| IED ID | IndEnz0002013942 |
| Enzyme Type ID | protease013942 |
| Protein Name |
Plasminogen EC 3.4.21.7 Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B |
| Gene Name | Plg |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MDHKEVILLFLLLLKPGQGDSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRNN |
| Enzyme Length | 812 |
| Uniprot Accession Number | P20918 |
| Absorption | |
| Active Site | ACT_SITE 624; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 667; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 762; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7; |
| DNA Binding | |
| EC Number | 3.4.21.7 |
| Enzyme 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). {ECO:0000250}.; FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (5); Disulfide bond (24); Domain (7); Modified residue (2); Peptide (1); Sequence conflict (5); Signal peptide (1) |
| Keywords | Blood coagulation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Fibrinolysis;Hemostasis;Hydrolase;Kringle;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Tissue remodeling;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. 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). {ECO:0000250}. |
| Modified Residue | MOD_RES 598; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00747; MOD_RES 690; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00747 |
| Post Translational Modification | PTM: 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). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..19 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10318667; 10537128; 10559390; 10634603; 10642175; 10816371; 10854210; 10880388; 10885855; 10903997; 11003846; 11154109; 11306011; 11306532; 11404420; 11500461; 11557572; 11562346; 11641723; 11733368; 11818362; 11848464; 11916082; 11929773; 12070304; 12083480; 12167431; 12192005; 12225871; 12417566; 12428098; 12431907; 12524546; 12559391; 12657615; 12702502; 12857855; 12875972; 12900459; 12911578; 12911586; 12928439; 1387105; 14651966; 14709993; 14988509; 15099286; 15161662; 15166500; 15220341; 15333838; 15364412; 1543918; 15456492; 15486301; 15522965; 15545316; 15630096; 15721299; 1572657; 15737740; 15743790; 15760467; 15841177; 15985536; 16006527; 16103174; 1612602; 16141072; 16147977; 16150044; 16204191; 16330749; 16413499; 16481742; 16505491; 16543819; 16554301; 16615898; 16763560; 16818777; 16949567; 16956791; 16964442; 16966370; 17022820; 17122079; 17135368; 17267741; 17293777; 17301181; 17395831; 17431190; 17482686; 17596135; 17656680; 17664291; 17690254; 17717150; 17722076; 17988229; 18039665; 18042398; 18195371; 18311818; 18337830; 18371407; 18420257; 1845916; 18566672; 18608216; 18628488; 18647637; 18677407; 18685433; 18957535; 18997104; 19147818; 19210287; 19220707; 19273908; 19286661; 19465692; 19683575; 19897580; 20110420; 20133625; 20163454; 20175210; 20440070; 20547128; 20653841; 21062905; 21115493; 21190118; 21239499; 21267068; 21273553; 21311769; 21326869; 21354127; 21614211; 21704601; 21719761; 21931322; 21931850; 21940822; 22056679; 22079981; 22159717; 22563086; 22815383; 23041318; 23106863; 23202729; 23239981; 23401155; 23456978; 23527289; 23555246; 23646899; 23702659; 23721211; 23943648; 24090483; 24196407; 24574269; 24581498; 24650562; 24664548; 24732409; 24791857; 24876560; 25165151; 25209997; 25409527; 25893677; 25918552; 26214526; 26473342; 26647393; 26791370; 27283026; 27319402; 27530373; 27592166; 28071719; 28270519; 28275164; 28320709; 28325863; 28336948; 28686706; 29400711; 29438518; 30254165; 30323258; 30341568; 31101623; 31316511; 31395599; 31462325; 31690812; 31819012; 32694536; 33543002; 33720950; 33827130; 34378815; 34423816; 6216475; 7586361; 7705657; 7894168; 8084607; 8111116; 8406442; 8612226; 8704243; 8854860; 8929539; 8987777; 9226367; 9242524; 9268631; 9275201; 9294211; 9373263; 9438420; 9473227; 9490683; 9671388; 9770530; 9819364; 9884337; 9933568; |
| Motif | |
| Gene Encoded By | |
| Mass | 90,808 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |