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Database: UniProt
Entry: P00749
LinkDB: P00749
Original site: P00749 
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   22-APR-2020, entry version 248.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Steffens G.J.,
RA   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 human
RT   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., Nishida M.,
RA   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 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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., 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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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; DOI=10.1016/0167-4838(95)00228-6;
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 with
RT   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 BY
RP   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., Sarin V.K.;
RT   "Characterization of a posttranslational fucosylation in the growth factor
RT   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 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; DOI=10.1515/bchm2.1982.363.2.1155;
RA   Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E., Flohe L.;
RT   "The primary structure of high molecular mass urokinase from human urine.
RT   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., Studer R.O.;
RT   "Human low-molecular-weight urinary urokinase. Partial characterization and
RT   preliminary sequence data of the two polypeptide chains.";
RL   Eur. J. Biochem. 125:251-257(1982).
RN   [16]
RP   PROTEIN SEQUENCE OF 158-410.
RX   PubMed=6754572; DOI=10.1515/bchm2.1982.363.2.1043;
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; DOI=10.1515/bchm3.1987.368.2.1427;
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 receptor-
RT   dependent ability to promote myelomonocytic adherence and 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., Danoe K.;
RT   "A urokinase receptor-associated protein with specific collagen binding
RT   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 density
RT   lipoprotein (LDL) receptor family, exhibits both overlapping and distinct
RT   properties with the LDL receptor-related protein.";
RL   J. Biol. Chem. 276:28889-28896(2001).
RN   [22]
RP   INTERACTION WITH LRP1; PLAUR; SERPINE1 AND SORL1.
RX   PubMed=15053742; DOI=10.1042/bj20040149;
RA   Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C.,
RA   Andreasen P.A.;
RT   "The mosaic receptor sorLA/LR11 binds components of the plasminogen-
RT   activating system and platelet-derived growth factor-BB similarly to LRP1
RT   (low-density lipoprotein receptor-related protein), but mediates slow
RT   internalization of bound ligand.";
RL   Biochem. J. 381:203-212(2004).
RN   [23]
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   [24]
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 plasminogen
RT   activator in prostate carcinoma cells.";
RL   Mol. Cell. Biol. 25:6279-6288(2005).
RN   [25]
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 PLAU,
RT   the urokinase plasminogen activator gene.";
RL   Blood 115:1264-1266(2010).
RN   [26]
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   [27]
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   [28]
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 plasminogen
RT   activator.";
RL   J. Mol. Biol. 235:1548-1559(1994).
RN   [29]
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   [30]
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 selective
RT   inhibitors of human urokinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000).
RN   [31]
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., Li Y.,
RA   Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B., Huang M.;
RT   "Structure of human urokinase plasminogen activator in complex with its
RT   receptor.";
RL   Science 311:656-659(2006).
RN   [32]
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   [33]
RP   ERRATUM OF PUBMED:9065988.
RA   Conne B., Berczy M., Belin D.;
RL   Thromb. Haemost. 78:973-973(1997).
RN   [34]
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   [35]
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., Heath S.,
RA   Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA   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 form
CC         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 of
CC       two chains, A and B. The high molecular mass form contains a long chain
CC       A which is cleaved to yield a short chain A. Forms heterodimer with
CC       SERPINA5. Binds LRP1B; binding is followed by internalization and
CC       degradation. Interacts with MRC2. Interacts with PLAUR. In complex with
CC       SERPINE1, interacts with PLAUR/uPAR (PubMed:15053742). Interacts with
CC       SORL1 and LRP1, either alone or in complex with SERPINE1; these
CC       interactions are abolished in the presence of LRPAP1/RAP
CC       (PubMed:15053742). The ternary complex composed of PLAUR-PLAU-PAI1 also
CC       interacts with SORLA (PubMed:15053742). {ECO:0000269|PubMed:10636902,
CC       ECO:0000269|PubMed:11384978, ECO:0000269|PubMed:15053742,
CC       ECO:0000269|PubMed:16456079}.
CC   -!- INTERACTION:
CC       P00749; Q9UKQ2: ADAM28; NbExp=3; IntAct=EBI-3905042, EBI-1384181;
CC       P00749; 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 systemic
CC       fibrinolysis, they show delayed onset bleeding after challenge, such as
CC       surgery. The hallmark of the disorder is markedly increased PLAU levels
CC       within platelets, which causes intraplatelet plasmin generation and
CC       secondary degradation of alpha-granule proteins.
CC       {ECO:0000269|PubMed:20007542}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- PHARMACEUTICAL: Available under the name Abbokinase (Abbott). Used in
CC       Pulmonary Embolism (PE) to initiate fibrinolysis. Clinically used for
CC       therapy of thrombolytic disorders.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       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/";
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   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   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   PDB; 6AG2; X-ray; 1.77 A; U=179-431.
DR   PDB; 6AG3; X-ray; 2.48 A; U=179-431.
DR   PDB; 6AG7; X-ray; 1.90 A; U=179-423.
DR   PDB; 6AG9; X-ray; 1.63 A; U=179-431.
DR   PDB; 6NMB; X-ray; 2.30 A; A/B/C/D=162-431.
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   PDBsum; 6AG2; -.
DR   PDBsum; 6AG3; -.
DR   PDBsum; 6AG7; -.
DR   PDBsum; 6AG9; -.
DR   PDBsum; 6NMB; -.
DR   SMR; P00749; -.
DR   BioGrid; 111344; 22.
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; 12.
DR   MINT; P00749; -.
DR   STRING; 9606.ENSP00000361850; -.
DR   BindingDB; P00749; -.
DR   ChEMBL; CHEMBL3286; -.
DR   DrugBank; DB07129; (2R)-1-(2,6-dimethylphenoxy)propan-2-amine.
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; DB02287; 2-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-Carboxamidine.
DR   DrugBank; DB03729; 2-Amino-1H-benzimidazol-5-ol.
DR   DrugBank; DB01725; 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide.
DR   DrugBank; DB08072; 4-(2-AMINOETHOXY)-3,5-DICHLORO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE.
DR   DrugBank; DB07625; 4-(2-aminoethoxy)-N-(2,5-diethoxyphenyl)-3,5-dimethylbenzamide.
DR   DrugBank; DB07626; 4-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide.
DR   DrugBank; DB08697; 4-(2-aminoethoxy)-N-(3-chloro-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide.
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; DB02705; 6-[N-(1-Isopropyl-1,2,3,4-Tetrahydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine.
DR   DrugBank; DB02473; 6-[N-(1-Isopropyl-3,4-Dihydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine.
DR   DrugBank; DB02398; 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine.
DR   DrugBank; DB02551; 6-[N-(4-Ethyl-1,2,3,4-Tetrahydro-6-Isoquinolinyl)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; DB04172; [2,4,6-Triisopropyl-Phenylsulfonyl-L-[3-Amidino-Phenylalanine]]-Piperazine-N'-Beta-Alanine.
DR   DrugBank; DB00594; Amiloride.
DR   DrugBank; DB03127; Benzamidine.
DR   DrugBank; DB02526; CRA_10655.
DR   DrugBank; DB03159; CRA_8696.
DR   DrugBank; DB05254; Fibrinolysin.
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; DB03876; Thieno[2,3-B]Pyridine-2-Carboxamidine.
DR   DrugBank; DB03476; Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine.
DR   DrugBank; DB00013; Urokinase.
DR   DrugCentral; P00749; -.
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   MassIVE; P00749; -.
DR   MaxQB; P00749; -.
DR   PaxDb; P00749; -.
DR   PeptideAtlas; P00749; -.
DR   PRIDE; P00749; -.
DR   ProteomicsDB; 51279; -. [P00749-1]
DR   ProteomicsDB; 51280; -. [P00749-2]
DR   ABCD; P00749; -.
DR   Antibodypedia; 1899; 1005 antibodies.
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   GeneCards; PLAU; -.
DR   HGNC; HGNC:9052; PLAU.
DR   HPA; ENSG00000122861; Tissue enhanced (placenta).
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   InParanoid; P00749; -.
DR   KO; K01348; -.
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   ChiTaRS; PLAU; human.
DR   EvolutionaryTrace; P00749; -.
DR   GeneWiki; PLAU; -.
DR   GenomeRNAi; 5328; -.
DR   Pharos; P00749; Tchem.
DR   PRO; PR:P00749; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P00749; protein.
DR   Bgee; ENSG00000122861; Expressed in epithelium of bronchus and 180 other tissues.
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   Direct protein sequencing; Disulfide bond; EGF-like domain; Fibrinolysis;
KW   Glycoprotein; Hemostasis; Hydrolase; Kringle; Pharmaceutical;
KW   Phosphoprotein; Plasminogen activation; Polymorphism; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:2023947,
FT                   ECO:0000269|PubMed:6754569"
FT   CHAIN           21..431
FT                   /note="Urokinase-type plasminogen activator"
FT                   /id="PRO_0000028318"
FT   CHAIN           21..177
FT                   /note="Urokinase-type plasminogen activator long chain A"
FT                   /id="PRO_0000028319"
FT   CHAIN           156..177
FT                   /note="Urokinase-type plasminogen activator short chain A"
FT                   /id="PRO_0000028320"
FT   CHAIN           179..431
FT                   /note="Urokinase-type plasminogen activator chain B"
FT                   /id="PRO_0000028321"
FT   DOMAIN          27..63
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          70..151
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          179..424
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          34..57
FT                   /note="Binds urokinase plasminogen activator surface
FT                   receptor"
FT                   /evidence="ECO:0000250"
FT   REGION          152..177
FT                   /note="Connecting peptide"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT   ACT_SITE        275
FT                   /note="Charge relay system"
FT   ACT_SITE        376
FT                   /note="Charge relay system"
FT   SITE            177..178
FT                   /note="Cleavage; during zymogen activation"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9151681"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9151681"
FT   CARBOHYD        38
FT                   /note="O-linked (Fuc) threonine"
FT                   /evidence="ECO:0000269|PubMed:2023947"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /id="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
FT                   /note="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
FT                   /note="MRALLARLLLCVLVVSDSKGSNELHQVPS -> MVFHLRTRYEQA (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_038368"
FT   VARIANT         15
FT                   /note="V -> L (in dbSNP:rs2227580)"
FT                   /evidence="ECO:0000269|Ref.7"
FT                   /id="VAR_038730"
FT   VARIANT         141
FT                   /note="P -> L (in dbSNP:rs2227564)"
FT                   /evidence="ECO:0000269|PubMed:15164054,
FT                   ECO:0000269|PubMed:18987736, ECO:0000269|PubMed:8652631,
FT                   ECO:0000269|PubMed:9065988, ECO:0000269|PubMed:9194591,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_006722"
FT   VARIANT         214
FT                   /note="I -> M (in dbSNP:rs1050120)"
FT                   /evidence="ECO:0000269|PubMed:2987867,
FT                   ECO:0000269|PubMed:6589620"
FT                   /id="VAR_013102"
FT   VARIANT         231
FT                   /note="K -> Q (in dbSNP:rs2227567)"
FT                   /evidence="ECO:0000269|Ref.7"
FT                   /id="VAR_038731"
FT   MUTAGEN         158
FT                   /note="S->E: Abolishes phosphorylation, proadhesive
FT                   function and ability to induce chemotactic response; when
FT                   associated with E-323."
FT                   /evidence="ECO:0000269|PubMed:9151681"
FT   MUTAGEN         323
FT                   /note="S->E: Abolishes phosphorylation, proadhesive
FT                   function and ability to induce chemotactic response; when
FT                   associated with E-158."
FT                   /evidence="ECO:0000269|PubMed:9151681"
FT   CONFLICT        150
FT                   /note="D -> G (in Ref. 6; BAG60754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="C -> W (in Ref. 2; CAA26535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="G -> C (in Ref. 2; CAA26535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="A -> V (in Ref. 2; CAA26535)"
FT                   /evidence="ECO:0000305"
FT   STRAND          34..36
FT                   /evidence="ECO:0000244|PDB:1URK"
FT   STRAND          38..41
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   TURN            43..47
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          49..52
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          57..59
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          64..67
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          70..72
FT                   /evidence="ECO:0000244|PDB:2I9B"
FT   STRAND          73..77
FT                   /evidence="ECO:0000244|PDB:3U73"
FT   STRAND          86..89
FT                   /evidence="ECO:0000244|PDB:1URK"
FT   STRAND          94..96
FT                   /evidence="ECO:0000244|PDB:1KDU"
FT   HELIX           99..101
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          102..104
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          106..108
FT                   /evidence="ECO:0000244|PDB:3BT1"
FT   HELIX           111..114
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          117..119
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          128..130
FT                   /evidence="ECO:0000244|PDB:2I9A"
FT   STRAND          132..137
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   STRAND          140..147
FT                   /evidence="ECO:0000244|PDB:2FD6"
FT   HELIX           162..165
FT                   /evidence="ECO:0000244|PDB:1GJA"
FT   STRAND          180..184
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           187..189
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          193..199
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          201..203
FT                   /evidence="ECO:0000244|PDB:4XSK"
FT   STRAND          205..215
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          218..221
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           223..225
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   TURN            226..228
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           232..234
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          235..240
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          243..246
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          252..261
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          268..271
FT                   /evidence="ECO:0000244|PDB:5HGG"
FT   STRAND          272..274
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          277..282
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          293..295
FT                   /evidence="ECO:0000244|PDB:1LMW"
FT   STRAND          312..318
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          329..331
FT                   /evidence="ECO:0000244|PDB:4DW2"
FT   STRAND          333..340
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           342..345
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   TURN            348..351
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           352..354
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   TURN            356..358
FT                   /evidence="ECO:0000244|PDB:4DW2"
FT   STRAND          359..363
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          365..367
FT                   /evidence="ECO:0000244|PDB:3KHV"
FT   STRAND          379..384
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          387..396
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          398..402
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   STRAND          407..411
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           412..414
FT                   /evidence="ECO:0000244|PDB:5YC6"
FT   HELIX           416..422
FT                   /evidence="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
//
DBGET integrated database retrieval system