Detail Information for IndEnz0002008045
IED ID IndEnz0002008045
Enzyme Type ID protease008045
Protein Name Plasminogen
EC 3.4.21.7

Cleaved into: Plasmin heavy chain A; Activation peptide; Plasmin heavy chain A, short form; Plasmin light chain B
Gene Name PLG
Organism Bos taurus (Bovine)
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MLPASPKMEHKAVVFLLLLFLKSGLGDLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGRIVGGCVSKPHSWPWQVSLRRSSRHFCGGTLISPKWVLTAAHCLDNILALSFYKVILGAHNEKVREQSVQEIPVSRLFREPSQADIALLKLSRPAIITKEVIPACLPPPNYMVAARTECYITGWGETQGTFGEGLLKEAHLPVIENKVCNRNEYLDGRVKPTELCAGHLIGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSPYVPWIEETMRRN
Enzyme Length 812
Uniprot Accession Number P06868
Absorption
Active Site ACT_SITE 624; /note=Charge relay system; ACT_SITE 667; /note=Charge relay system; ACT_SITE 762; /note=Charge relay system
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}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (4); Disulfide bond (24); Domain (7); Glycosylation (2); Modified residue (1); Peptide (1); Sequence conflict (4); Signal peptide (1)
Keywords Blood coagulation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Fibrinolysis;Glycoprotein;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 600; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00747
Post Translational Modification PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:3846532}.; PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-583, 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..26; /evidence=ECO:0000269|PubMed:3846532
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 91,216
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda