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Urokinase-type plasminogen activator (U-plasminogen activator) (uPA) (EC 3.4.21.73) [Cleaved into: Urokinase-type plasminogen activator long chain A; Urokinase-type plasminogen activator short chain A; Urokinase-type plasminogen activator chain B]

 UROK_HUMAN              Reviewed;         431 AA.
P00749; B4DPZ2; Q15844; Q16618; Q53XS3; Q5SWW9; Q969W6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
12-SEP-2018, entry version 233.
RecName: Full=Urokinase-type plasminogen activator;
Short=U-plasminogen activator;
Short=uPA;
EC=3.4.21.73;
Contains:
RecName: Full=Urokinase-type plasminogen activator long chain A;
Contains:
RecName: Full=Urokinase-type plasminogen activator short chain A;
Contains:
RecName: Full=Urokinase-type plasminogen activator chain B;
Flags: Precursor;
Name=PLAU;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Holmes W.E., Pennica D., Blaber M., Rey M.W., Guenzler W.A.,
Steffens G.J., Heyneker H.L.;
"Cloning and expression of the gene for pro-urokinase in Escherichia
coli.";
Biotechnology (N.Y.) 3:923-929(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3888571; DOI=10.1089/dna.1985.4.139;
Jacobs P., Cravador A., Loriau R., Brockly F., Colau B., Chuchana P.,
van Elsen A., Herzog A., Bollen A.;
"Molecular cloning, sequencing, and expression in Escherichia coli of
human preprourokinase cDNA.";
DNA 4:139-146(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2415429; DOI=10.1016/0378-1119(85)90084-8;
Nagai M., Hiramatsu R., Kaneda T., Hayasuke N., Arimura H.,
Nishida M., Suyama T.;
"Molecular cloning of cDNA coding for human preprourokinase.";
Gene 36:183-188(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-214.
PubMed=2987867; DOI=10.1093/nar/13.8.2759;
Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F.;
"The human urokinase-plasminogen activator gene and its promoter.";
Nucleic Acids Res. 13:2759-2771(1985).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) System Donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Mesangial cell;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-15; LEU-141 AND
GLN-231.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-141.
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-431, AND VARIANT LEU-141.
PubMed=8652631;
Yoshimoto M., Ushiyama Y., Sakai M., Tamaki S., Hara H., Takahashi K.,
Sawasaki Y., Hanada K.;
"Characterization of single chain urokinase-type plasminogen activator
with a novel amino-acid substitution in the kringle structure.";
Biochim. Biophys. Acta 1293:83-89(1996).
[12]
PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=2023947; DOI=10.1073/pnas.88.9.3992;
Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R.,
Sarin V.K.;
"Characterization of a posttranslational fucosylation in the growth
factor domain of urinary plasminogen activator.";
Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431, AND VARIANT
MET-214.
PubMed=6589620; DOI=10.1073/pnas.81.15.4727;
Verde P., Stoppelli M.P., Galeffi P., di Nocera P., Blasi F.;
"Identification and primary sequence of an unspliced human urokinase
poly(A)+ RNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:4727-4731(1984).
[14]
PROTEIN SEQUENCE OF 21-177.
PubMed=6754569;
Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E.,
Flohe L.;
"The primary structure of high molecular mass urokinase from human
urine. The complete amino acid sequence of the A chain.";
Hoppe-Seyler's Z. Physiol. Chem. 363:1155-1165(1982).
[15]
PROTEIN SEQUENCE OF 156-176 AND 179-224.
PubMed=6749491; DOI=10.1111/j.1432-1033.1982.tb06676.x;
Schaller J., Nick H., Rickli E.E., Gillessen D., Lergier W.,
Studer R.O.;
"Human low-molecular-weight urinary urokinase. Partial
characterization and preliminary sequence data of the two polypeptide
chains.";
Eur. J. Biochem. 125:251-257(1982).
[16]
PROTEIN SEQUENCE OF 158-410.
PubMed=6754572;
Steffens G.J., Gunzler W.A., Otting F., Frankus E., Flohe L.;
"The complete amino acid sequence of low molecular mass urokinase from
human urine.";
Hoppe-Seyler's Z. Physiol. Chem. 363:1043-1058(1982).
[17]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=3501295;
Stief T.W., Radtke K.P., Heimburger N.;
"Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for
identity of PCI and plasminogen activator inhibitor 3.";
Biol. Chem. Hoppe-Seyler 368:1427-1433(1987).
[18]
PHOSPHORYLATION AT SER-158 AND SER-323, AND MUTAGENESIS OF SER-158 AND
SER-323.
PubMed=9151681; DOI=10.1083/jcb.137.3.779;
Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C.,
Mastronicola M.R., Nolli M.L., Stoppelli M.P.;
"Phosphorylation of human pro-urokinase on Ser138/303 impairs its
receptor-dependent ability to promote myelomonocytic adherence and
motility.";
J. Cell Biol. 137:779-791(1997).
[19]
HETERODIMER WITH SERPINA5.
PubMed=10340997; DOI=10.1093/molehr/5.6.513;
He S., Lin Y.L., Liu Y.X.;
"Functionally inactive protein C inhibitor in seminal plasma may be
associated with infertility.";
Mol. Hum. Reprod. 5:513-519(1999).
[20]
INTERACTION WITH MRC2.
PubMed=10636902; DOI=10.1074/jbc.275.3.1993;
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M.,
Danoe K.;
"A urokinase receptor-associated protein with specific collagen
binding properties.";
J. Biol. Chem. 275:1993-2002(2000).
[21]
INTERACTION WITH LRP1B.
PubMed=11384978; DOI=10.1074/jbc.M102727200;
Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
"The putative tumor suppressor LRP1B, a novel member of the low
density lipoprotein (LDL) receptor family, exhibits both overlapping
and distinct properties with the LDL receptor-related protein.";
J. Biol. Chem. 276:28889-28896(2001).
[22]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=14696115; DOI=10.1002/ijc.11594;
Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K.,
Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.;
"Regulation of carcinoma cell invasion by protein C inhibitor whose
expression is decreased in renal cell carcinoma.";
Int. J. Cancer 108:516-523(2004).
[23]
TISSUE SPECIFICITY.
PubMed=15988036; DOI=10.1128/MCB.25.14.6279-6288.2005;
Ustach C.V., Kim H.-R.C.;
"Platelet-derived growth factor D is activated by urokinase
plasminogen activator in prostate carcinoma cells.";
Mol. Cell. Biol. 25:6279-6288(2005).
[24]
INVOLVEMENT IN QPD.
PubMed=20007542; DOI=10.1182/blood-2009-07-233965;
Paterson A.D., Rommens J.M., Bharaj B., Blavignac J., Wong I.,
Diamandis M., Waye J.S., Rivard G.E., Hayward C.P.;
"Persons with Quebec platelet disorder have a tandem duplication of
PLAU, the urokinase plasminogen activator gene.";
Blood 115:1264-1266(2010).
[25]
STRUCTURE BY NMR.
PubMed=2536903; DOI=10.1038/337579a0;
Oswald R.E., Bogusky M.J., Bamberger M., Smith R.A.G., Dobson C.M.;
"Dynamics of the multidomain fibrinolytic protein urokinase from two-
dimensional NMR.";
Nature 337:579-582(1989).
[26]
STRUCTURE BY NMR OF 67-155.
PubMed=1327118; DOI=10.1021/bi00155a008;
Li X., Smith R.A.G., Dobson C.M.;
"Sequential 1H NMR assignments and secondary structure of the kringle
domain from urokinase.";
Biochemistry 31:9562-9571(1992).
[27]
STRUCTURE BY NMR OF 67-155.
PubMed=8107091; DOI=10.1006/jmbi.1994.1106;
Li X., Bokman A.M., Llinas M., Smith R.A.G., Dobson C.M.;
"Solution structure of the kringle domain from urokinase-type
plasminogen activator.";
J. Mol. Biol. 235:1548-1559(1994).
[28]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8591045; DOI=10.1016/S0969-2126(01)00203-9;
Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D.,
Dobson C.M., Stuart D.I., Jones E.Y.;
"The crystal structure of the catalytic domain of human urokinase-type
plasminogen activator.";
Structure 3:681-691(1995).
[29]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
PubMed=10805774; DOI=10.1073/pnas.97.10.5113;
Sperl S., Jacob U., Arroyo de Prada N., Sturzebecher J., Wilhelm O.G.,
Bode W., Magdolen V., Huber R., Moroder L.;
"(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly
selective inhibitors of human urokinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000).
[30]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-152 IN COMPLEX WITH PLAUR.
PubMed=16456079; DOI=10.1126/science.1121143;
Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J.,
Li Y., Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B.,
Huang M.;
"Structure of human urokinase plasminogen activator in complex with
its receptor.";
Science 311:656-659(2006).
[31]
VARIANT LEU-141.
PubMed=9065988;
Conne B., Berczy M., Belin D.;
"Detection of polymorphisms in the human urokinase-type plasminogen
activator gene.";
Thromb. Haemost. 77:434-435(1997).
[32]
ERRATUM.
Conne B., Berczy M., Belin D.;
Thromb. Haemost. 78:973-973(1997).
[33]
VARIANT LEU-141.
PubMed=9194591; DOI=10.1002/elps.1150180505;
Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W.,
Creutzburg S., Graeff H., Magdolen V.;
"Mutational analysis of the genes encoding urokinase-type plasminogen
activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer.";
Electrophoresis 18:686-689(1997).
[34]
VARIANT [LARGE SCALE ANALYSIS] LEU-141.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
active enzyme plasmin.
-!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
plasminogen to form plasmin.
-!- ACTIVITY REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:3501295}.
-!- SUBUNIT: Found in high and low molecular mass forms. Each consists
of two chains, A and B. The high molecular mass form contains a
long chain A which is cleaved to yield a short chain A. Forms
heterodimer with SERPINA5. Binds LRP1B; binding is followed by
internalization and degradation. Interacts with MRC2. Interacts
with PLAUR. {ECO:0000269|PubMed:10636902,
ECO:0000269|PubMed:11384978, ECO:0000269|PubMed:16456079}.
-!- INTERACTION:
Q03405-1:PLAUR; NbExp=2; IntAct=EBI-3905042, EBI-15695188;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00749-1; Sequence=Displayed;
Name=2;
IsoId=P00749-2; Sequence=VSP_038368;
-!- TISSUE SPECIFICITY: Expressed in the prostate gland and prostate
cancers. {ECO:0000269|PubMed:15988036}.
-!- PTM: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive
ability but does not interfere with receptor binding.
{ECO:0000269|PubMed:9151681}.
-!- DISEASE: Quebec platelet disorder (QPD) [MIM:601709]: An autosomal
dominant bleeding disorder due to a gain-of-function defect in
fibrinolysis. Although affected individuals do not exhibit
systemic fibrinolysis, they show delayed onset bleeding after
challenge, such as surgery. The hallmark of the disorder is
markedly increased PLAU levels within platelets, which causes
intraplatelet plasmin generation and secondary degradation of
alpha-granule proteins. {ECO:0000269|PubMed:20007542}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- PHARMACEUTICAL: Available under the name Abbokinase (Abbott). Used
in Pulmonary Embolism (PE) to initiate fibrinolysis. Clinically
used for therapy of thrombolytic disorders.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Urokinase entry;
URL="https://en.wikipedia.org/wiki/Urokinase";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/plau/";
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EMBL; M15476; AAA61253.1; -; mRNA.
EMBL; X02760; CAA26535.1; -; mRNA.
EMBL; D00244; BAA00175.1; -; mRNA.
EMBL; K03226; AAC97138.1; -; mRNA.
EMBL; X02419; CAA26268.1; -; Genomic_DNA.
EMBL; AF377330; AAK53822.1; -; Genomic_DNA.
EMBL; BT007391; AAP36055.1; -; mRNA.
EMBL; AK298560; BAG60754.1; -; mRNA.
EMBL; AL596247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54544.1; -; Genomic_DNA.
EMBL; BC013575; AAH13575.1; -; mRNA.
EMBL; D11143; BAA01919.1; -; mRNA.
EMBL; K02286; AAA61252.1; -; Genomic_DNA.
CCDS; CCDS44442.1; -. [P00749-2]
CCDS; CCDS7339.1; -. [P00749-1]
PIR; A00931; UKHU.
RefSeq; NP_001138503.1; NM_001145031.2. [P00749-2]
RefSeq; NP_001306120.1; NM_001319191.1.
RefSeq; NP_002649.1; NM_002658.4. [P00749-1]
UniGene; Hs.77274; -.
PDB; 1C5W; X-ray; 1.94 A; A=156-178, B=179-431.
PDB; 1C5X; X-ray; 1.75 A; A=156-178, B=179-431.
PDB; 1C5Y; X-ray; 1.65 A; A=156-178, B=179-431.
PDB; 1C5Z; X-ray; 1.85 A; A=156-178, B=179-431.
PDB; 1EJN; X-ray; 1.80 A; A=179-431.
PDB; 1F5K; X-ray; 1.80 A; U=179-431.
PDB; 1F5L; X-ray; 2.10 A; A=179-431.
PDB; 1F92; X-ray; 2.60 A; A=179-431.
PDB; 1FV9; X-ray; 3.00 A; A=179-423.
PDB; 1GI7; X-ray; 1.79 A; A=156-178, B=179-423.
PDB; 1GI8; X-ray; 1.75 A; A=156-178, B=179-423.
PDB; 1GI9; X-ray; 1.80 A; A=156-178, B=179-423.
PDB; 1GJ7; X-ray; 1.50 A; A=156-178, B=179-431.
PDB; 1GJ8; X-ray; 1.64 A; A=156-178, B=179-431.
PDB; 1GJ9; X-ray; 1.80 A; A=156-178, B=179-431.
PDB; 1GJA; X-ray; 1.56 A; A=156-178, B=179-431.
PDB; 1GJB; X-ray; 1.90 A; A=156-178, B=179-431.
PDB; 1GJC; X-ray; 1.73 A; A=156-178, B=179-431.
PDB; 1GJD; X-ray; 1.75 A; A=156-178, B=179-431.
PDB; 1KDU; NMR; -; A=69-153.
PDB; 1LMW; X-ray; 2.50 A; A/C=156-178, B/D=179-431.
PDB; 1O3P; X-ray; 1.81 A; A=156-178, B=179-431.
PDB; 1O5A; X-ray; 1.68 A; A=156-178, B=179-431.
PDB; 1O5B; X-ray; 1.85 A; A=156-178, B=179-431.
PDB; 1O5C; X-ray; 1.63 A; A=156-178, B=179-431.
PDB; 1OWD; X-ray; 2.32 A; A=179-423.
PDB; 1OWE; X-ray; 1.60 A; A=179-423.
PDB; 1OWH; X-ray; 1.61 A; A=179-423.
PDB; 1OWI; X-ray; 2.93 A; A=179-423.
PDB; 1OWJ; X-ray; 3.10 A; A=179-423.
PDB; 1OWK; X-ray; 2.80 A; A=179-423.
PDB; 1SC8; X-ray; 2.40 A; U=164-425.
PDB; 1SQA; X-ray; 2.00 A; A=179-423.
PDB; 1SQO; X-ray; 1.84 A; A=179-423.
PDB; 1SQT; X-ray; 1.90 A; A=179-423.
PDB; 1U6Q; X-ray; 2.02 A; A=179-423.
PDB; 1URK; NMR; -; A=26-155.
PDB; 1VJ9; X-ray; 2.40 A; U=164-425.
PDB; 1VJA; X-ray; 2.00 A; U=164-425.
PDB; 1W0Z; X-ray; 1.90 A; U=179-425.
PDB; 1W10; X-ray; 2.00 A; U=179-425.
PDB; 1W11; X-ray; 2.00 A; U=179-425.
PDB; 1W12; X-ray; 2.40 A; U=179-425.
PDB; 1W13; X-ray; 2.00 A; U=179-425.
PDB; 1W14; X-ray; 2.20 A; U=179-425.
PDB; 2FD6; X-ray; 1.90 A; A=31-152.
PDB; 2I9A; X-ray; 1.90 A; A/B/C/D=21-163.
PDB; 2I9B; X-ray; 2.80 A; A/B/C/D=21-163.
PDB; 2NWN; X-ray; 2.15 A; A=179-431.
PDB; 2O8T; X-ray; 1.45 A; A=179-431.
PDB; 2O8U; X-ray; 1.70 A; A=179-431.
PDB; 2O8W; X-ray; 1.86 A; A=179-431.
PDB; 2R2W; X-ray; 2.01 A; U=179-431.
PDB; 2VIN; X-ray; 1.90 A; A=179-431.
PDB; 2VIO; X-ray; 1.80 A; A=179-431.
PDB; 2VIP; X-ray; 1.72 A; A=179-431.
PDB; 2VIQ; X-ray; 2.00 A; A=179-431.
PDB; 2VIV; X-ray; 1.72 A; A=179-431.
PDB; 2VIW; X-ray; 2.05 A; A=179-431.
PDB; 2VNT; X-ray; 2.20 A; A/B/C/D/E/F=156-431.
PDB; 3BT1; X-ray; 2.80 A; A=21-153.
PDB; 3BT2; X-ray; 2.50 A; A=21-153.
PDB; 3IG6; X-ray; 1.83 A; A/C=156-178, B/D=179-431.
PDB; 3KGP; X-ray; 2.35 A; A=179-431.
PDB; 3KHV; X-ray; 2.35 A; A=179-431.
PDB; 3KID; X-ray; 2.71 A; U=179-431.
PDB; 3M61; X-ray; 1.68 A; U=179-431.
PDB; 3MHW; X-ray; 1.45 A; U=179-425.
PDB; 3MWI; X-ray; 2.03 A; U=179-424.
PDB; 3OX7; X-ray; 1.58 A; U=179-431.
PDB; 3OY5; X-ray; 2.31 A; U=179-431.
PDB; 3OY6; X-ray; 2.31 A; U=179-431.
PDB; 3PB1; X-ray; 2.30 A; E=179-431.
PDB; 3QN7; X-ray; 1.90 A; A=179-431.
PDB; 3U73; X-ray; 3.19 A; A=21-152.
PDB; 4DVA; X-ray; 1.94 A; U=179-424.
PDB; 4DW2; X-ray; 2.97 A; U=179-424.
PDB; 4FU7; X-ray; 2.00 A; A=179-424.
PDB; 4FU8; X-ray; 2.20 A; A=179-424.
PDB; 4FU9; X-ray; 1.60 A; A=179-424.
PDB; 4FUB; X-ray; 1.90 A; A=179-424.
PDB; 4FUC; X-ray; 1.72 A; A=179-424.
