Plasminogen activator inhibitor-1

SERPINE1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1A7C, 1B3K, 1C5G, 1DB2, 1DVM, 1DVN, 1LJ5, 1OC0, 3CVM, 3EOX, 3PB1, 3Q02, 3Q03, 3R4L, 3UT3, 4AQH, 4G8O, 4G8R, 4IC0, 9PAI, 5BRR,%%s1C5G
Identifiers
Aliases	SERPINE1, PAI, PAI-1, PAI1, PLANH1, serpin family E member 1
External IDs	OMIM: 173360; MGI: 97608; HomoloGene: 68070; GeneCards: SERPINE1; OMA:SERPINE1 - orthologs
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q22.1 Start 101,127,104 bp[1] End 101,139,247 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 G2 Start 137,090,358 bp[2] End 137,101,122 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vena cava stromal cell of endometrium decidua saphenous vein ascending aorta gallbladder Descending thoracic aorta pericardium tibial arteries right coronary artery Top expressed in endothelial cell of lymphatic vessel stroma of bone marrow decidua tunica media of zone of aorta gastrula ascending aorta calvaria aortic valve muscle of thigh subcutaneous adipose tissue More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase inhibitor activity protease binding protein binding signaling receptor binding serine-type endopeptidase inhibitor activity Cellular component extracellular matrix plasma membrane extracellular exosome platelet alpha granule lumen extracellular region extracellular space collagen-containing extracellular matrix Biological process negative regulation of endothelial cell apoptotic process positive regulation of receptor-mediated endocytosis negative regulation of peptidase activity negative regulation of fibrinolysis positive regulation of inflammatory response negative regulation of plasminogen activation fibrinolysis negative regulation of smooth muscle cell-matrix adhesion negative regulation of blood coagulation negative regulation of vascular wound healing regulation of signaling receptor activity negative regulation of smooth muscle cell migration positive regulation of monocyte chemotaxis platelet degranulation extracellular matrix organization positive regulation of angiogenesis negative regulation of cell migration positive regulation of blood coagulation defense response to Gram-negative bacterium negative regulation of extrinsic apoptotic signaling pathway via death domain receptors circadian rhythm angiogenesis positive regulation of interleukin-8 production negative regulation of wound healing cellular response to lipopolysaccharide negative regulation of cell adhesion mediated by integrin negative regulation of endopeptidase activity positive regulation of transcription by RNA polymerase II positive regulation of leukotriene production involved in inflammatory response replicative senescence dentinogenesis positive regulation of odontoblast differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5054 18787 Ensembl ENSG00000106366 ENSMUSG00000037411 UniProt P05121 P22777 RefSeq (mRNA) NM_001165413 NM_000602 NM_008871 RefSeq (protein) NP_000593 NP_000593.1 NP_032897 Location (UCSC) Chr 7: 101.13 – 101.14 Mb Chr 5: 137.09 – 137.1 Mb PubMed search [3] [4]
Wikidata
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Plasminogen activator inhibitor-1 (PAI-1) also known as endothelial plasminogen activator inhibitor (serpin E1) is a protein that in humans is encoded by the SERPINE1 gene. Elevated PAI-1 is a risk factor for thrombosis and atherosclerosis.^[5]

PAI-1 is a serine protease inhibitor (serpin) that functions as the principal inhibitor of tissue-type plasminogen activator (tPA) and urokinase (uPA), the activators of plasminogen and hence fibrinolysis (the physiological breakdown of blood clots). It is a serine protease inhibitor (serpin) protein (SERPINE1).

The other PAI, plasminogen activator inhibitor-2 (PAI-2) is secreted by the placenta and only present in significant amounts during pregnancy. In addition, protease nexin acts as an inhibitor of tPA and urokinase. PAI-1, however, is the main inhibitor of the plasminogen activators.