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Plasminogen activator inhibitor 1 (PAI) (PAI-1) (Endothelial plasminogen activator inhibitor) (Serpin E1)

 PAI1_HUMAN              Reviewed;         402 AA.
P05121; B7Z4S0; F8WD53;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 211.
RecName: Full=Plasminogen activator inhibitor 1;
Short=PAI;
Short=PAI-1;
AltName: Full=Endothelial plasminogen activator inhibitor;
AltName: Full=Serpin E1;
Flags: Precursor;
Name=SERPINE1; Synonyms=PAI1, PLANH1;
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).
PubMed=2430793;
Pannekoek H., Veerman H., Lambers H., Diergaarde P., Verweij C.L.,
van Zonneveld A.-J., van Mourik J.A.;
"Endothelial plasminogen activator inhibitor (PAI): a new member of
the Serpin gene family.";
EMBO J. 5:2539-2544(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2820474; DOI=10.1021/bi00387a004;
Loskutoff D.J., Linders M., Keijer J., Veerman H.,
van Heerikhuizen H., Pannekoek H.;
"Structure of the human plasminogen activator inhibitor 1 gene:
nonrandom distribution of introns.";
Biochemistry 26:3763-3768(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3097076; DOI=10.1172/JCI112761;
Ginsburg D., Zeheb R., Yang A.Y., Rafferty U.M., Andreasen P.A.,
Nielsen L., Dano K., Lebo R.V., Gelehrter T.D.;
"cDNA cloning of human plasminogen activator-inhibitor from
endothelial cells.";
J. Clin. Invest. 78:1673-1680(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2612914; DOI=10.1016/0378-1119(89)90519-2;
Follo M., Ginsburg D.;
"Structure and expression of the human gene encoding plasminogen
activator inhibitor, PAI-1.";
Gene 84:447-453(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3262512; DOI=10.1111/j.1432-1033.1988.tb14320.x;
Strandberg L., Lawrence D., Ny T.;
"The organization of the human-plasminogen-activator-inhibitor-1 gene.
Implications on the evolution of the serine-protease inhibitor
family.";
Eur. J. Biochem. 176:609-616(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3132455;
Bosma P.J., van den Berg E.A., Kooistra T., Siemieniak D.R.,
Slightom J.L.;
"Human plasminogen activator inhibitor-1 gene. Promoter and structural
gene nucleotide sequences.";
J. Biol. Chem. 263:9129-9141(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Pannekoek H.;
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-15; ILE-17;
PRO-25; HIS-209 AND ASN-255.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[11]
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-402 (ISOFORM 1).
PubMed=3092219; DOI=10.1073/pnas.83.18.6776;
Ny T., Sawdey M., Lawrence D., Millan J.L., Loskutoff D.J.;
"Cloning and sequence of a cDNA coding for the human beta-migrating
endothelial-cell-type plasminogen activator inhibitor.";
Proc. Natl. Acad. Sci. U.S.A. 83:6776-6780(1986).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 AND 364-402 (ISOFORM 1).
PubMed=3025016; DOI=10.1016/0014-5793(86)81113-9;
Andreasen P.A., Riccio A., Welinder K.G., Douglas R., Sartorio R.,
Nielsen L.S., Oppenheimer C., Blasi F., Danoe K.;
"Plasminogen activator inhibitor type-1: reactive center and amino-
terminal heterogeneity determined by protein and cDNA sequencing.";
FEBS Lett. 209:213-218(1986).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-402 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Placenta;
PubMed=3026837; DOI=10.1016/0014-5793(87)81288-7;
Wun T.C., Kretzmer K.K.;
"cDNA cloning and expression in E. coli of a plasminogen activator
inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell.";
FEBS Lett. 210:11-16(1987).
[15]
INTERACTION WITH VTN.
PubMed=7522053; DOI=10.1016/0167-4838(94)90166-X;
Sigurdardottir O., Wiman B.;
"Identification of a PAI-1 binding site in vitronectin.";
Biochim. Biophys. Acta 1208:104-110(1994).
[16]
INVOLVEMENT IN PAI-1D.
PubMed=9207454;
Fay W.P., Parker A.C., Condrey L.R., Shapiro A.D.;
"Human plasminogen activator inhibitor-1 (PAI-1) deficiency:
characterization of a large kindred with a null mutation in the PAI-1
gene.";
Blood 90:204-208(1997).
[17]
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).
[18]
FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
HETERODIMER WITH TMPRSS7.
PubMed=15853774; DOI=10.1042/BJ20050299;
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
"Matriptase-3 is a novel phylogenetically preserved membrane-anchored
serine protease with broad serpin reactivity.";
Biochem. J. 390:231-242(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=1731226; DOI=10.1038/355270a0;
Mottonen J., Strand A., Symersky J., Sweet R.M., Danley D.E.,
Geoghegan K.F., Gerard R.D., Goldsmith E.J.;
"Structural basis of latency in plasminogen activator inhibitor-1.";
Nature 355:270-273(1992).
[21]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=7552714; DOI=10.1038/nsb1095-891;
Aertgeerts K., de Bondt H.L., de Ranter C.J., Declerck P.J.;
"Mechanisms contributing to the conformational and functional
flexibility of plasminogen activator inhibitor-1.";
Nat. Struct. Biol. 2:891-897(1995).
[22]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
PubMed=9634700; DOI=10.1016/S0969-2126(98)00064-1;
Xue Y., Bjoerquist P., Inghardt T., Linschoten M., Musil D.,
Sjoelin L., Deinum J.;
"Interfering with the inhibitory mechanism of serpins: crystal
structure of a complex formed between cleaved plasminogen activator
inhibitor type 1 and a reactive-centre loop peptide.";
Structure 6:627-636(1998).
[23]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS).
PubMed=10368279; DOI=10.1016/S0969-2126(99)80018-5;
Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B.,
Ginsburg D., Lawrence D.A., Read R.J.;
"The active conformation of plasminogen activator inhibitor 1, a
target for drugs to control fibrinolysis and cell adhesion.";
Structure 7:111-118(1999).
[24]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=10731421; DOI=10.1006/jmbi.2000.3604;
Nar H., Bauer M., Stassen J.M., Lang D., Gils A., Declerck P.J.;
"Plasminogen activator inhibitor 1. Structure of the native serpin,
comparison to its other conformers and implications for serpin
inactivation.";
J. Mol. Biol. 297:683-695(2000).
[25]
VARIANT THR-15.
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).
[26]
VARIANTS THR-15 AND ILE-17.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[27]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
-!- FUNCTION: Serine protease inhibitor. This inhibitor acts as 'bait'
for tissue plasminogen activator, urokinase, protein C and
matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function
as a major control point in the regulation of fibrinolysis.
{ECO:0000269|PubMed:15853774}.
-!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
Interacts with VTN. Binds LRP1B; binding is followed by
internalization and degradation. {ECO:0000269|PubMed:11384978,
ECO:0000269|PubMed:7522053}.
-!- INTERACTION:
P02763:ORM1; NbExp=4; IntAct=EBI-953978, EBI-976767;
O43765:SGTA; NbExp=5; IntAct=EBI-953978, EBI-347996;
Q96EQ0:SGTB; NbExp=5; IntAct=EBI-953978, EBI-744081;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-10173939;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05121-1; Sequence=Displayed;
Name=2;
IsoId=P05121-2; Sequence=VSP_045493;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in plasma and platelets and in
endothelial, hepatoma and fibrosarcoma cells.
-!- PTM: Inactivated by proteolytic attack of the urokinase-type (u-
PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370
bond.
-!- DISEASE: Plasminogen activator inhibitor-1 deficiency (PAI-1D)
[MIM:613329]: A hematologic disorder characterized by increased
bleeding after trauma, injury, or surgery. Affected females have
menorrhagia. The bleeding defect is due to increased fibrinolysis
of fibrin blood clots due to deficiency of plasminogen activator
inhibitor-1, which inhibits tissue and urinary activators of
plasminogen. {ECO:0000269|PubMed:9207454}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=High concentrations of SERPINE1 seem to contribute
to the development of venous but not arterial occlusions.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Plasminogen activator
inhibitor-1 entry;
URL="https://en.wikipedia.org/wiki/Plasminogen_activator_inhibitor-1";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/serpine1/";
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EMBL; X04429; CAA28025.1; -; mRNA.
EMBL; M14083; AAA60008.1; -; mRNA.
EMBL; X04729; CAA28438.1; -; mRNA.