PDB; 4FUD; X-ray; 2.00 A; A=179-424.
PDB; 4FUE; X-ray; 2.00 A; A=179-424.
PDB; 4FUF; X-ray; 2.00 A; A=179-424.
PDB; 4FUG; X-ray; 1.80 A; A=179-424.
PDB; 4FUH; X-ray; 1.60 A; A=179-424.
PDB; 4FUI; X-ray; 2.00 A; A=179-424.
PDB; 4FUJ; X-ray; 2.05 A; A=179-424.
PDB; 4GLY; X-ray; 1.52 A; A=179-423.
PDB; 4H42; X-ray; 2.01 A; U=179-426.
PDB; 4JK5; X-ray; 1.55 A; A=179-423.
PDB; 4JK6; X-ray; 2.20 A; A=179-423.
PDB; 4JNI; X-ray; 1.17 A; U=179-425.
PDB; 4JNL; X-ray; 2.00 A; U=179-425.
PDB; 4K24; X-ray; 4.50 A; A=21-153.
PDB; 4MNV; X-ray; 1.80 A; A=179-423.
PDB; 4MNW; X-ray; 1.49 A; A=179-423.
PDB; 4MNX; X-ray; 1.85 A; A=179-423.
PDB; 4MNY; X-ray; 1.70 A; A/B=179-423.
PDB; 4OS1; X-ray; 2.20 A; A=179-423.
PDB; 4OS2; X-ray; 1.79 A; A=179-423.
PDB; 4OS4; X-ray; 2.00 A; A=179-423.
PDB; 4OS5; X-ray; 2.26 A; A=179-423.
PDB; 4OS6; X-ray; 1.75 A; A=179-423.
PDB; 4OS7; X-ray; 2.00 A; A=179-423.
PDB; 4X0W; X-ray; 2.10 A; U=179-425.
PDB; 4X1N; X-ray; 1.80 A; U=179-425.
PDB; 4X1P; X-ray; 1.60 A; U=179-425.
PDB; 4X1Q; X-ray; 2.28 A; U=179-425.
PDB; 4X1R; X-ray; 2.10 A; U=179-425.
PDB; 4X1S; X-ray; 1.90 A; U=179-425.
PDB; 4XSK; X-ray; 1.50 A; U=179-424.
PDB; 4ZHL; X-ray; 2.06 A; U=179-425.
PDB; 4ZHM; X-ray; 1.90 A; U=179-425.
PDB; 4ZKN; X-ray; 1.36 A; U=179-425.
PDB; 4ZKO; X-ray; 1.29 A; U=179-425.
PDB; 4ZKR; X-ray; 1.36 A; U=179-425.
PDB; 4ZKS; X-ray; 1.85 A; U=179-425.
PDB; 5HGG; X-ray; 1.97 A; A/B=179-424.
PDB; 5XG4; X-ray; 3.00 A; U=179-424.
PDBsum; 1C5W; -.
PDBsum; 1C5X; -.
PDBsum; 1C5Y; -.
PDBsum; 1C5Z; -.
PDBsum; 1EJN; -.
PDBsum; 1F5K; -.
PDBsum; 1F5L; -.
PDBsum; 1F92; -.
PDBsum; 1FV9; -.
PDBsum; 1GI7; -.
PDBsum; 1GI8; -.
PDBsum; 1GI9; -.
PDBsum; 1GJ7; -.
PDBsum; 1GJ8; -.
PDBsum; 1GJ9; -.
PDBsum; 1GJA; -.
PDBsum; 1GJB; -.
PDBsum; 1GJC; -.
PDBsum; 1GJD; -.
PDBsum; 1KDU; -.
PDBsum; 1LMW; -.
PDBsum; 1O3P; -.
PDBsum; 1O5A; -.
PDBsum; 1O5B; -.
PDBsum; 1O5C; -.
PDBsum; 1OWD; -.
PDBsum; 1OWE; -.
PDBsum; 1OWH; -.
PDBsum; 1OWI; -.
PDBsum; 1OWJ; -.
PDBsum; 1OWK; -.
PDBsum; 1SC8; -.
PDBsum; 1SQA; -.
PDBsum; 1SQO; -.
PDBsum; 1SQT; -.
PDBsum; 1U6Q; -.
PDBsum; 1URK; -.
PDBsum; 1VJ9; -.
PDBsum; 1VJA; -.
PDBsum; 1W0Z; -.
PDBsum; 1W10; -.
PDBsum; 1W11; -.
PDBsum; 1W12; -.
PDBsum; 1W13; -.
PDBsum; 1W14; -.
PDBsum; 2FD6; -.
PDBsum; 2I9A; -.
PDBsum; 2I9B; -.
PDBsum; 2NWN; -.
