P50449 · PAI1_NEOVI

Function

function

Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence (By similarity).
Plays a role in alveolar type 2 cells senescence in the lung (By similarity).
Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (By similarity).

Features

Showing features for site.

140050100150200250300350400
TypeIDPosition(s)Description
Site367-368Reactive bond

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processnegative regulation of plasminogen activation
Biological Processnegative regulation of vascular wound healing
Biological Processreplicative senescence

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Plasminogen activator inhibitor 1
  • Short names
    PAI; PAI-1
  • Alternative names
    • Endothelial plasminogen activator inhibitor
    • Serpin E1

Gene names

    • Name
      SERPINE1
    • Synonyms
      PAI-1, PAI1, PLANH1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Musteloidea > Mustelidae > Mustelinae > Neogale

Accessions

  • Primary accession
    P50449

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000003250122-400Plasminogen activator inhibitor 1
Glycosylation230N-linked (GlcNAc...) asparagine
Glycosylation286N-linked (GlcNAc...) asparagine
Glycosylation350N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Subunit

Forms a heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Interacts with PPP1CB. In complex with PLAU/uPA, interacts with PLAUR/uPAR (By similarity).
Interacts with SORL1 and LRP1, either alone or in complex with PLAU; these interactions are abolished in the presence of LRPAP1/RAP (By similarity).
The ternary complex composed of PLAUR-PLAU-PAI1 also interacts with SORL1 (By similarity).
Also interacts with SORL1, when complexed to PLAT/tPA (By similarity).

Structure

Family & Domains

Sequence similarities

Belongs to the serpin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    400
  • Mass (Da)
    45,153
  • Last updated
    1996-10-01 v1
  • Checksum
    DF45E0694DE28401
MQMSTVCLALGLALVFGEASASYLHETRAAELATDFGVKVFKQVAQASKDRNMVFSPYGLASVLAMLQLTTAGETRQQIQEAMRFQIDEKGMAPALRQLYKELMGPWNKDEISTADAIFVQRDLKLVHGFMPYFFRLFQTTVKQVDFSEVERARFIINDWVKRHTKGMIGDLLGRGTVDQLTRLMLVNALYFNGQWKTPFPKSGTHHRLFHKSDGSTVSVPMMAQTNKFNYTEFSTPEGRYYDILELPYHGDTLSMFIAAPYEKDVPLSALTNILDAQLISQWKGNMTRRLRLLVLPKFSLESEVNLRGPLENLGMTDMFRPNQADFSSLSDQEALYVSQALQKVKIEVNESGTVASSSTAIIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X58541
EMBL· GenBank· DDBJ
CAA41433.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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