EMBL; X04731; CAA28442.1; -; mRNA.
EMBL; M16006; AAA60003.1; -; mRNA.
EMBL; M22321; AAA60009.1; -; Genomic_DNA.
EMBL; M22314; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22315; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22316; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22317; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22318; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22319; AAA60009.1; JOINED; Genomic_DNA.
EMBL; M22320; AAA60009.1; JOINED; Genomic_DNA.
EMBL; X13323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X13338; CAA31722.1; -; Genomic_DNA.
EMBL; X13339; CAB51639.1; -; Genomic_DNA.
EMBL; X13340; CAB51737.1; -; Genomic_DNA.
EMBL; X13341; CAB51606.1; -; Genomic_DNA.
EMBL; X13342; CAB51607.1; -; Genomic_DNA.
EMBL; X13343; CAB51738.1; -; Genomic_DNA.
EMBL; X13344; CAB51739.1; -; Genomic_DNA.
EMBL; X13345; CAA31729.1; -; Genomic_DNA.
EMBL; J03764; AAA60007.1; -; Genomic_DNA.
EMBL; X12701; CAA31208.1; -; mRNA.
EMBL; AF386492; AAK60338.1; -; Genomic_DNA.
EMBL; AK297728; BAH12656.1; -; mRNA.
EMBL; AC004876; AAD45828.1; -; Genomic_DNA.
EMBL; BC010860; AAH10860.1; -; mRNA.
EMBL; X04744; CAA28444.1; -; mRNA.
CCDS; CCDS5711.1; -. [P05121-1]
PIR; A28107; ITHUP1.
RefSeq; NP_000593.1; NM_000602.4. [P05121-1]
UniGene; Hs.414795; -.
UniGene; Hs.713079; -.
UniGene; Hs.741440; -.
PDB; 1A7C; X-ray; 1.95 A; A=24-402.
PDB; 1B3K; X-ray; 2.99 A; A/B/C/D=24-402.
PDB; 1C5G; X-ray; 2.60 A; A=1-402.
PDB; 1DB2; X-ray; 2.70 A; A/B=26-402.
PDB; 1DVM; X-ray; 2.40 A; A/B/C/D=24-402.
PDB; 1DVN; X-ray; 2.10 A; A=24-402.
PDB; 1LJ5; X-ray; 1.80 A; A=24-402.
PDB; 1OC0; X-ray; 2.28 A; A=24-402.
PDB; 3CVM; X-ray; 2.02 A; A/B=21-402.
PDB; 3EOX; X-ray; 2.61 A; A=24-402.
PDB; 3PB1; X-ray; 2.30 A; I=24-402.
PDB; 3Q02; X-ray; 2.30 A; A/B=24-402.
PDB; 3Q03; X-ray; 2.64 A; A/B=24-402.
PDB; 3R4L; X-ray; 2.70 A; A=24-402.
PDB; 3UT3; X-ray; 2.42 A; A/B/C/D=28-402.
PDB; 4AQH; X-ray; 2.40 A; A/B/C=24-402.
PDB; 4G8O; X-ray; 2.71 A; A/B/C/D=28-402.
PDB; 4G8R; X-ray; 2.19 A; A/B=28-402.
PDB; 4IC0; X-ray; 2.32 A; A/B/C/D=24-402.
PDB; 5BRR; X-ray; 3.16 A; I=24-402.
PDB; 9PAI; X-ray; 2.70 A; A=24-369, B=370-402.
PDBsum; 1A7C; -.
PDBsum; 1B3K; -.
PDBsum; 1C5G; -.
PDBsum; 1DB2; -.
PDBsum; 1DVM; -.
PDBsum; 1DVN; -.
PDBsum; 1LJ5; -.
PDBsum; 1OC0; -.
PDBsum; 3CVM; -.
PDBsum; 3EOX; -.
PDBsum; 3PB1; -.
PDBsum; 3Q02; -.
PDBsum; 3Q03; -.
PDBsum; 3R4L; -.
PDBsum; 3UT3; -.
PDBsum; 4AQH; -.
PDBsum; 4G8O; -.
PDBsum; 4G8R; -.
PDBsum; 4IC0; -.
PDBsum; 5BRR; -.
PDBsum; 9PAI; -.
DisProt; DP00320; -.
ProteinModelPortal; P05121; -.