PDBsum; 2O8T; -.
PDBsum; 2O8U; -.
PDBsum; 2O8W; -.
PDBsum; 2R2W; -.
PDBsum; 2VIN; -.
PDBsum; 2VIO; -.
PDBsum; 2VIP; -.
PDBsum; 2VIQ; -.
PDBsum; 2VIV; -.
PDBsum; 2VIW; -.
PDBsum; 2VNT; -.
PDBsum; 3BT1; -.
PDBsum; 3BT2; -.
PDBsum; 3IG6; -.
PDBsum; 3KGP; -.
PDBsum; 3KHV; -.
PDBsum; 3KID; -.
PDBsum; 3M61; -.
PDBsum; 3MHW; -.
PDBsum; 3MWI; -.
PDBsum; 3OX7; -.
PDBsum; 3OY5; -.
PDBsum; 3OY6; -.
PDBsum; 3PB1; -.
PDBsum; 3QN7; -.
PDBsum; 3U73; -.
PDBsum; 4DVA; -.
PDBsum; 4DW2; -.
PDBsum; 4FU7; -.
PDBsum; 4FU8; -.
PDBsum; 4FU9; -.
PDBsum; 4FUB; -.
PDBsum; 4FUC; -.
PDBsum; 4FUD; -.
PDBsum; 4FUE; -.
PDBsum; 4FUF; -.
PDBsum; 4FUG; -.
PDBsum; 4FUH; -.
PDBsum; 4FUI; -.
PDBsum; 4FUJ; -.
PDBsum; 4GLY; -.
PDBsum; 4H42; -.
PDBsum; 4JK5; -.
PDBsum; 4JK6; -.
PDBsum; 4JNI; -.
PDBsum; 4JNL; -.
PDBsum; 4K24; -.
PDBsum; 4MNV; -.
PDBsum; 4MNW; -.
PDBsum; 4MNX; -.
PDBsum; 4MNY; -.
PDBsum; 4OS1; -.
PDBsum; 4OS2; -.
PDBsum; 4OS4; -.
PDBsum; 4OS5; -.
PDBsum; 4OS6; -.
PDBsum; 4OS7; -.
PDBsum; 4X0W; -.
PDBsum; 4X1N; -.
PDBsum; 4X1P; -.
PDBsum; 4X1Q; -.
PDBsum; 4X1R; -.
PDBsum; 4X1S; -.
PDBsum; 4XSK; -.
PDBsum; 4ZHL; -.
PDBsum; 4ZHM; -.
PDBsum; 4ZKN; -.
PDBsum; 4ZKO; -.
PDBsum; 4ZKR; -.
PDBsum; 4ZKS; -.
PDBsum; 5HGG; -.
PDBsum; 5XG4; -.
ProteinModelPortal; P00749; -.
SMR; P00749; -.
BioGrid; 111344; 21.
ComplexPortal; CPX-483; uPA-PAI-1 complex.
ComplexPortal; CPX-487; uPA-uPAR complex.
ComplexPortal; CPX-501; uPA-uPAR-vitronectin complex.
DIP; DIP-46387N; -.
ELM; P00749; -.
IntAct; P00749; 9.
MINT; P00749; -.
STRING; 9606.ENSP00000361850; -.
BindingDB; P00749; -.
ChEMBL; CHEMBL3286; -.
DrugBank; DB07122; 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine.
DrugBank; DB01905; 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine.
DrugBank; DB06854; 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DrugBank; DB02193; 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine.
DrugBank; DB03729; 2-Amino-5-Hydroxy-Benzimidazole.
DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine.
DrugBank; DB01977; 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine.
DrugBank; DB07076; 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE.
DrugBank; DB03082; 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide.
DrugBank; DB02398; 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine.
DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine.
DrugBank; DB06855; 6-FLUORO-2-(2-HYDROXY-3-ISOBUTOXY-PHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DrugBank; DB06856; 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE.
DrugBank; DB03046; 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide.
DrugBank; DB04059; 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide.
DrugBank; DB00594; Amiloride.
DrugBank; DB03127; Benzamidine.
DrugBank; DB02526; CRA_10655.
DrugBank; DB03159; CRA_8696.
DrugBank; DB03782; N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea.
DrugBank; DB06857; N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE.
DrugBank; DB05254; Plasmin.
DrugBank; DB03476; Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine.
DrugBank; DB00013; Urokinase.
GuidetoPHARMACOLOGY; 2393; -.
MEROPS; S01.231; -.
GlyConnect; 503; -.
GlyConnect; 519; -.
GlyConnect; 612; -.
iPTMnet; P00749; -.
PhosphoSitePlus; P00749; -.
UniCarbKB; P00749; -.
BioMuta; PLAU; -.
DMDM; 254763341; -.
