Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Serpine1. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the serine proteinase inhibitor (serpin) superfamily. This member is the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), and hence is an inhibitor of fibrinolysis. Defects in this gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the gene product are associated with thrombophilia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Serpine1
  • participates in the following biological processes:
    • negative regulation of endopeptidase activity ^[5]
    • regulation of angiogenesis ^[4]
  • performs the following molecular functions:
    • serine-type endopeptidase inhibitor activity ^[5]
• The gene product of Serpine1 has been shown to bind to the gene products of Tmprss11e. ^{[5, 6]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Serpine1
  • participates in the following biological processes:
    • defense response to Gram-negative bacterium ^[8]
    • negative regulation of plasminogen activation ^[2]
    • negative regulation of vascular wound healing ^[3]
    • positive regulation of angiogenesis ^[1]
• Researchers have inferred, based on genetic interactions, that the gene product of Serpine1
  • participates in the following biological processes:
    • regulation of cell proliferation based on interactions with Apc ^[7]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Serpine1:
  • participates in the following biological processes:
    • cellular response to chemical stimulus
    • cellular response to lipopolysaccharide
    • defense response to Gram-negative bacterium
    • negative regulation of apoptotic process
    • negative regulation of cell adhesion mediated by integrin
    • negative regulation of cell migration
    • negative regulation of endopeptidase activity
    • negative regulation of fibrinolysis
    • negative regulation of plasminogen activation
    • negative regulation of smooth muscle cell migration
    • negative regulation of smooth muscle cell-matrix adhesion
    • negative regulation of vascular wound healing
    • positive regulation of angiogenesis
    • positive regulation of blood coagulation
    • positive regulation of coagulation
    • positive regulation of inflammatory response
    • positive regulation of interleukin-8 production
    • positive regulation of leukotriene production involved in inflammatory response
    • positive regulation of monocyte chemotaxis
    • positive regulation of receptor-mediated endocytosis
    • regulation of receptor activity
    • wound healing
  • performs the following molecular functions:
    • protease binding
    • serine-type endopeptidase inhibitor activity
  • is located in the following cellular components:
    • extracellular matrix
    • extracellular region
    • extracellular space

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Serpine1 indicates that it:
  • participates in the following biological processes:
    • negative regulation of peptidase activity
  • performs the following molecular functions:
    • peptidase inhibitor activity

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References

1. Bajou K et al. (2008) Plasminogen activator inhibitor-1 protects endothelial cells from FasL-mediated apoptosis. Cancer Cell, 14:324-34. (PubMed:18835034)
2. Boulaftali Y et al. (2010) Anticoagulant and antithrombotic properties of platelet protease nexin-1. Blood, 115:97-106. (PubMed:19855083)
3. Carmeliet P et al. (1997) Inhibitory role of plasminogen activator inhibitor-1 in arterial wound healing and neointima formation: a gene targeting and gene transfer study in mice [see comments] Circulation, 96:3180-91. (PubMed:9386191)
4. Devy L et al. (2002) The pro- or antiangiogenic effect of plasminogen activator inhibitor 1 is dose dependent. FASEB J, 16:147-54. (PubMed:11818362)
5. Hobson JP et al. (2004) Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes. J Biol Chem, 279:46981-94. (PubMed:15328353)
6. Lang IM et al. (1996) Purification of storage granule protein-23. A novel protein identified by phage display technology and interaction with type I plasminogen activator inhibitor. J Biol Chem, 271:30126-35. (PubMed:8939962)
7. Mutoh M et al. (2008) Plasminogen activator inhibitor-1 (Pai-1) blockers suppress intestinal polyp formation in Min mice. Carcinogenesis, 29:824-9. (PubMed:18258607)
8. Renckens R et al. (2007) Plasminogen activator inhibitor type 1 is protective during severe Gram-negative pneumonia. Blood, 109:1593-601. (PubMed:17032919)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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