Summary for peptidase S01.233: plasmin

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors Pharma

 

Names
MEROPS Nameplasmin
Other namesdelta-plasmin, fibrinase, fibrinolysin, plasminogen (activated), follicular regulatory protein, microplasmin, miniplasmin, TAL6003, ocriplasmin
Domain architecture
MEROPS Classification
Classification Clan PA >> Subclan PA(S) >> Family S1 >> Subfamily A >> S01.233
Holotypeplasmin (Homo sapiens), Uniprot accession P00747 (peptidase unit: 581-810), MERNUM MER0000175
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeSerine
PeplistIncluded in the Peplist with identifier PL00321
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.7
EnzymologyBRENDA database
Proteolytic eventsCutDB database (71 cleavages)
Activity statushuman: active (Castellino, 2004)
mouse: active (by similarity)
PhysiologyDegrades fibrin clots, but many additional physiologic roles have been proposed. In mouse, plasmin has been identified as an extracellular chemokine activator, enhancing the activity of monocyte chemoattractant protein-1 (MCP-1) by removal of its C-terminus (Sheehan et al., 2007).
KnockoutPlasminogen knockout mice showed severe thrombosis, and deposition of fibrin in the liver (Bugge et al., 1995). They also showed impaired wound-healing in the skin (Romer et al., 1996) and complete lack of infarct healing after myocardial infarction (Creemers et al., 2000). The plasminogen-deficient mice are resistant to excitotoxic neurodegeneration (Sheehan et al., 2007).
Pharmaceutical relevanceMicroplasmin has been described as a novel thrombolytic agent that improves behavioural outcome after embolic strokes in rabbits (Lapchak et al., 2002). An engineered, thrombin-activatable form of plasminogen has also shown promise as a thrombolytic agent (Comer et al., 2005).
Pathways KEGGComplement and coagulation cascades
KEGGInfluenza A
KEGGNeuroactive ligand-receptor interaction
KEGGStaphylococcus aureus infection
Other databases WIKIPEDIAhttp://en.wikipedia.org/wiki/Plasmin
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/RKScissile bond-/-/-/- (based on 126 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 10 10 8 0 11 4 7 12
Pro 18 2 12 0 0 5 11 11
Ala 16 9 11 0 20 8 9 9
Val 4 5 5 0 6 12 6 6
Leu 7 8 15 0 8 7 8 11
Ile 5 5 3 0 4 8 5 7
Met 2 1 2 0 3 0 2 2
Phe 2 4 11 0 3 8 4 7
Tyr 2 3 8 0 4 5 6 7
Trp 0 0 3 0 0 0 2 0
Ser 8 12 13 0 23 12 13 7
Thr 5 6 3 0 4 3 5 5
Cys 2 2 2 0 1 1 2 3
Asn 2 3 7 0 2 7 5 2
Gln 5 11 6 1 1 6 8 4
Asp 5 5 3 1 3 3 2 3
Glu 4 7 2 1 3 2 7 4
Lys 5 4 4 57 6 8 3 4
Arg 13 17 3 65 10 13 6 7
His 2 6 2 1 3 3 4 4
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
PLG 6q26 ENSG00000122194 5340 PLG 173350
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
Plg 17:A1 ENSMUSG00000014434 18815 MGI:97620