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M3X3T9 · M3X3T9_FELCA

Function

function

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
    EC:3.4.21.7 (UniProtKB | ENZYME | Rhea)

Activity regulation

Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site158L-lysine (UniProtKB | ChEBI)
Binding site172L-lysine (UniProtKB | ChEBI)
Binding site428L-lysine (UniProtKB | ChEBI)
Binding site441L-lysine (UniProtKB | ChEBI)
Active site618Charge relay system
Active site661Charge relay system
Active site756Charge relay system

GO annotations

AspectTerm
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular space
Cellular Componentglutamatergic synapse
Cellular ComponentSchaffer collateral - CA1 synapse
Molecular Functionapolipoprotein binding
Molecular Functionendopeptidase activity
Molecular Functionkinase binding
Molecular Functionprotease binding
Molecular Functionprotein antigen binding
Molecular Functionprotein domain specific binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionserine-type endopeptidase activity
Molecular Functionsignaling receptor binding
Biological Processbiological process involved in interaction with symbiont
Biological Processblood coagulation
Biological Processextracellular matrix disassembly
Biological Processfibrinolysis
Biological Processlabyrinthine layer blood vessel development
Biological Processmononuclear cell migration
Biological Processmuscle cell cellular homeostasis
Biological Processmyoblast differentiation
Biological Processnegative regulation of cell-substrate adhesion
Biological Processnegative regulation of fibrinolysis
Biological Processpositive regulation of blood vessel endothelial cell migration
Biological Processpositive regulation of fibrinolysis
Biological Processprotein processing
Biological Processproteolysis
Biological Processtissue regeneration
Biological Processtissue remodeling
Biological Processtrans-synaptic signaling by BDNF, modulating synaptic transmission
Biological Processtrophoblast giant cell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Plasminogen
  • EC number

Gene names

    • Name
      PLG

Organism names

  • Taxonomic identifier
  • Strain
    • Abyssinian
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Felinae > Felis

Accessions

  • Primary accession
    M3X3T9

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_501625809120-806Plasminogen
Disulfide bond185↔262
Disulfide bond206↔245
Disulfide bond234↔257
Disulfide bond271↔348
Disulfide bond292↔331
Disulfide bond320↔343
Disulfide bond373↔450
Disulfide bond394↔433
Disulfide bond422↔445

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with CSPG4 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation. Interacts (via Kringle 4 domain) with ADA; the interaction stimulates PLG activation when in complex with DPP4. Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of the angiogenic effects of angiostatin.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain20-98Apple
Domain102-181Kringle
Domain184-262Kringle
Domain270-348Kringle
Domain372-450Kringle
Region454-477Disordered
Compositional bias457-471Polar residues
Domain476-556Kringle
Domain577-804Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    806
  • Mass (Da)
    90,360
  • Last updated
    2018-10-10 v3
  • MD5 Checksum
    9A1CB194EDA855A3711F1F9B3F9ED363
MEHKEVILLLLLFLKSGHGDPLDDYVNTQGASLVSLTKKQLSAGSIEECAARCEEETGFICRSFQYHSKEQHCVIMAENSKNSAVFRMRDVVLFEKKIYLSECKIGNGKSYRGTMSKTKNGVTCQKWSDNAPHKPNYSPDKYPAEGLEENYCRNPDSDEDGPWCYTTDPNKRFDYCDIPECEDECMHCSGENYEGKISKTISGIKCQSWNSQTPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPNKRWEFCDIPRCTTPGPTYECLKGKGENYRGKVSLTVSGHTCQRWSEQTPHKHNRTPENFPCKNLDENYCRNPDGETTPWCYTTNSEVRWEYCQIPSCESSPLSSEHLDAPVPPEQTPVVQECYRGNGQSYRGTSSTTITGKKCQPWSSMVPHRHVKTPERYPDAGLTMNYCRNPDADKSPWCYTTDPSVRWEFCNLKKCPDREESATKSPTVSQVPSAEDPSESDCMFGNGKGYRGKRATTVSGIPCQEWGAQEPHRHGIFTPVTNPQSGLEKNYCRNPDGDVNGPWCYTMSPRKLFDYCDVPQCASASFDCGKPQVEPKKCPGRVVGGCVANPHSWPWQVSLRTRFGQHFCGGTLIAPEWVLTAAHCLERSSRPAAYKVILGAHRELNLETDVQDIEVSKLFLEPTRADIALLKLSRSAVITSKVIPACLPPPNYVVADRTLCYITGWGDTQGTFGAGLLKEAQLPVIENKVCNRYEYLNGRVKSTELCAGNLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVPWIEGIMRNN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias457-471Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AANG04000169
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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