SMR; P05121; -.
BioGrid; 111091; 16.
IntAct; P05121; 13.
MINT; MINT-202409; -.
STRING; 9606.ENSP00000223095; -.
BindingDB; P05121; -.
ChEMBL; CHEMBL3475; -.
DrugBank; DB00009; Alteplase.
DrugBank; DB00029; Anistreplase.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB05254; Plasmin.
DrugBank; DB00015; Reteplase.
DrugBank; DB00031; Tenecteplase.
DrugBank; DB00197; Troglitazone.
DrugBank; DB00013; Urokinase.
MEROPS; I04.020; -.
iPTMnet; P05121; -.
PhosphoSitePlus; P05121; -.
UniCarbKB; P05121; -.
BioMuta; SERPINE1; -.
DMDM; 129576; -.
OGP; P05121; -.
SWISS-2DPAGE; P05121; -.
EPD; P05121; -.
MaxQB; P05121; -.
PaxDb; P05121; -.
PeptideAtlas; P05121; -.
PRIDE; P05121; -.
DNASU; 5054; -.
Ensembl; ENST00000223095; ENSP00000223095; ENSG00000106366. [P05121-1]
GeneID; 5054; -.
KEGG; hsa:5054; -.
UCSC; uc003uxt.4; human. [P05121-1]
CTD; 5054; -.
DisGeNET; 5054; -.
EuPathDB; HostDB:ENSG00000106366.8; -.
GeneCards; SERPINE1; -.
HGNC; HGNC:8583; SERPINE1.
HPA; HPA050039; -.
MalaCards; SERPINE1; -.
MIM; 173360; gene.
MIM; 613329; phenotype.
neXtProt; NX_P05121; -.
OpenTargets; ENSG00000106366; -.
Orphanet; 465; Congenital plasminogen activator inhibitor type 1 deficiency.
PharmGKB; PA261; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00900000140788; -.
HOGENOM; HOG000238519; -.
HOVERGEN; HBG106493; -.
InParanoid; P05121; -.
KO; K03982; -.
OMA; PYEKEVP; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; P05121; -.
TreeFam; TF352620; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
SIGNOR; P05121; -.
ChiTaRS; SERPINE1; human.
EvolutionaryTrace; P05121; -.
GeneWiki; Plasminogen_activator_inhibitor-1; -.
GenomeRNAi; 5054; -.
PMAP-CutDB; P05121; -.
PRO; PR:P05121; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106366; -.
CleanEx; HS_SERPINE1; -.
ExpressionAtlas; P05121; baseline and differential.
Genevisible; P05121; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0001300; P:chronological cell aging; IEP:BHF-UCL.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
GO; GO:0030195; P:negative regulation of blood coagulation; IC:BHF-UCL.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:BHF-UCL.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0061044; P:negative regulation of vascular wound healing; IGI:BHF-UCL.
GO; GO:0061045; P:negative regulation of wound healing; IC:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:BHF-UCL.
GO; GO:0035491; P:positive regulation of leukotriene production involved in inflammatory response; IMP:BHF-UCL.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IMP:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0010469; P:regulation of receptor activity; IDA:BHF-UCL.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Glycoprotein; Polymorphism;
Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 23
CHAIN 24 402 Plasminogen activator inhibitor 1.
/FTId=PRO_0000032499.
SITE 369 370 Reactive bond.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 31 45 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045493.
VARIANT 15 15 A -> T (in dbSNP:rs6092).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:9194591,
ECO:0000269|Ref.8}.
/FTId=VAR_007099.
VARIANT 17 17 V -> I (in dbSNP:rs6090).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.8}.
/FTId=VAR_011750.
VARIANT 25 25 H -> P (in dbSNP:rs2227647).
{ECO:0000269|Ref.8}.
/FTId=VAR_013086.
VARIANT 209 209 R -> H (in dbSNP:rs2227669).
{ECO:0000269|Ref.8}.
/FTId=VAR_013087.
VARIANT 255 255 T -> N (in dbSNP:rs2227685).
{ECO:0000269|Ref.8}.
/FTId=VAR_013088.
CONFLICT 53 53 R -> A (in Ref. 7; CAA31208).
{ECO:0000305}.
CONFLICT 55 55 V -> L (in Ref. 2; AAA60009).
