ID PLMN_HUMAN Reviewed; 810 AA. AC P00747; Q15146; Q5TEH4; Q6PA00; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 27-MAR-2024, entry version 269. DE RecName: Full=Plasminogen {ECO:0000303|PubMed:2318848}; DE EC=3.4.21.7 {ECO:0000269|PubMed:2143188}; DE Contains: DE RecName: Full=Plasmin heavy chain A; DE Contains: DE RecName: Full=Activation peptide; DE Contains: DE RecName: Full=Angiostatin {ECO:0000303|PubMed:9102221}; DE Contains: DE RecName: Full=Plasmin heavy chain A, short form; DE Contains: DE RecName: Full=Plasmin light chain B; DE Flags: Precursor; GN Name=PLG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-472. RX PubMed=2318848; DOI=10.1016/s0021-9258(19)39298-1; RA Petersen T.E., Martzen M.R., Ichinose A., Davie E.W.; RT "Characterization of the gene for human plasminogen, a key proenzyme in the RT fibrinolytic system."; RL J. Biol. Chem. 265:6104-6111(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3030813; DOI=10.1016/0014-5793(87)81501-6; RA Forsgren M., Raden B., Israelsson M., Larsson K., Heden L.-O.; RT "Molecular cloning and characterization of a full-length cDNA clone for RT human plasminogen."; RL FEBS Lett. 213:254-260(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Browne M.J., Chapman C.G., Dodd I., Carey J.E., Lawrence G.M.P., RA Mitchell D., Robinson J.H.; RT "Expression of recombinant human plasminogen and aglycoplasminogen in HeLa RT cells."; RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-57; GLN-133; HIS-261; RP TRP-408; ASN-472; VAL-494 AND TRP-523. RG SeattleSNPs variation discovery resource; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-676. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 20-810, AND VARIANT ASN-472. RA Sottrup-Jensen L., Petersen T.E., Magnusson S.; RL Submitted (JUL-1977) to the PIR data bank. RN [8] RP PROTEIN SEQUENCE OF 20-100. RX PubMed=122932; DOI=10.1111/j.1432-1033.1975.tb09887.x; RA Wiman B., Wallen P.; RT "Structural relationship between 'glutamic acid' and 'lysine' forms of RT human plasminogen and their interaction with the NH2-terminal activation RT peptide as studied by affinity chromatography."; RL Eur. J. Biochem. 50:489-494(1975). RN [9] RP PROTEIN SEQUENCE OF 95-580; 581-626; 657-700 AND 732-810, AND VARIANT RP ASN-472. RA Sottrup-Jensen L., Claeys H., Zajdel M., Petersen T.E., Magnusson S.; RT "The primary structure of human plasminogen."; RL (In) Davidson J.F., Rowan R.M., Samama M.M., Desnoyers P.C. (eds.); RL Progress in chemical fibrinolysis and thrombolysis, pp.3:191-209, Raven RL Press, New York (1978). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-810. RX PubMed=6148961; DOI=10.1021/bi00313a035; RA Malinowski D.P., Sadler J.E., Davie E.W.; RT "Characterization of a complementary deoxyribonucleic acid coding for human RT and bovine plasminogen."; RL Biochemistry 23:4243-4250(1984). RN [11] RP PROTEIN SEQUENCE OF 483-604. RX PubMed=126863; DOI=10.1111/j.1432-1033.1975.tb02403.x; RA Wiman B., Wallen P.; RT "Amino-acid sequence of the cyanogen-bromide fragment from human RT plasminogen that forms the linkage between the plasmin chains."; RL Eur. J. Biochem. 58:539-547(1975). RN [12] RP PROTEIN SEQUENCE OF 581-810. RX PubMed=142009; DOI=10.1111/j.1432-1033.1977.tb11578.x; RA Wiman B.; RT "Primary structure of the B-chain of human plasmin."; RL Eur. J. Biochem. 