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edit Plasminogen PDB rendering based on 1b2i. Available structures PDB 1B2I, 1BML, 1BUI, 1CEA, 1CEB, 1DDJ, 1HPJ, 1HPK, 1I5K, 1I71, 1JFN, 1KI0, 1KIV, 1KRN, 1L4D, 1L4Z, 1PK4, 1PKR, 1PMK, 1QRZ, 1RJX, 2DOH, 2DOI, 2FEB, 2KNF, 2L0S, 2PK4, 3KIV, 4KIV, 5HPG Identifiers Symbols PLG; DKFZp779M0222 External IDs OMIM: 173350 MGI: 97620 HomoloGene: 55452 GeneCards: PLG Gene EC number Gene Ontology Molecular function • serine-type endopeptidase activity • serine-type endopeptidase activity • serine-type endopeptidase activity • protein binding • peptidase activity • apolipoprotein binding • cell surface binding Cellular component • extracellular region • extracellular region • extracellular space • plasma membrane • platelet alpha granule lumen • extrinsic to external side of plasma membrane Biological process • platelet degranulation • proteolysis • blood coagulation • blood coagulation • negative regulation of cell proliferation • negative regulation of cell-substrate adhesion • extracellular matrix disassembly • platelet activation • fibrinolysis • tissue remodeling • negative regulation of fibrinolysis • positive regulation of fibrinolysis Sources: Amigo / QuickGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 5340 18815 Ensembl ENSG00000122194 ENSMUSG00000059481 UniProt P00747 Q3V1T9 RefSeq (mRNA) NM_000301.3 NM_008877.3 RefSeq (protein) NP_000292.1 NP_032903.3 Location (UCSC) Chr 6: 161.12 - 161.17 Mb Chr 17: 12.57 - 12.61 Mb PubMed search [1] [2] Plasmin is an important enzyme (EC present in blood that degrades many blood plasma proteins, most notably, fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the PLG gene.[1] Contents 1 Function 2 Pathology 3 Interactions 4 References 5 Further reading 6 External links Function Plasmin is a serine protease that acts to dissolve fibrin blood clots. Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system and weakens the wall of the Graafian follicle (leading to ovulation). It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor. Plasmin, like trypsin, belongs to the family of serine proteases. Plasmin is released as a zymogen called plasminogen (PLG) from the liver into the systemic circulation. Plasminogen is converted into active plasmin by a variety of enzymes, including tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), kallikrein, and factor XII (Hageman factor). Fibrin is a cofactor for plasminogen activation by tissue plasminogen activator. Urokinase plasminogen activator receptor (uPAR) is a cofactor for plasminogen activation by urokinase plasminogen activator. The conversion of plasminogen to plasmin involves the cleavage of the peptide bond between Arg-560 and Val-561.[1][2][3] Plasmin cleavage produces angiostatin. Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition. Pathology Deficiency in plasmin may lead to thrombosis, as clots are not degraded adequately. Plasminogen deficiency in mice leads to defective liver repair,[4] defective wound healing, reproductive abnormalities.[citation needed] In human, a rare disorder called plasminogen deficiency type I (OMIM 217090) is caused by mutations of the PLG gene and is often manifested by ligneous conjunctivitis. Interactions Plasmin has been shown to interact with Thrombospondin 1,[5][6] Alpha 2-antiplasmin[7][8] and IGFBP3.[9] References ^ a b "Entrez Gene: plasminogen".  ^ Miyata T, Iwanaga S, Sakata Y, Aoki N (October 1982). "Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site". Proc. Natl. Acad. Sci. U.S.A. 79 (20): 6132–6. doi:10.1073/pnas.79.20.6132. PMC 347073. PMID 6216475.  ^ Forsgren M, Råden B, Israelsson M, Larsson K, Hedén LO (March 1987). "Molecular cloning and characterization of a full-length cDNA clone for human plasminogen". FEBS Lett. 213 (2): 254–60. doi:10.1016/0014-5793(87)81501-6. PMID 3030813.  ^ Jorge A. Bezerra, Thomas H. Bugge, Hector Melin-Aldana, Gregg Sabla, Keith W. Kombrinck, David P. Witte, and Jay L. Degen (December 21, 1999). Plasminogen deficiency leads to impaired remodeling after a toxic injury to the liver. Proceedings of the National Academy of Sciences of the United States of America. PMID 10611352. Retrieved June 03, 2011.  ^ Silverstein, R L; Leung L L, Harpel P C, Nachman R L (Nov. 1984). "Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator". J. Clin. Invest. (UNITED STATES) 74 (5): 1625–33. doi:10.1172/JCI111578. ISSN 0021-9738. PMC 425339. PMID 6438154.  ^ DePoli, P; Bacon-Baguley T, Kendra-Franczak S, Cederholm M T, Walz D A (Mar. 1989). "Thrombospondin interaction with plasminogen. Evidence for binding to a specific region of the kringle structure of plasminogen". Blood (UNITED STATES) 73 (4): 976–82. ISSN 0006-4971. PMID 2522013.  ^ Wiman, B; Collen D (Sep. 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. Chem. (UNITED STATES) 254 (18): 9291–7. ISSN 0021-9258. PMID 158022.  ^ Shieh, B H; Travis J (May. 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. (UNITED STATES) 262 (13): 6055–9. ISSN 0021-9258. PMID 2437112.  ^ Campbell, P G; Durham S K, Suwanichkul A, Hayes J D, Powell D R (Aug. 1998). "Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3". Am. J. Physiol. (UNITED STATES) 275 (2 Pt 1): E321–31. ISSN 0002-9513. PMID 9688635.  Further reading Shanmukhappa K, Mourya R, Sabla GE, Degen JL, Bezerra JA (July 2005). "Hepatic to pancreatic switch defines a role for hemostatic factors in cellular plasticity in mice". Proc. Natl. Acad. Sci. U.S.A. 102 (29): 10182–7. doi:10.1073/pnas.0501691102. PMC 1177369. PMID 16006527.  Anglés-Cano E, Rojas G (2003). "Apolipoprotein(a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site". Biol. Chem. 383 (1): 93–9. doi:10.1515/BC.2002.009. PMID 11928826.  Ranson M, Andronicos NM (2004). "Plasminogen binding and cancer: promises and pitfalls". Front. Biosci. 8: s294–304. doi:10.2741/1044. PMID 12700073.  v · d · ePDB gallery 1b2i: KRINGLE 2 DOMAIN OF HUMAN PLASMINOGEN: NMR SOLUTION STRUCTURE OF TRANS-4-AMINOMETHYLCYCLOHEXANE-1-CARBOXYLIC ACID (AMCHA) COMPLEX   1bml: COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE   1bui: STRUCTURE OF THE TERNARY MICROPLASMIN-STAPHYLOKINASE-MICROPLASMIN COMPLEX: A PROTEINASE-COFACTOR-SUBSTRATE COMPLEX IN ACTION.   1cea: THE STRUCTURE OF THE NON-COVALENT COMPLEX OF RECOMBINANT KRINGLE 1 DOMAIN OF HUMAN PLASMINOGEN WITH EACA (EPSILON-AMINOCAPROIC ACID)   1ceb: THE STRUCTURE OF THE NON-COVALENT COMPLEX OF RECOMBINANT KRINGLE 1 DOMAIN OF HUMAN PLASMINOGEN WITH AMCHA (TRANS-4-AMINOMETHYLCYCLOHEXANE-1-CARBOXYLIC ACID)   1ddj: CRYSTAL STRUCTURE OF HUMAN PLASMINOGEN CATALYTIC DOMAIN   1hpj: SOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, 12 STRUCTURES   1hpk: SOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, MINIMIZED AVERAGE STRUCTURE   1i5k: STRUCTURE AND BINDING DETERMINANTS OF THE RECOMBINANT KRINGLE-2 DOMAIN OF HUMAN PLASMINOGEN TO AN INTERNAL PEPTIDE FROM A GROUP A STREPTOCOCCAL SURFACE PROTEIN   1ki0: The X-ray Structure of Human Angiostatin   1krn: STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION   1l4d: CRYSTAL STRUCTURE OF MICROPLASMINOGEN-STREPTOKINASE ALPHA DOMAIN COMPLEX   1l4z: X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS   1pk4: CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN PLASMINOGEN KRINGLE 4 REFINED AT 1.9-ANGSTROMS RESOLUTION   1pkr: THE STRUCTURE OF RECOMBINANT PLASMINOGEN KRINGLE 1 AND THE FIBRIN BINDING SITE   1pmk: KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES   1qrz: CATALYTIC DOMAIN OF PLASMINOGEN   1rjx: Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT   2doh: The X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound a to a peptide from the group A streptococcal surface protein PAM   2doi: The X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcus protein PAM   2pk4: THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE   5hpg: STRUCTURE AND LIGAND DETERMINANTS OF THE RECOMBINANT KRINGLE 5 DOMAIN OF HUMAN PLASMINOGEN   External links The MEROPS online database for peptidases and their inhibitors: S01.233 MeSH Plasmin This article incorporates text from the United States National Library of Medicine, which is in the public domain. v · d · eProteins: Globular proteins Serum globulins Alpha globulins serpins: alpha-1 (Alpha 1-antichymotrypsin, Alpha 1-antitrypsin) · alpha-2 (Alpha 2-antiplasmin) · Antithrombin (Heparin cofactor II) carrier proteins: alpha-1 (Transcortin) · alpha-2 (Ceruloplasmin) · Retinol binding protein other: alpha-1 (Orosomucoid) · alpha-2 (alpha-2-Macroglobulin, Haptoglobin) Beta globulins carrier proteins: Sex hormone-binding globulin · Transferrin other: Angiostatin · Hemopexin · Beta-2 microglobulin · Factor H · Plasminogen · Properdin Gamma globulin Immunoglobulins Other Fibronectin (Fetal fibronectin) · Macroglobulin/Microglobulin · Transcobalamin Other globulins Beta-lactoglobulin (Lactoferrin) · Thyroglobulin · Alpha-lactalbumin Albumins Egg white Conalbumin · Ovalbumin · Avidin Serum albumin Human serum albumin · Bovine serum albumin · Prealbumin Other C-reactive protein · Lactalbumin (Alpha-lactalbumin) · Parvalbumin · Ricin see also disorders of globin and globulin proteins B proteins: BY STRUCTURE: membrane, globular (en, ca, an), fibrous v · d · eProteins: coagulation Coagulation factors Primary hemostasis vWF platelet membrane glycoproteins: Ib (A, B, IX) · IIb/IIIa (IIb, IIIa) · VI Intrinsic pathway HMWK/Bradykinin · Prekallikrein/Kallikrein · XII "Hageman" XI · IX · VIII Extrinsic pathway III "Tissue factor" · VII Common pathway X · V · II "(Pro)thrombin" · I "Fibrin" · Fibrinogen (FGA, FGG) XIII Coagulation inhibitors Antithrombin (inhibits II, IX, X, XI, XII) · Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) · Protein Z (inhibits X) · ZPI (inhibits X, XI) · TFPI (inhibits III) Thrombolysis/fibrinolysis Plasmin · tPA/urokinase · PAI-1/2 · α2-AP · α2-macroglobulin · TAFI M: MYL cell/phys (coag, heme, immu, gran), csfs rbmg/mogr/tumr/hist, sysi/epon, btst drug (B1/2/3+5+6), btst, trns v · d · eEndopeptidases: serine proteases/serine endopeptidases (EC 3.4.21) Digestive enzymes Enteropeptidase · Trypsin · Chymotrypsin · Elastase (Neutrophil, Pancreatic) Coagulation factors: Thrombin · Factor VIIa · Factor IXa · Factor Xa · Factor XIa · Factor XIIa · Kallikrein (PSA, KLK1, KLK2, KLK3, KLK4, KLK5, KLK6, KLK7, KLK8, KLK9, KLK10, KLK11, KLK12, KLK13, KLK14, KLK15) fibrinolysis: Plasmin · Plasminogen activator (Tissue plasminogen activator · Urinary plasminogen activator) Complement system Factor B · Factor D · Factor I · MASP (MASP1, MASP2) · C3-convertase Other immune system Chymase · Granzyme · Tryptase · Proteinase 3/Myeloblastin Venombin Ancrod · Batroxobin Other Acrosin · Prolyl endopeptidase · Pronase · Proprotein convertases (1, 2) · Reelin · Subtilisin/Furin · Streptokinase · S1P · Cathepsin (A, G) B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7,, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6