EPD; P00749; -.
MaxQB; P00749; -.
PaxDb; P00749; -.
PeptideAtlas; P00749; -.
PRIDE; P00749; -.
ProteomicsDB; 51279; -.
ProteomicsDB; 51280; -. [P00749-2]
DNASU; 5328; -.
Ensembl; ENST00000372764; ENSP00000361850; ENSG00000122861.
Ensembl; ENST00000496777; ENSP00000431795; ENSG00000122861.
GeneID; 5328; -.
KEGG; hsa:5328; -.
UCSC; uc001jwa.4; human. [P00749-1]
CTD; 5328; -.
DisGeNET; 5328; -.
EuPathDB; HostDB:ENSG00000122861.15; -.
GeneCards; PLAU; -.
HGNC; HGNC:9052; PLAU.
HPA; HPA008719; -.
MalaCards; PLAU; -.
MIM; 191840; gene.
MIM; 601709; phenotype.
neXtProt; NX_P00749; -.
Orphanet; 220436; Quebec platelet disorder.
PharmGKB; PA33382; -.
eggNOG; ENOG410IGFI; Eukaryota.
eggNOG; COG5640; LUCA.
HOVERGEN; HBG008633; -.
InParanoid; P00749; -.
KO; K01348; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00749; -.
TreeFam; TF329901; -.
BRENDA; 3.4.21.73; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
SABIO-RK; P00749; -.
SIGNOR; P00749; -.
EvolutionaryTrace; P00749; -.
GeneWiki; PLAU; -.
GenomeRNAi; 5328; -.
PMAP-CutDB; Q53XS3; -.
PRO; PR:P00749; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122861; Expressed in 181 organ(s), highest expression level in epithelium of bronchus.
CleanEx; HS_PLAU; -.
ExpressionAtlas; P00749; baseline and differential.
Genevisible; P00749; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0031639; P:plasminogen activation; IDA:AgBase.
GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010469; P:regulation of signaling receptor activity; IDA:BHF-UCL.
GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:2000097; P:regulation of smooth muscle cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0061041; P:regulation of wound healing; IC:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
CDD; cd00108; KR; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
InterPro; IPR034814; Urokinase.
PANTHER; PTHR24264:SF38; PTHR24264:SF38; 1.
Pfam; PF00051; Kringle; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00130; KR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00021; KRINGLE_1; 1.
PROSITE; PS50070; KRINGLE_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation;
Complete proteome; Direct protein sequencing; Disulfide bond;
EGF-like domain; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
Kringle; Pharmaceutical; Phosphoprotein; Plasminogen activation;
Polymorphism; Protease; Reference proteome; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL 1 20 {ECO:0000269|PubMed:2023947,
ECO:0000269|PubMed:6754569}.
CHAIN 21 431 Urokinase-type plasminogen activator.
/FTId=PRO_0000028318.
CHAIN 21 177 Urokinase-type plasminogen activator long
chain A.
/FTId=PRO_0000028319.
CHAIN 156 177 Urokinase-type plasminogen activator
short chain A.
/FTId=PRO_0000028320.
CHAIN 179 431 Urokinase-type plasminogen activator
chain B.
/FTId=PRO_0000028321.
DOMAIN 27 63 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 70 151 Kringle. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 179 424 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 34 57 Binds urokinase plasminogen activator
surface receptor. {ECO:0000250}.
REGION 152 177 Connecting peptide.
ACT_SITE 224 224 Charge relay system.
ACT_SITE 275 275 Charge relay system.
ACT_SITE 376 376 Charge relay system.
SITE 177 178 Cleavage; during zymogen activation.
MOD_RES 158 158 Phosphoserine.
{ECO:0000269|PubMed:9151681}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000269|PubMed:9151681}.
CARBOHYD 38 38 O-linked (Fuc) threonine.
{ECO:0000269|PubMed:2023947}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000026.
DISULFID 31 39
DISULFID 33 51
DISULFID 53 62
DISULFID 70 151
DISULFID 91 133
DISULFID 122 146
DISULFID 168 299 Interchain (between A and B chains).
DISULFID 209 225
DISULFID 217 288
DISULFID 313 382
DISULFID 345 361
DISULFID 372 400
VAR_SEQ 1 29 MRALLARLLLCVLVVSDSKGSNELHQVPS -> MVFHLRTR
YEQA (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038368.
VARIANT 15 15 V -> L (in dbSNP:rs2227580).
{ECO:0000269|Ref.7}.
/FTId=VAR_038730.
VARIANT 141 141 P -> L (in dbSNP:rs2227564).
{ECO:0000269|PubMed:15164054,
ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:8652631,
ECO:0000269|PubMed:9065988,
ECO:0000269|PubMed:9194591,
ECO:0000269|Ref.7}.
/FTId=VAR_006722.