76:129-137(1977). RN [13] RP ACTIVE SITE. RX PubMed=4694729; DOI=10.1016/s0021-9258(19)44237-3; RA Robbins K.C., Bernabe P., Arzadon L., Summaria L.; RT "The primary structure of human plasminogen. II. The histidine loop of RT human plasmin: light (B) chain active center histidine sequence."; RL J. Biol. Chem. 248:1631-1633(1973). RN [14] RP ACTIVE SITE. RX PubMed=4240117; DOI=10.1016/s0021-9258(18)83410-x; RA Groskopf W.R., Summaria L., Robbins K.C.; RT "Studies on the active center of human plasmin. Partial amino acid sequence RT of a peptide containing the active center serine residue."; RL J. Biol. Chem. 244:3590-3597(1969). RN [15] RP OMEGA-AMINOCARBOXYLIC ACID-BINDING SITES. RX PubMed=6919539; DOI=10.1016/s0021-9258(18)34391-6; RA Trexler M., Vali Z., Patthy L.; RT "Structure of the omega-aminocarboxylic acid-binding sites of human RT plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of RT ligand by kringle 4."; RL J. Biol. Chem. 257:7401-7406(1982). RN [16] RP FIBRIN AND OMEGA-AMINOCARBOXYLIC ACID BINDING SITES. RX PubMed=6094526; DOI=10.1016/s0021-9258(18)89800-3; RA Vali Z., Patthy L.; RT "The fibrin-binding site of human plasminogen. Arginines 32 and 34 are RT essential for fibrin affinity of the kringle 1 domain."; RL J. Biol. Chem. 259:13690-13694(1984). RN [17] RP PHOSPHORYLATION AT SER-597. RX PubMed=9201958; DOI=10.1021/bi970328d; RA Wang H., Prorok M., Bretthauer R.K., Castellino F.J.; RT "Serine-578 is a major phosphorylation locus in human plasma plasminogen."; RL Biochemistry 36:8100-8106(1997). RN [18] RP GLYCOSYLATION AT SER-268; ASN-308 AND THR-365, AND STRUCTURE OF RP CARBOHYDRATES. RX PubMed=3356193; DOI=10.1111/j.1432-1033.1988.tb13966.x; RA Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., RA van Halbeek H., Vliegenthart J.F.G.; RT "The N- and O-linked carbohydrate chains of human, bovine and porcine RT plasminogen. Species specificity in relation to sialylation and RT fucosylation patterns."; RL Eur. J. Biochem. 173:57-63(1988). RN [19] RP INTERACTION WITH HRG. RX PubMed=9102401; DOI=10.1074/jbc.272.9.5718; RA Borza D.B., Morgan W.T.; RT "Acceleration of plasminogen activation by tissue plasminogen activator on RT surface-bound histidine-proline-rich glycoprotein."; RL J. Biol. Chem. 272:5718-5726(1997). RN [20] RP GLYCOSYLATION AT SER-268. RX PubMed=9054441; DOI=10.1074/jbc.272.11.7408; RA Pirie-Shepherd S.R., Stevens R.D., Andon N.L., Enghild J.J., Pizzo S.V.; RT "Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human RT plasminogen 2."; RL J. Biol. Chem. 272:7408-7411(1997). RN [21] RP CHARACTERIZATION OF ANGIOSTATIN, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=7525077; DOI=10.1016/0092-8674(94)90200-3; RA O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M., RA Lane W.S., Cao Y., Sage E.H., Folkman J.; RT "Angiostatin: a novel angiogenesis inhibitor that mediates the suppression RT of metastases by a Lewis lung carcinoma."; RL Cell 79:315-328(1994). RN [22] RP CHARACTERIZATION OF ANGIOSTATIN. RX PubMed=9102221; RA Sim B.K., O'Reilly M.S., Liang H., Fortier A.H., He W., Madsen J.W., RA Lapcevich R., Nacy C.A.; RT "A recombinant human angiostatin protein inhibits experimental primary and RT metastatic cancer."; RL Cancer Res. 57:1329-1334(1997). RN [23] RP PROTEOLYTIC CLEAVAGE. RX PubMed=9548733; DOI=10.1021/bi9731798; RA Lijnen H.R., Ugwu F., Bini A., Collen D.; RT "Generation of an angiostatin-like fragment from plasminogen by RT stromelysin-1 (MMP-3)."; RL Biochemistry 37:4699-4702(1998). RN [24] RP INTERACTION WITH