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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   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/";
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
//
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