Plg
entrez
18815
canonical
uniprot
P20918
canonical
ensembl
ENSMUSG00000059481
resolver
ensp
ENSMUSP00000014578
resolver
enst
ENSMUST00000014578
resolver
genesymbol
Plg
resolver
uniprot
Q3V1T9
resolver
uniprot
Q8CIS2
resolver
uniprot
Q91WJ5
resolver
uniprot_entry
PLMN_MOUSE
resolver
uniprot_entry
Q3V1T9_MOUSE
resolver
uniprot_sec
Q8CIS2
resolver
uniprot_sec
Q91WJ5
resolver
activity_regulation
ACTIVITY REGULATION: [Plasmin]: Converted into plasmin by tissue-type (PLAT) and urokinase-type (PLAU) plasminogen activator. The activation by PLAT is enhanced by fibrin at the surface of blood clots. The partial proteolysis of fibrin by plasmin mainly exposes C-terminal lysine residues which in turn help recruit and activate plasminogen. The activation by PLAU occurs at the surface of cells and is more specific of extracellular matrix remodeling. Activated by streptokinase. Plasmin activity is also inhibited by SERPINF2; plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot. {ECO:0000250|UniProtKB:P00747}.
uniprot
proteins
amino_acid_sequence
MDHKEVILLFLLLLKPGQGDSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRNN
uniprot
proteins
ec_number
3.4.21.7
uniprot
proteins
function
FUNCTION: [Plasmin]: Protease which primary function is to degrade fibrin, the main component of blood clots. Also cleaves other components of blood clots like thrombospondin-1/THBS1 and von Willebrand factor/VWF. Can also directly and/or through the activation of other proteases degrade the various components of the extracellular matrix including collagen, fibronectin and laminin. Thereby, regulates a variety of biological processes including embryonic development, tissue remodeling, and inflammation (By similarity). In ovulation, weakens the walls of the Graafian follicle (By similarity). In vitro, it is also able to cleave several complement zymogens, such as C1, C4 and C5 (By similarity). {ECO:0000250|UniProtKB:P00747, ECO:0000250|UniProtKB:Q01177}.; FUNCTION: [Angiostatin]: Has an antiangiogenic activity and inhibits neovascularization. Could act through the inhibition of the ATP synthase subunit ATP5F1A. {ECO:0000250|UniProtKB:P00747}.
uniprot
proteins
mass_dalton
90808
uniprot
proteins
post_translational_modification
PTM: [Plasmin]: Activation requires cleavage in two chains held together by two disulfide bonds. Removal of the activation peptide is also part of the activation mechanisms. {ECO:0000250|UniProtKB:P00747}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
protein_family
Plasminogen subfamily
uniprot
proteins
pubmed
12149246
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
2081600
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7525077
uniprot
proteins
sequence_length
812
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Plasmin]: Secreted {ECO:0000250|UniProtKB:P00747}. 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. {ECO:0000250|UniProtKB:P00747}.; SUBCELLULAR LOCATION: [Angiostatin]: Secreted {ECO:0000250|UniProtKB:P00747}.
uniprot
proteins