ATP5F1A, AND SUBCELLULAR LOCATION. RX PubMed=10077593; DOI=10.1073/pnas.96.6.2811; RA Moser T.L., Stack M.S., Asplin I., Enghild J.J., Hojrup P., Everitt L., RA Hubchak S., Schnaper H.W., Pizzo S.V.; RT "Angiostatin binds ATP synthase on the surface of human endothelial RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2811-2816(1999). RN [25] RP INTERACTION WITH CSPG4, AND DOMAIN. RX PubMed=10889192; DOI=10.1074/jbc.m002290200; RA Goretzki L., Lombardo C.R., Stallcup W.B.; RT "Binding of the NG2 proteoglycan to kringle domains modulates the RT functional properties of angiostatin and plasmin(ogen)."; RL J. Biol. Chem. 275:28625-28633(2000). RN [26] RP PROTEOLYTIC PROCESSING, ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION RP OF PLASMIN, AND MUTAGENESIS OF SER-741. RX PubMed=14699093; DOI=10.1074/jbc.m310964200; RA Rossignol P., Ho-Tin-Noe B., Vranckx R., Bouton M.C., Meilhac O., RA Lijnen H.R., Guillin M.C., Michel J.B., Angles-Cano E.; RT "Protease nexin-1 inhibits plasminogen activation-induced apoptosis of RT adherent cells."; RL J. Biol. Chem. 279:10346-10356(2004). RN [27] RP INTERACTION WITH ADA. RX PubMed=15016824; DOI=10.1074/jbc.m401023200; RA Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.; RT "Cell surface adenosine deaminase binds and stimulates plasminogen RT activation on 1-LN human prostate cancer cells."; RL J. Biol. Chem. 279:20993-20998(2004). RN [28] RP INTERACTION WITH AMOT. RX PubMed=16043488; DOI=10.1074/jbc.m503915200; RA Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., RA Holmgren L.; RT "Angiomotin regulates endothelial cell-cell junctions and cell motility."; RL J. Biol. Chem. 280:34859-34869(2005). RN [29] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [30] RP CATALYTIC ACTIVITY. RX PubMed=2143188; DOI=10.1016/s0021-9258(18)77401-2; RA Kirschbaum N.E., Budzynski A.Z.; RT "A unique proteolytic fragment of human fibrinogen containing the A alpha RT COOH-terminal domain of the native molecule."; RL J. Biol. Chem. 265:13669-13676(1990). RN [31] RP INTERACTION WITH HRG. RX PubMed=19712047; DOI=10.1042/bj20090794; RA Poon I.K., Olsson A.K., Hulett M.D., Parish C.R.; RT "Regulation of histidine-rich glycoprotein (HRG) function via plasmin- RT mediated proteolytic cleavage."; RL Biochem. J. 424:27-37(2009). RN [32] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH P.FALCIPARUM ENO RP (MICROBIAL INFECTION), AND MUTAGENESIS OF SER-741. RX PubMed=21949403; DOI=10.1073/pnas.1103657108; RA Ghosh A.K., Coppens I., Gaardsvoll H., Ploug M., Jacobs-Lorena M.; RT "Plasmodium ookinetes coopt mammalian plasminogen to invade the mosquito RT midgut."; RL Proc. Natl. Acad. Sci. U.S.A. 108:17153-17158(2011). RN [33] RP POSSIBLE FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH B.BURGDORFERI RP OSPC (MICROBIAL INFECTION). RX PubMed=22433849; DOI=10.1074/jbc.m111.290775; RA Oender O., Humphrey P.T., McOmber B., Korobova F., Francella N., RA Greenbaum D.C., Brisson D.; RT "OspC is potent plasminogen receptor on surface of Borrelia burgdorferi."; RL J. Biol. Chem. 287:16860-16868(2012). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [35] RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN FNBB (MICROBIAL INFECTION). RX PubMed=27387503; DOI=10.1074/jbc.m116.731125; RA Pietrocola G., Nobile G., Gianotti V., Zapotoczna M., Foster T.J., RA Geoghegan J.A., Speziale P.; RT "Molecular Interactions of human plasminogen with fibronectin-binding RT Protein B (FnBPB), a fibrinogen/fibronectin-binding protein from RT Staphylococcus aureus."; RL J. Biol. Chem. 291:18148-18162(2016). RN [36] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461. RX PubMed=1657148; DOI=10.1021/bi00107a029; RA Mulichak A.M., Tulinsky A., Ravichandran K.G.; RT "Crystal and molecular structure of human plasminogen kringle 4 refined at RT 1.9-A resolution."; RL Biochemistry 30:10576-10588(1991). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461. RX PubMed=1657149; DOI=10.1021/bi00107a030; RA Wu T.-P., Padmanabhan K., Tulinsky A., Mulichak A.M.; RT "The refined structure of the epsilon-aminocaproic acid complex of human RT plasminogen kringle 4."; RL Biochemistry 30:10589-10594(1991). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 101-181. RX PubMed=8054447; DOI=10.1097/00001721-199404000-00001; RA Wu T.-P., Padmanabhan K.P., Tulinsky A.; RT "The structure of recombinant plasminogen kringle 1 and the fibrin binding RT site."; RL Blood Coagul. Fibrinolysis 5:157-166(1994). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181. RX PubMed=8611560; DOI=10.1021/bi9521351; RA Mathews I.I., Vanderhoff-Hanaver P., Castellino F.J., Tulinsky A.; RT "Crystal structures of the recombinant kringle 1 domain of human RT plasminogen in complexes with the ligands epsilon-aminocaproic acid and RT trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid."; RL Biochemistry 35:2567-2576(1996). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454. RX PubMed=15299951; DOI=10.1107/s0907444996012267; RA Stec B., Yamano A., Whitlow M., Teeter M.M.; RT "Structure of human plasminogen kringle 4 at 1.68 Angstrom and 277 K. A RT possible structural role of disordered residues."; RL Acta Crystallogr. D 53:169-178(1997). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 561-810, AND DISULFIDE BONDS. RX PubMed=9783753; DOI=10.1038/2359; RA Parry M.A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K.P., RA Schlott B., Guehrs K.H., Bode W.; RT "The ternary microplasmin-staphylokinase-microplasmin complex is a RT proteinase-cofactor-substrate complex in action."; RL Nat. Struct. Biol. 5:917-923(1998). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563. RX PubMed=9521645; DOI=10.1021/bi972284e; RA Chang Y., Mochalkin I., McCance S.G., Cheng B., Tulinsky A., RA Castellino F.J.; RT "Structure and ligand binding determinants of the recombinant kringle 5 RT domain of human plasminogen."; RL Biochemistry 37:3258-3271(1998). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 564-810, AND DISULFIDE BONDS. RX PubMed=10656799; DOI=10.1006/jmbi.1999.3397; RA Wang X., Terzyan S., Tang J., Loy J.A., Lin X., Zhang X.C.; RT "Human plasminogen catalytic domain undergoes an unusual conformational RT change upon activation."; RL J. Mol. Biol. 295:903-914(2000). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 183-262. RX PubMed=11350170; DOI=10.1006/jmbi.2001.4646; RA Rios-Steiner J.L., Schenone M., Mochalkin I., Tulinsky A., Castellino F.J.; RT "Structure and binding determinants of the recombinant kringle-2 domain of RT human plasminogen to an internal peptide from a group A Streptococcal RT surface protein."; RL J. Mol. Biol. 308:705-719(2001). RN [45] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 100-352, AND DISULFIDE BONDS. RX PubMed=12054798; DOI=10.1016/s0022-2836(02)00211-5; RA Abad M.C., Arni R.K., Grella D.K., Castellino F.J., Tulinsky A., RA Geiger J.H.; RT "The X-ray crystallographic structure of the angiogenesis inhibitor RT angiostatin."; RL J. Mol. Biol. 318:1009-1017(2002). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 562-810. RX PubMed=12456874; DOI=10.1093/protein/15.9.753; RA Wakeham N., Terzyan S., Zhai P., Loy J.A., Tang J., Zhang X.C.; RT "Effects of deletion of streptokinase residues 48-59 on plasminogen RT activation."; RL Protein Eng. 15:753-761(2002). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 564-810. RX PubMed=15211511; DOI=10.1002/prot.20070; RA Terzyan S., Wakeham N., Zhai P., Rodgers K., Zhang X.C.; RT "Characterization of Lys-698-to-Met substitution in human plasminogen RT catalytic domain."; RL Proteins 56:277-284(2004). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 564-810 IN COMPLEX WITH THE SNAKE RP VENOM PROTEASE INHIBITOR TEXTILININ-1, AND DISULFIDE BOND. RX PubMed=23335990; DOI=10.1371/journal.pone.0054104; RA Millers E.K., Johnson L.A., Birrell G.W., Masci P.P., Lavin M.F., RA de Jersey J., Guddat L.W.; RT "The structure of human microplasmin in complex with textilinin-1, an RT aprotinin-like inhibitor from the Australian brown snake."; RL PLoS ONE 8:E54104-E54104(2013). RN [49] RP STRUCTURE BY NMR OF 374-461. RX PubMed=2157850; DOI=10.1016/0022-2836(90)90330-o; RA Atkinson R.A., Williams R.J.P.; RT "Solution structure of the kringle 4 domain from human plasminogen by 1H RT nuclear magnetic resonance spectroscopy and distance geometry."; RL J. Mol. Biol. 212:541-552(1990). RN [50] RP STRUCTURE BY NMR OF 96-184. RX PubMed=8181475; DOI=10.1111/j.1432-1033.1994.tb18808.x; RA Rejante M.R., Llinas M.; RT "1H-NMR assignments and secondary structure of human plasminogen kringle RT 1."; RL Eur. J. Biochem. 221:927-937(1994). RN [51] RP STRUCTURE BY NMR OF 96-184. RX PubMed=8181476; DOI=10.1111/j.1432-1033.1994.tb18809.x; RA Rejante M.R., Llinas M.; RT "Solution structure of the epsilon-aminohexanoic acid complex of human RT plasminogen kringle 1."; RL Eur. J. Biochem. 221:939-949(1994). RN [52] RP STRUCTURE BY NMR OF 183-354. RX PubMed=8652577; DOI=10.1021/bi9520949; RA Soehndel S., Hu C.-K., Marti D., Affolter M., Schaller J., Llinas M., RA Rickli E.E.; RT "Recombinant gene expression and 1H NMR characteristics of the kringle (2 + RT 3) supermodule: spectroscopic/functional individuality of plasminogen RT kringle domains."; RL Biochemistry 35:2357-2364(1996). RN [53] RP STRUCTURE BY NMR OF 183-263. RX PubMed=9305949; DOI=10.1021/bi971316v; RA Marti D.N., Hu C.K., An S.S., von Haller P., Schaller J., Llinas M.; RT "Ligand preferences of kringle 2 and homologous domains of human RT plasminogen: canvassing weak, intermediate, and high-affinity binding sites RT by 1H-NMR."; RL Biochemistry 36:11591-11604(1997). RN [54] {ECO:0007744|PDB:4DCB} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 576-585 IN COMPLEX WITH Y.PESTIS RP PLASMINOGEN ACTIVATOR, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=22645135; DOI=10.1074/jbc.M112.376418; RA Eren E., van den Berg B.; RT "Structural basis for activation of an integral membrane protease by RT lipopolysaccharide."; RL J. Biol. Chem. 287:23971-23976(2012). RN [55] RP VARIANTS PLGD PHE-374 AND THR-620. RX PubMed=1986355; DOI=10.1073/pnas.88.1.115; RA Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., RA Maruyama I., Petersen T.E., Davie E.W.; RT "Two types of abnormal genes for plasminogen in families with a RT predisposition for thrombosis."; RL Proc. Natl. Acad. Sci. U.S.A. 88:115-119(1991). RN [56] RP ERRATUM OF PUBMED:1986355. RA Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., RA Maruyama I., Petersen T.E., Davie E.W.; RL Proc. Natl. Acad. Sci. U.S.A. 88:2067-2067(1991). RN [57] RP VARIANT PLGD PRO-591. RX PubMed=8392398; RA Azuma H., Uno Y., Shigekiyo T., Saito S.; RT "Congenital plasminogen deficiency caused by a Ser-572 to Pro mutation."; RL Blood 82:475-480(1993). RN [58] RP VARIANT PLGD THR-620. RX PubMed=6216475; DOI=10.1073/pnas.79.20.6132; RA Miyata T., Iwanaga S., Sakata Y., Aoki N.; RT "Plasminogen Tochigi: inactive plasmin resulting from replacement of RT alanine-600 by threonine in the active site."; RL Proc. Natl. Acad. Sci. U.S.A. 79:6132-6136(1982). RN [59] RP VARIANT PLGD THR-620. RX PubMed=6238949; DOI=10.1093/oxfordjournals.jbchem.a134836; RA Miyata T., Iwanaga S., Sakata Y., Aoki N., Takamatsu J., Kamiya T.; RT "Plasminogens Tochigi II and Nagoya: two additional molecular defects with RT Ala-600-->Thr replacement found in plasmin light chain variants."; RL J. Biochem. 96:277-287(1984). RN [60] RP VARIANT PLGD THR-620. RX PubMed=1427790; DOI=10.1007/bf00210737; RA Kikuchi S., Yamanouchi Y., Li L., Kobayashi K., Ijima H., Miyazaki R., RA Tsuchiya S., Hamaguchi H.; RT "Plasminogen with type-I mutation is polymorphic in the Japanese RT population."; RL Hum. Genet. 90:7-11(1992). RN [61] RP VARIANT PLGD HIS-235. RX PubMed=9242524; RA Schuster V., Mingers A.-M., Seidenspinner S., Nuessgens Z., Pukrop T., RA Kreth H.W.; RT "Homozygous mutations in the plasminogen gene of two unrelated girls with RT ligneous conjunctivitis."; RL Blood 90:958-966(1997). RN [62] RP VARIANT PLGD ARG-751. RX PubMed=9858247; DOI=10.1046/j.1365-2141.1998.01074.x; RA Higuchi Y., Furihata K., Ueno I., Ishikawa S., Okumura N., Tozuka M., RA Sakurai N.; RT "Plasminogen Kanagawa-I, a novel missense mutation, is caused by the amino RT acid substitution G732R."; RL Br. J. Haematol. 103:867-870(1998). RN [63] RP VARIANTS PLGD GLU-38; PRO-147 AND HIS-532. RX PubMed=10233898; RA Schuster V., Seidenspinner S., Zeitler P., Escher C., Pleyer U., RA Bernauer W., Stiehm E.R., Isenberg S., Seregard S., Olsson T., RA Mingers A.-M., Schambeck C., Kreth H.W.; RT "Compound-heterozygous mutations in the plasminogen gene predispose to the RT development of ligneous conjunctivitis."; RL Blood 93:3457-3466(1999). RN [64] RP INTERACTION WITH C.ALBICANS GPD2 (MICROBIAL INFECTION). RX PubMed=23204165; DOI=10.1093/infdis/jis718; RA Luo S., Hoffmann R., Skerka C., Zipfel P.F.; RT "Glycerol-3-phosphate dehydrogenase 2 is a novel factor H-, factor H-like RT protein 1-, and plasminogen-binding surface protein of Candida albicans."; RL J. Infect. Dis. 207:594-603(2013). RN [65] RP VARIANT HAE4 GLU-330, AND INVOLVEMENT IN HAE4. RX PubMed=28795768; DOI=10.1111/all.13270; RA Bork K., Wulff K., Steinmueller-Magin L., Braenne I., Staubach-Renz P., RA Witzke G., Hardt J.; RT "Hereditary angioedema with a mutation in the plasminogen gene."; RL Allergy 73:442-450(2018). RN [66] RP VARIANT HAE4 GLU-330, AND INVOLVEMENT IN HAE4. RX PubMed=29952006; DOI=10.1111/all.13543; RA Belbezier A., Hardy G., Marlu R., Defendi F., Dumestre Perard C., RA Boccon-Gibod I., Launay D., Bouillet L.; RT "Plasminogen gene mutation with normal C1 inhibitor hereditary angioedema: RT Three additional French families."; RL Allergy 73:2237-2239(2018). RN [67] RP VARIANT HAE4 GLU-330, AND INVOLVEMENT IN HAE4. RX PubMed=29987869; DOI=10.1111/all.13550; RA Yakushiji H., Hashimura C., Fukuoka K., Kaji A., Miyahara H., Kaname S., RA Horiuchi T.; RT "A missense mutation of the plasminogen gene in hereditary angioedema with RT normal C1 inhibitor in Japan."; RL Allergy 73:2244-2247(2018). RN [68] RP VARIANT HAE4 GLU-330, AND INVOLVEMENT IN HAE4. RX PubMed=29548426; DOI=10.1016/j.bbrc.2017.12.060; RA Dewald G.; RT "A missense mutation in the plasminogen gene, within the plasminogen RT kringle 3 domain, in hereditary angioedema with normal C1 inhibitor."; RL Biochem. Biophys. Res. Commun. 498:193-198(2018). RN [69] RP VARIANTS HAE4 GLU-330 AND GLU-728, AND VARIANT LYS-89. RX PubMed=33114181; DOI=10.3390/jcm9113402; RA Loules G., Parsopoulou F., Zamanakou M., Csuka D., Bova M., RA Gonzalez-Quevedo T., Psarros F., Porebski G., Speletas M., Firinu D., RA Del Giacco S., Suffritti C., Makris M., Vatsiou S., Zanichelli A., RA Farkas H., Germenis A.E.; RT "Deciphering the genetics of primary angioedema with normal levels of C1 RT inhibitor."; RL J. Clin. Med. 9:0-0(2020). RN [70] RP VARIANT HAE4 GLU-330. RX PubMed=33799813; DOI=10.3390/genes12030402; RA Farkas H., Doczy A., Szabo E., Varga L., Csuka D.; RT "Screening for plasminogen mutations in hereditary angioedema patients."; RL Genes (Basel) 12:0-0(2021). CC -!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a CC proteolytic factor in a variety of other processes including embryonic CC development, tissue remodeling, tumor invasion, and inflammation. In CC ovulation, weakens the walls of the Graafian follicle. It activates the CC urokinase-type plasminogen activator, collagenases and several CC complement zymogens, such as C1 and C5. Cleavage of fibronectin and CC laminin leads to cell detachment and apoptosis. Also cleaves fibrin, CC thrombospondin and von Willebrand factor. Its role in tissue remodeling CC and tumor invasion may be modulated by CSPG4. Binds to cells. CC {ECO:0000269|PubMed:14699093}. CC -!- FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks CC neovascularization and growth of experimental primary and metastatic CC tumors in vivo. {ECO:0000269|PubMed:14699093}. CC -!- FUNCTION: (Microbial infection) ENO/enoloase from parasite P.falciparum CC (strain NF54) interacts with PLG present in the mosquito blood meal to CC promote the invasion of the mosquito midgut by the parasite ookinete CC (PubMed:21949403). The catalytic active form, plasmin, is essential for CC the invasion of the mosquito midgut (PubMed:21949403). CC {ECO:0000269|PubMed:21949403}. CC -!- FUNCTION: (Microbial infection) Binds to OspC on the surface of CC B.burgdorferi cells, possibly conferring an extracellular protease CC activity on the bacteria that allows it to traverse host tissue. CC {ECO:0000269|PubMed:22433849}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher CC selectivity than trypsin. Converts fibrin into soluble products.; CC EC=3.4.21.7; Evidence={ECO:0000269|PubMed:2143188}; CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators, CC both plasminogen and its activator being bound to fibrin. Activated CC with catalytic amounts of streptokinase. Plasmin activity inhibited by CC SERPINE2. {ECO:0000269|PubMed:14699093}. CC -!