X-ray; 1.80 A; A=179-424. DR PDB; 4FUH; X-ray; 1.60 A; A=179-424. DR PDB; 4FUI; X-ray; 2.00 A; A=179-424. DR PDB; 4FUJ; X-ray; 2.05 A; A=179-424. DR PDB; 4GLY; X-ray; 1.52 A; A=179-423. DR PDB; 4H42; X-ray; 2.01 A; U=179-426. DR PDB; 4JK5; X-ray; 1.55 A; A=179-423. DR PDB; 4JK6; X-ray; 2.20 A; A=179-423. DR PDB; 4K24; X-ray; 4.50 A; A=21-153. DR PDB; 4MNV; X-ray; 1.80 A; A=179-423. DR PDB; 4MNW; X-ray; 1.49 A; A=179-423. DR PDB; 4MNX; X-ray; 1.85 A; A=179-423. DR PDB; 4MNY; X-ray; 1.70 A; A/B=179-423. DR PDB; 4OS1; X-ray; 2.20 A; A=179-423. DR PDB; 4OS2; X-ray; 1.79 A; A=179-423. DR PDB; 4OS4; X-ray; 2.00 A; A=179-423. DR PDB; 4OS5; X-ray; 2.26 A; A=179-423. DR PDB; 4OS6; X-ray; 1.75 A; A=179-423. DR PDB; 4OS7; X-ray; 2.00 A; A=179-423. DR PDB; 4X0W; X-ray; 2.10 A; U=179-425. DR PDB; 4X1N; X-ray; 1.80 A; U=179-425. DR PDB; 4X1P; X-ray; 1.60 A; U=179-425. DR PDB; 4X1Q; X-ray; 2.28 A; U=179-425. DR PDB; 4X1R; X-ray; 2.10 A; U=179-425. DR PDB; 4X1S; X-ray; 1.90 A; U=179-425. DR PDB; 4XSK; X-ray; 1.50 A; U=179-424. DR PDB; 4ZHL; X-ray; 2.06 A; U=179-425. DR PDB; 4ZHM; X-ray; 1.90 A; U=179-425. DR PDB; 4ZKN; X-ray; 1.36 A; U=179-425. DR PDB; 4ZKO; X-ray; 1.29 A; U=179-425. DR PDB; 4ZKR; X-ray; 1.36 A; U=179-425. DR PDB; 4ZKS; X-ray; 1.85 A; U=179-425. DR PDB; 5HGG; X-ray; 1.97 A; A/B=179-424. DR PDB; 5WXF; X-ray; 1.46 A; U=179-431. DR PDB; 5WXO; X-ray; 1.64 A; U=179-431. DR PDB; 5WXP; X-ray; 1.75 A; U=179-431. DR PDB; 5WXQ; X-ray; 1.79 A; U=179-431. DR PDB; 5WXR; X-ray; 1.75 A; U=179-431. DR PDB; 5WXS; X-ray; 2.30 A; U=179-431. DR PDB; 5WXT; X-ray; 2.10 A; U=179-431. DR PDB; 5XG4; X-ray; 3.00 A; U=179-424. DR PDB; 5YC6; X-ray; 1.18 A; U=179-424. DR PDB; 5YC7; X-ray; 2.00 A; U=179-424. DR PDB; 5Z1C; X-ray; 1.45 A; U=179-423. DR PDB; 5ZA7; X-ray; 1.70 A; U=179-431. DR PDB; 5ZA8; X-ray; 1.90 A; U=179-431. DR PDB; 5ZA9; X-ray; 1.62 A; U=179-431. DR PDB; 5ZAE; X-ray; 1.73 A; U=179-431. DR PDB; 5ZAF; X-ray; 1.65 A; U=179-431. DR PDB; 5ZAG; X-ray; 1.95 A; U=179-431. DR PDB; 5ZAH; X-ray; 2.98 A; U=179-431. DR PDB; 5ZAJ; X-ray; 1.65 A; U=179-431. DR PDB; 5ZC5; X-ray; 1.90 A; U=179-431. DR PDBsum; 1C5W; -. DR PDBsum; 1C5X; -. DR PDBsum; 1C5Y; -. DR PDBsum; 1C5Z; -. DR PDBsum; 1EJN; -. DR PDBsum; 1F5K; -. DR PDBsum; 1F5L; -. DR PDBsum; 1F92; -. DR PDBsum; 1FV9; -. DR PDBsum; 1GI7; -. DR PDBsum; 1GI8; -. DR PDBsum; 1GI9; -. DR PDBsum; 1GJ7; -. DR PDBsum; 1GJ8; -. DR PDBsum; 1GJ9; -. DR PDBsum; 1GJA; -. DR PDBsum; 1GJB; -. DR PDBsum; 1GJC; -. DR PDBsum; 1GJD; -. DR PDBsum; 1KDU; -. DR PDBsum; 1LMW; -. DR PDBsum; 1O3P; -. DR PDBsum; 1O5A; -. DR PDBsum; 1O5B; -. DR PDBsum; 1O5C; -. DR PDBsum; 1OWD; -. DR PDBsum; 1OWE; -. DR PDBsum; 1OWH; -. DR PDBsum; 1OWI; -. DR PDBsum; 1OWJ; -. DR PDBsum; 1OWK; -. DR PDBsum; 1SC8; -. DR PDBsum; 1SQA; -. DR PDBsum; 1SQO; -. DR PDBsum; 1SQT; -. DR PDBsum; 1U6Q; -. DR PDBsum; 1URK; -. DR PDBsum; 1VJ9; -. DR PDBsum; 1VJA; -. DR PDBsum; 1W0Z; -. DR PDBsum; 1W10; -. DR PDBsum; 1W11; -. DR PDBsum; 1W12; -. DR PDBsum; 1W13; -. DR