{ECO:0000305}.
CONFLICT 75 75 G -> V (in Ref. 7; CAA31208).
{ECO:0000305}.
CONFLICT 138 138 R -> K (in Ref. 7; CAA31208).
{ECO:0000305}.
CONFLICT 226 226 A -> V (in Ref. 9; BAH12656).
{ECO:0000305}.
CONFLICT 280 282 QLI -> HVM (in Ref. 7; CAA31208).
{ECO:0000305}.
HELIX 27 49 {ECO:0000244|PDB:1LJ5}.
STRAND 51 53 {ECO:0000244|PDB:4IC0}.
STRAND 55 57 {ECO:0000244|PDB:1LJ5}.
HELIX 59 72 {ECO:0000244|PDB:1LJ5}.
HELIX 75 85 {ECO:0000244|PDB:1LJ5}.
HELIX 94 106 {ECO:0000244|PDB:1LJ5}.
HELIX 108 110 {ECO:0000244|PDB:1LJ5}.
STRAND 111 123 {ECO:0000244|PDB:1LJ5}.
HELIX 132 140 {ECO:0000244|PDB:1LJ5}.
STRAND 145 147 {ECO:0000244|PDB:1LJ5}.
HELIX 149 151 {ECO:0000244|PDB:3UT3}.
HELIX 152 165 {ECO:0000244|PDB:1LJ5}.
TURN 166 169 {ECO:0000244|PDB:1LJ5}.
STRAND 170 172 {ECO:0000244|PDB:9PAI}.
HELIX 176 179 {ECO:0000244|PDB:4G8R}.
STRAND 186 200 {ECO:0000244|PDB:1LJ5}.
HELIX 204 206 {ECO:0000244|PDB:3CVM}.
STRAND 209 213 {ECO:0000244|PDB:1LJ5}.
STRAND 216 218 {ECO:0000244|PDB:1C5G}.
STRAND 219 237 {ECO:0000244|PDB:1LJ5}.
TURN 239 241 {ECO:0000244|PDB:1C5G}.
STRAND 243 251 {ECO:0000244|PDB:1LJ5}.
STRAND 254 265 {ECO:0000244|PDB:1LJ5}.
HELIX 271 274 {ECO:0000244|PDB:1LJ5}.
HELIX 279 288 {ECO:0000244|PDB:1LJ5}.
STRAND 290 299 {ECO:0000244|PDB:1LJ5}.
STRAND 301 308 {ECO:0000244|PDB:1LJ5}.
HELIX 310 315 {ECO:0000244|PDB:1LJ5}.
HELIX 320 322 {ECO:0000244|PDB:1LJ5}.
TURN 324 326 {ECO:0000244|PDB:1LJ5}.
TURN 330 332 {ECO:0000244|PDB:1LJ5}.
STRAND 334 336 {ECO:0000244|PDB:1LJ5}.
STRAND 340 351 {ECO:0000244|PDB:1LJ5}.
STRAND 353 368 {ECO:0000244|PDB:1LJ5}.
STRAND 374 376 {ECO:0000244|PDB:3CVM}.
STRAND 380 387 {ECO:0000244|PDB:1LJ5}.
TURN 388 391 {ECO:0000244|PDB:1LJ5}.
STRAND 392 400 {ECO:0000244|PDB:1LJ5}.
SEQUENCE 402 AA; 45060 MW; A2E181ED28DD6082 CRC64;
MQMSPALTCL VLGLALVFGE GSAVHHPPSY VAHLASDFGV RVFQQVAQAS KDRNVVFSPY
GVASVLAMLQ LTTGGETQQQ IQAAMGFKID DKGMAPALRH LYKELMGPWN KDEISTTDAI
FVQRDLKLVQ GFMPHFFRLF RSTVKQVDFS EVERARFIIN DWVKTHTKGM ISNLLGKGAV
DQLTRLVLVN ALYFNGQWKT PFPDSSTHRR LFHKSDGSTV SVPMMAQTNK FNYTEFTTPD
GHYYDILELP YHGDTLSMFI AAPYEKEVPL SALTNILSAQ LISHWKGNMT RLPRLLVLPK
FSLETEVDLR KPLENLGMTD MFRQFQADFT SLSDQEPLHV AQALQKVKIE VNESGTVASS
STAVIVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM EP


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