P20918 · PLMN_MOUSE
- ProteinPlasminogen
- GenePlg
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids812 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (By similarity).
Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Miscellaneous
Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
In the presence of the inhibitor, the activation involves only cleavage after Arg-581, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide.
Catalytic activity
Activity regulation
Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 624 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 667 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 762 | Charge relay system | ||||
Sequence: S |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePlasminogen
- EC number
- Cleaved into 5 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP20918
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for signal, peptide, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MDHKEVILLFLLLLKPGQG | ||||||
Peptide | PRO_0000028071 | 20-97 | Activation peptide | |||
Sequence: DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKR | ||||||
Chain | PRO_0000028070 | 20-581 | Plasmin heavy chain A | |||
Sequence: DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGR | ||||||
Chain | PRO_0000028069 | 20-812 | Plasminogen | |||
Sequence: DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRNN | ||||||
Disulfide bond | 49↔73 | |||||
Sequence: CLAKCEGETDFVCRSFQYHSKEQQC | ||||||
Disulfide bond | 53↔61 | |||||
Sequence: CEGETDFVC | ||||||
Chain | PRO_0000028073 | 98-?436 | Angiostatin | |||
Sequence: VYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPW | ||||||
Chain | PRO_0000028072 | 98-581 | Plasmin heavy chain A, short form | |||
Sequence: VYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGR | ||||||
Disulfide bond | 103↔181 | |||||
Sequence: CKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPEC | ||||||
Disulfide bond | 124↔164 | |||||
Sequence: CQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWC | ||||||
Disulfide bond | 152↔176 | |||||
Sequence: CRNPDNDEQGPWCYTTDPDKRYDYC | ||||||
Disulfide bond | 185↔262 | |||||
Sequence: CMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRC | ||||||
Disulfide bond | 188↔316 | |||||
Sequence: CSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPC | ||||||
Disulfide bond | 206↔245 | |||||
Sequence: CQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWC | ||||||
Disulfide bond | 234↔257 | |||||
Sequence: CRNPDGEPRPWCFTTDPTKRWEYC | ||||||
Disulfide bond | 275↔352 | |||||
Sequence: CLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC | ||||||
Disulfide bond | 296↔335 | |||||
Sequence: CQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWC | ||||||
Disulfide bond | 324↔347 | |||||
Sequence: CRNPDGETAPWCYTTDSQLRWEYC | ||||||
Disulfide bond | 377↔454 | |||||
Sequence: CYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRC | ||||||
Disulfide bond | 398↔437 | |||||
Sequence: CQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWC | ||||||
Disulfide bond | 426↔449 | |||||
Sequence: CRNPDGDKGPWCYTTDPSVRWEYC | ||||||
Disulfide bond | 481↔560 | |||||
Sequence: CMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLC | ||||||
Disulfide bond | 502↔543 | |||||
Sequence: CQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWC | ||||||
Disulfide bond | 531↔555 | |||||
Sequence: CRNPDGDVNGPWCYTTNPRKLYDYC | ||||||
Disulfide bond | 568↔687 | Interchain (between A and B chains) | ||||
Sequence: CGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPAC | ||||||
Disulfide bond | 578↔586 | Interchain (between A and B chains) | ||||
Sequence: CPGRVVGGC | ||||||
Chain | PRO_0000028074 | 582-812 | Plasmin light chain B | |||
Sequence: VVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRNN | ||||||
Modified residue | 598 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 609↔625 | |||||
Sequence: CGGTLIAPEWVLTAAHC | ||||||
Modified residue | 690 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 701↔768 | |||||
Sequence: CYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVC | ||||||
Disulfide bond | 731↔747 | |||||
Sequence: CNRVEYLNNRVKSTELC | ||||||
Disulfide bond | 758↔786 | |||||
Sequence: CQGDSGGPLVCFEKDKYILQGVTSWGLGC |
Post-translational modification
In the presence of the inhibitor, the activation involves only cleavage after Arg-581, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts (both mature PLG and the angiostatin peptide) with AMOT and CSPG4. 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
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-98 | PAN | ||||
Sequence: DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRV | ||||||
Domain | 103-181 | Kringle 1 | ||||
Sequence: CKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPEC | ||||||
Domain | 184-262 | Kringle 2 | ||||
Sequence: ECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRC | ||||||
Domain | 275-352 | Kringle 3 | ||||
Sequence: CLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC | ||||||
Domain | 377-454 | Kringle 4 | ||||
Sequence: CYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRC | ||||||
Domain | 481-560 | Kringle 5 | ||||
Sequence: CMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLC | ||||||
Domain | 582-810 | Peptidase S1 | ||||
Sequence: VVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMR |
Domain
Kringle domains mediate interaction with CSPG4.
Sequence similarities
Belongs to the peptidase S1 family. Plasminogen subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length812
- Mass (Da)90,808
- Last updated2011-06-28 v3
- ChecksumE70E1AC8E52844E9
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 235 | in Ref. 1; AAA50168 | ||||
Sequence: R → H | ||||||
Sequence conflict | 525 | in Ref. 1; AAA50168 | ||||
Sequence: G → D | ||||||
Sequence conflict | 649 | in Ref. 2; AAM22156 and 4; AAH14773/AAH57186 | ||||
Sequence: L → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04766 EMBL· GenBank· DDBJ | AAA50168.1 EMBL· GenBank· DDBJ | mRNA | ||
AF481053 EMBL· GenBank· DDBJ | AAM22156.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC087901 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC014773 EMBL· GenBank· DDBJ | AAH14773.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057186 EMBL· GenBank· DDBJ | AAH57186.1 EMBL· GenBank· DDBJ | mRNA | ||
AY134430 EMBL· GenBank· DDBJ | AAN15805.1 EMBL· GenBank· DDBJ | Genomic DNA |