PDBsum; 1W14; -. DR PDBsum; 2FD6; -. DR PDBsum; 2I9A; -. DR PDBsum; 2I9B; -. DR PDBsum; 2NWN; -. DR PDBsum; 2O8T; -. DR PDBsum; 2O8U; -. DR PDBsum; 2O8W; -. DR PDBsum; 2R2W; -. DR PDBsum; 2VIN; -. DR PDBsum; 2VIO; -. DR PDBsum; 2VIP; -. DR PDBsum; 2VIQ; -. DR PDBsum; 2VIV; -. DR PDBsum; 2VIW; -. DR PDBsum; 2VNT; -. DR PDBsum; 3BT1; -. DR PDBsum; 3BT2; -. DR PDBsum; 3IG6; -. DR PDBsum; 3KGP; -. DR PDBsum; 3KHV; -. DR PDBsum; 3KID; -. DR PDBsum; 3M61; -. DR PDBsum; 3MHW; -. DR PDBsum; 3MWI; -. DR PDBsum; 3OX7; -. DR PDBsum; 3OY5; -. DR PDBsum; 3OY6; -. DR PDBsum; 3PB1; -. DR PDBsum; 3QN7; -. DR PDBsum; 3U73; -. DR PDBsum; 4DVA; -. DR PDBsum; 4DW2; -. DR PDBsum; 4FU7; -. DR PDBsum; 4FU8; -. DR PDBsum; 4FU9; -. DR PDBsum; 4FUB; -. DR PDBsum; 4FUC; -. DR PDBsum; 4FUD; -. DR PDBsum; 4FUE; -. DR PDBsum; 4FUF; -. DR PDBsum; 4FUG; -. DR PDBsum; 4FUH; -. DR PDBsum; 4FUI; -. DR PDBsum; 4FUJ; -. DR PDBsum; 4GLY; -. DR PDBsum; 4H42; -. DR PDBsum; 4JK5; -. DR PDBsum; 4JK6; -. DR PDBsum; 4K24; -. DR PDBsum; 4MNV; -. DR PDBsum; 4MNW; -. DR PDBsum; 4MNX; -. DR PDBsum; 4MNY; -. DR PDBsum; 4OS1; -. DR PDBsum; 4OS2; -. DR PDBsum; 4OS4; -. DR PDBsum; 4OS5; -. DR PDBsum; 4OS6; -. DR PDBsum; 4OS7; -. DR PDBsum; 4X0W; -. DR PDBsum; 4X1N; -. DR PDBsum; 4X1P; -. DR PDBsum; 4X1Q; -. DR PDBsum; 4X1R; -. DR PDBsum; 4X1S; -. DR PDBsum; 4XSK; -. DR PDBsum; 4ZHL; -. DR PDBsum; 4ZHM; -. DR PDBsum; 4ZKN; -. DR PDBsum; 4ZKO; -. DR PDBsum; 4ZKR; -. DR PDBsum; 4ZKS; -. DR PDBsum; 5HGG; -. DR PDBsum; 5WXF; -. DR PDBsum; 5WXO; -. DR PDBsum; 5WXP; -. DR PDBsum; 5WXQ; -. DR PDBsum; 5WXR; -. DR PDBsum; 5WXS; -. DR PDBsum; 5WXT; -. DR PDBsum; 5XG4; -. DR PDBsum; 5YC6; -. DR PDBsum; 5YC7; -. DR PDBsum; 5Z1C; -. DR PDBsum; 5ZA7; -. DR PDBsum; 5ZA8; -. DR PDBsum; 5ZA9; -. DR PDBsum; 5ZAE; -. DR PDBsum; 5ZAF; -. DR PDBsum; 5ZAG; -. DR PDBsum; 5ZAH; -. DR PDBsum; 5ZAJ; -. DR PDBsum; 5ZC5; -. DR ProteinModelPortal; P00749; -. DR SMR; P00749; -. DR BioGrid; 111344; 21. DR ComplexPortal; CPX-483; uPA-PAI-1 complex. DR ComplexPortal; CPX-487; uPA-uPAR complex. DR ComplexPortal; CPX-501; uPA-uPAR-vitronectin complex. DR CORUM; P00749; -. DR DIP; DIP-46387N; -. DR ELM; P00749; -. DR IntAct; P00749; 9. DR MINT; P00749; -. DR STRING; 9606.ENSP00000361850; -. DR BindingDB; P00749; -. DR ChEMBL; CHEMBL3286; -. DR DrugBank; DB07122; 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine. DR DrugBank; DB01905; 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine. DR DrugBank; DB06854; 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE. DR DrugBank; DB02193; 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine. DR DrugBank; DB03729; 2-Amino-5-Hydroxy-Benzimidazole. DR DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine. DR DrugBank; DB01977; 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine. DR DrugBank; DB07076; 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE. DR DrugBank; DB03082; 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide. DR DrugBank; DB02398; 