VARIANT 214 214 I -> M. {ECO:0000269|PubMed:2987867,
ECO:0000269|PubMed:6589620}.
/FTId=VAR_013102.
VARIANT 231 231 K -> Q (in dbSNP:rs2227567).
{ECO:0000269|Ref.7}.
/FTId=VAR_038731.
MUTAGEN 158 158 S->E: Abolishes phosphorylation,
proadhesive function and ability to
induce chemotactic response; when
associated with E-323.
{ECO:0000269|PubMed:9151681}.
MUTAGEN 323 323 S->E: Abolishes phosphorylation,
proadhesive function and ability to
induce chemotactic response; when
associated with E-158.
{ECO:0000269|PubMed:9151681}.
CONFLICT 150 150 D -> G (in Ref. 6; BAG60754).
{ECO:0000305}.
CONFLICT 151 151 C -> W (in Ref. 2; CAA26535).
{ECO:0000305}.
CONFLICT 386 386 G -> C (in Ref. 2; CAA26535).
{ECO:0000305}.
CONFLICT 430 430 A -> V (in Ref. 2; CAA26535).
{ECO:0000305}.
STRAND 34 36 {ECO:0000244|PDB:1URK}.
STRAND 38 41 {ECO:0000244|PDB:2FD6}.
TURN 43 47 {ECO:0000244|PDB:2FD6}.
STRAND 49 52 {ECO:0000244|PDB:2FD6}.
STRAND 57 59 {ECO:0000244|PDB:2FD6}.
STRAND 64 67 {ECO:0000244|PDB:2FD6}.
STRAND 70 72 {ECO:0000244|PDB:2I9B}.
STRAND 73 77 {ECO:0000244|PDB:3U73}.
STRAND 86 89 {ECO:0000244|PDB:1URK}.
STRAND 94 96 {ECO:0000244|PDB:1KDU}.
HELIX 99 101 {ECO:0000244|PDB:2FD6}.
STRAND 102 104 {ECO:0000244|PDB:2FD6}.
STRAND 106 108 {ECO:0000244|PDB:3BT1}.
HELIX 111 114 {ECO:0000244|PDB:2FD6}.
STRAND 117 119 {ECO:0000244|PDB:2FD6}.
STRAND 128 130 {ECO:0000244|PDB:2I9A}.
STRAND 132 137 {ECO:0000244|PDB:2FD6}.
STRAND 140 147 {ECO:0000244|PDB:2FD6}.
HELIX 162 165 {ECO:0000244|PDB:1GJA}.
STRAND 180 184 {ECO:0000244|PDB:4JNI}.
HELIX 187 189 {ECO:0000244|PDB:4JNI}.
STRAND 193 199 {ECO:0000244|PDB:4JNI}.
STRAND 201 203 {ECO:0000244|PDB:4XSK}.
STRAND 205 215 {ECO:0000244|PDB:4JNI}.
STRAND 218 221 {ECO:0000244|PDB:4JNI}.
HELIX 223 225 {ECO:0000244|PDB:4JNI}.
TURN 226 228 {ECO:0000244|PDB:4JNI}.
HELIX 232 234 {ECO:0000244|PDB:4JNI}.
STRAND 235 240 {ECO:0000244|PDB:4JNI}.
STRAND 243 246 {ECO:0000244|PDB:4JNI}.
STRAND 252 261 {ECO:0000244|PDB:4JNI}.
STRAND 268 271 {ECO:0000244|PDB:5HGG}.
STRAND 272 274 {ECO:0000244|PDB:3MHW}.
STRAND 277 282 {ECO:0000244|PDB:4JNI}.
STRAND 293 295 {ECO:0000244|PDB:1LMW}.
STRAND 312 318 {ECO:0000244|PDB:4JNI}.
STRAND 329 331 {ECO:0000244|PDB:4DW2}.
STRAND 333 340 {ECO:0000244|PDB:4JNI}.
HELIX 342 345 {ECO:0000244|PDB:4JNI}.
TURN 348 351 {ECO:0000244|PDB:4JNI}.
HELIX 352 354 {ECO:0000244|PDB:4JNI}.
TURN 356 358 {ECO:0000244|PDB:4DW2}.
STRAND 359 363 {ECO:0000244|PDB:4JNI}.
STRAND 365 367 {ECO:0000244|PDB:3KHV}.
STRAND 379 384 {ECO:0000244|PDB:4JNI}.
STRAND 387 396 {ECO:0000244|PDB:4JNI}.
STRAND 398 402 {ECO:0000244|PDB:4JNI}.
STRAND 407 411 {ECO:0000244|PDB:4JNI}.
HELIX 412 414 {ECO:0000244|PDB:4JNI}.
HELIX 416 422 {ECO:0000244|PDB:4JNI}.
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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