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine. DR DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine. DR DrugBank; DB06855; 6-FLUORO-2-(2-HYDROXY-3-ISOBUTOXY-PHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE. DR DrugBank; DB06856; 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE. DR DrugBank; DB03046; 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide. DR DrugBank; DB04059; 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide. DR DrugBank; DB00594; Amiloride. DR DrugBank; DB03127; Benzamidine. DR DrugBank; DB02526; CRA_10655. DR DrugBank; DB03159; CRA_8696. DR DrugBank; DB03782; N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea. DR DrugBank; DB06857; N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE. DR DrugBank; DB05254; Plasmin. DR DrugBank; DB03476; Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine. DR DrugBank; DB00013; Urokinase. DR GuidetoPHARMACOLOGY; 2393; -. DR MEROPS; S01.231; -. DR GlyConnect; 519; -. DR GlyConnect; 612; -. DR iPTMnet; P00749; -. DR PhosphoSitePlus; P00749; -. DR UniCarbKB; P00749; -. DR BioMuta; PLAU; -. DR DMDM; 254763341; -. DR EPD; P00749; -. DR jPOST; P00749; -. DR MaxQB; P00749; -. DR PaxDb; P00749; -. DR PeptideAtlas; P00749; -. DR PRIDE; P00749; -. DR ProteomicsDB; 51279; -. DR ProteomicsDB; 51280; -. [P00749-2] DR DNASU; 5328; -. DR Ensembl; ENST00000372764; ENSP00000361850; ENSG00000122861. DR Ensembl; ENST00000496777; ENSP00000431795; ENSG00000122861. DR GeneID; 5328; -. DR KEGG; hsa:5328; -. DR UCSC; uc001jwa.4; human. [P00749-1] DR CTD; 5328; -. DR DisGeNET; 5328; -. DR EuPathDB; HostDB:ENSG00000122861.15; -. DR GeneCards; PLAU; -. DR HGNC; HGNC:9052; PLAU. DR HPA; HPA008719; -. DR MalaCards; PLAU; -. DR MIM; 191840; gene. DR MIM; 601709; phenotype. DR neXtProt; NX_P00749; -. DR Orphanet; 220436; Quebec platelet disorder. DR PharmGKB; PA33382; -. DR eggNOG; ENOG410IGFI; Eukaryota. DR eggNOG; COG5640; LUCA. DR HOVERGEN; HBG008633; -. DR InParanoid; P00749; -. DR KO; K01348; -. DR OrthoDB; 972218at2759; -. DR PhylomeDB; P00749; -. DR TreeFam; TF329901; -. DR BRENDA; 3.4.21.73; 2681. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot. DR SABIO-RK; P00749; -. DR SIGNOR; P00749; -. DR EvolutionaryTrace; P00749; -. DR GeneWiki; PLAU; -. DR GenomeRNAi; 5328; -. DR PMAP-CutDB; P00749; -. DR PRO; PR:P00749; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000122861; Expressed in 181 organ(s), highest expression level in epithelium of bronchus. DR ExpressionAtlas; P00749; baseline and differential. DR Genevisible; P00749; HS. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0042730; P:fibrinolysis; IBA:GO_Central. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0031639; P:plasminogen activation; IDA:AgBase. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:BHF-UCL. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:BHF-UCL. DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL. DR GO; GO:2000097; P:regulation of smooth muscle cell-matrix adhesion; IDA:BHF-UCL. DR GO; GO:0061041; P:regulation of wound healing; IC:BHF-UCL. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl. DR CDD; cd00108; KR; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; -; 1. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR InterPro; IPR034814; Urokinase. DR PANTHER; PTHR24264:SF38; PTHR24264:SF38; 1. DR Pfam; PF00051; Kringle; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00130; KR; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57440; SSF57440; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS00021; KRINGLE_1; 1. DR PROSITE; PS50070; KRINGLE_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood coagulation; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW EGF-like domain; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase; KW Kringle; Pharmaceutical; Phosphoprotein; Plasminogen activation; KW Polymorphism; Protease; Reference proteome; Secreted; Serine protease; KW Signal; Zymogen. FT SIGNAL 1 20 {ECO:0000269|PubMed:2023947, FT ECO:0000269|PubMed:6754569}. FT CHAIN 21 431 Urokinase-type plasminogen activator. FT /FTId=PRO_0000028318. FT CHAIN 21 177 Urokinase-type plasminogen activator long FT chain A. FT /FTId=PRO_0000028319. FT CHAIN 156 177 Urokinase-type plasminogen activator FT short chain A. FT /FTId=PRO_0000028320. FT CHAIN 179 431 Urokinase-type plasminogen activator FT chain B. FT /FTId=PRO_0000028321. FT DOMAIN 27 63 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 70 151 Kringle. {ECO:0000255|PROSITE- FT ProRule:PRU00121}. FT DOMAIN 179 424 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT REGION 34 57 Binds urokinase plasminogen activator FT surface receptor. {ECO:0000250}. FT REGION 152 177 Connecting peptide. FT ACT_SITE 224 224 Charge relay system. FT ACT_SITE 275 275 Charge relay system. FT ACT_SITE 376 376 Charge relay system. FT SITE 177 178 Cleavage; during zymogen activation. FT MOD_RES 158 158 Phosphoserine. FT {ECO:0000269|PubMed:9151681}. FT MOD_RES 323 323 Phosphoserine. FT {ECO:0000269|PubMed:9151681}. FT CARBOHYD 38 38 O-linked (Fuc) threonine. FT {ECO:0000269|PubMed:2023947}. FT CARBOHYD 322 322 N-linked (GlcNAc...) asparagine. FT /FTId=CAR_000026. FT DISULFID 31 39 FT DISULFID 33 51 FT DISULFID 53 62 FT DISULFID 70 151 FT DISULFID 91 133 FT DISULFID 122 146 FT DISULFID 168 299 Interchain (between A and B chains). FT DISULFID 209 225 FT DISULFID 217 288 FT DISULFID 313 382 FT DISULFID 345 361 FT DISULFID 372 400 FT VAR_SEQ 1 29 MRALLARLLLCVLVVSDSKGSNELHQVPS -> MVFHLRTR FT YEQA (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038368. FT VARIANT 15 15 V -> L (in dbSNP:rs2227580). FT {ECO:0000269|Ref.7}. FT /FTId=VAR_038730. FT VARIANT 141 141 P -> L (in dbSNP:rs2227564). FT {ECO:0000269|PubMed:15164054, FT ECO:0000269|PubMed:18987736, FT ECO:0000269|PubMed:8652631, FT ECO:0000269|PubMed:9065988, FT ECO:0000269|PubMed:9194591, FT ECO:0000269|Ref.7}. FT /FTId=VAR_006722. FT VARIANT 214 214 I -> M. {ECO:0000269|PubMed:2987867, FT ECO:0000269|PubMed:6589620}. FT /FTId=VAR_013102. FT VARIANT 231 231 K -> Q (in dbSNP:rs2227567). FT {ECO:0000269|Ref.7}. FT /FTId=VAR_038731. FT MUTAGEN 158 158 S->E: Abolishes phosphorylation, FT proadhesive function and ability to FT induce chemotactic response; when FT associated with E-323. FT {ECO:0000269|PubMed:9151681}. FT MUTAGEN 323 323 S->E: Abolishes phosphorylation, FT proadhesive function and ability to FT induce chemotactic response; when FT associated with E-158. FT {ECO:0000269|PubMed:9151681}. FT CONFLICT 150 150 D -> G (in Ref. 6; BAG60754). FT {ECO:0000305}. FT CONFLICT 151 151 C -> W (in Ref. 2; CAA26535). FT {ECO:0000305}. FT CONFLICT 386 386 G -> C (in Ref. 2; CAA26535). FT {ECO:0000305}. FT CONFLICT 430 430 A -> V (in Ref. 2; CAA26535). FT {ECO:0000305}. FT STRAND 34 36 {ECO:0000244|PDB:1URK}. FT STRAND 38 41 {ECO:0000244|PDB:2FD6}. FT TURN 43 47 {ECO:0000244|PDB:2FD6}. FT STRAND 49 52 {ECO:0000244|PDB:2FD6}. FT STRAND 57 59 {ECO:0000244|PDB:2FD6}. FT STRAND 64 67 {ECO:0000244|PDB:2FD6}. FT STRAND 70 72 {ECO:0000244|PDB:2I9B}. FT STRAND 73 77 {ECO:0000244|PDB:3U73}. FT STRAND 86 89 {ECO:0000244|PDB:1URK}. FT STRAND 94 96 {ECO:0000244|PDB:1KDU}. FT HELIX 99 101 {ECO:0000244|PDB:2FD6}. FT STRAND 102 104 {ECO:0000244|PDB:2FD6}. FT STRAND 106 108 {ECO:0000244|PDB:3BT1}. FT HELIX 111 114 {ECO:0000244|PDB:2FD6}. FT STRAND 117 119 {ECO:0000244|PDB:2FD6}. FT STRAND 128 130 {ECO:0000244|PDB:2I9A}. FT STRAND 132 137 {ECO:0000244|PDB:2FD6}. FT STRAND 140 147 {ECO:0000244|PDB:2FD6}. FT HELIX 162 165 {ECO:0000244|PDB:1GJA}. FT STRAND 180 184 {ECO:0000244|PDB:5YC6}. FT HELIX 187 189 {ECO:0000244|PDB:5YC6}. FT STRAND 193 199 {ECO:0000244|PDB:5YC6}. FT STRAND 201 203 {ECO:0000244|PDB:4XSK}. FT STRAND 205 215 {ECO:0000244|PDB:5YC6}. FT STRAND 218 221 {ECO:0000244|PDB:5YC6}. FT HELIX 223 225 {ECO:0000244|PDB:5YC6}. FT TURN 226 228 {ECO:0000244|PDB:5YC6}. FT HELIX 232 234 {ECO:0000244|PDB:5YC6}. FT STRAND 235 240 {ECO:0000244|PDB:5YC6}. FT STRAND 243 246 {ECO:0000244|PDB:5YC6}. FT STRAND 252 261 {ECO:0000244|PDB:5YC6}. FT STRAND 268 271 {ECO:0000244|PDB:5HGG}. FT STRAND 272 274 {ECO:0000244|PDB:5YC6}. FT STRAND 277 282 {ECO:0000244|PDB:5YC6}. FT STRAND 293 295 {ECO:0000244|PDB:1LMW}. FT STRAND 312 318 {ECO:0000244|PDB:5YC6}. FT STRAND 329 331 {ECO:0000244|PDB:4DW2}. FT STRAND 333 340 {ECO:0000244|PDB:5YC6}. FT HELIX 342 345 {ECO:0000244|PDB:5YC6}. FT TURN 348 351 {ECO:0000244|PDB:5YC6}. FT HELIX 352 354 {ECO:0000244|PDB:5YC6}. FT TURN 356 358 {ECO:0000244|PDB:4DW2}. FT STRAND 359 363 {ECO:0000244|PDB:5YC6}. FT STRAND 365 367 {ECO:0000244|PDB:3KHV}. FT STRAND 379 384 {ECO:0000244|PDB:5YC6}. FT STRAND 387 396 {ECO:0000244|PDB:5YC6}. FT STRAND 398 402 {ECO:0000244|PDB:5YC6}. FT STRAND 407 411 {ECO:0000244|PDB:5YC6}. FT HELIX 412 414 {ECO:0000244|PDB:5YC6}. FT HELIX 416 422 {ECO:0000244|PDB:5YC6}. SQ SEQUENCE 431 AA; 48507 MW; 62C72400BC23115F CRC64; MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSHFLPWIR SHTKEENGLA L //