- SUBUNIT: Interacts (both mature PLG and the angiostatin peptide) with CC CSPG4 and AMOT (PubMed:10889192, PubMed:16043488). Interacts (via the CC Kringle domains) with HRG; the interaction tethers PLG to the cell CC surface and enhances its activation (PubMed:9102401, PubMed:19712047). CC Interacts (via Kringle 4 domain) with ADA; the interaction stimulates CC PLG activation when in complex with DPP4 (PubMed:15016824). CC Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of CC the angiogenic effects of angiostatin (PubMed:10077593). CC {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:10889192, CC ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:16043488, CC ECO:0000269|PubMed:19712047, ECO:0000269|PubMed:9102401}. CC -!- SUBUNIT: (Microbial infection) Interacts with C.albicans GPD2; the CC interaction is direct and provides active plasmin on the surface of CC fungal cells. {ECO:0000269|PubMed:23204165}. CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus CC protein FnbB; this interaction provides active plasmin on the surface CC of bacterial cells. {ECO:0000269|PubMed:27387503}. CC -!- SUBUNIT: (Microbial infection) Interacts with P.falciparum (strain CC NF54) enolase ENO (via DKSLVK motif); the interaction occurs at the CC ookinete cell surface and is required for ookinete invasion of the CC mosquito midgut. {ECO:0000269|PubMed:21949403}. CC -!- SUBUNIT: (Microbial infection) Interacts with B.burgdorferi OspC. CC {ECO:0000269|PubMed:22433849}. CC -!- INTERACTION: CC P00747; P02749: APOH; NbExp=2; IntAct=EBI-999394, EBI-2114682; CC P00747; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-999394, EBI-6425864; CC P00747; PRO_0000018520 [P28300]: LOX; NbExp=2; IntAct=EBI-999394, EBI-20724846; CC P00747; Q8N4S9: MARVELD2; NbExp=2; IntAct=EBI-999394, EBI-6875061; CC P00747; P75390: pdhA; Xeno; NbExp=5; IntAct=EBI-999394, EBI-2259629; CC P00747; P75391: pdhB; Xeno; NbExp=11; IntAct=EBI-999394, EBI-2259621; CC P00747; P75392: pdhC; Xeno; NbExp=5; IntAct=EBI-999394, EBI-2259593; CC P00747; P75393: pdhD; Xeno; NbExp=3; IntAct=EBI-999394, EBI-2259617; CC P00747; Q99SU7: sak; Xeno; NbExp=7; IntAct=EBI-999394, EBI-7689378; CC P00747; P00779: skc; Xeno; NbExp=2; IntAct=EBI-999394, EBI-1035089; CC P00747; Q6V4L1; Xeno; NbExp=2; IntAct=EBI-999394, EBI-984250; CC P00747; Q6V4L4; Xeno; NbExp=2; IntAct=EBI-999394, EBI-984286; CC P00747; Q6V4L5; Xeno; NbExp=2; IntAct=EBI-999394, EBI-984118; CC P00747; Q6V4L9; Xeno; NbExp=2; IntAct=EBI-999394, EBI-984197; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077593, CC ECO:0000269|PubMed:14699093}. Note=Locates to the cell surface where it CC is proteolytically cleaved to produce the active plasmin. Interaction CC with HRG tethers it to the cell surface. CC -!- TISSUE SPECIFICITY: Present in plasma and many other extracellular CC fluids. It is synthesized in the liver. CC -!- DOMAIN: Kringle domains mediate interaction with CSPG4. CC {ECO:0000269|PubMed:10889192}. CC -!- PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O- CC linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 CC sialic acid residues (microheterogeneity). CC {ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193, CC ECO:0000269|PubMed:9054441}. CC -!- PTM: In the presence of the inhibitor, the activation involves only CC cleavage after Arg-580, yielding two chains held together by two CC disulfide bonds. In the absence of the inhibitor, the activation CC involves additionally the removal of the activation peptide. CC {ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:9548733}. CC -!- PTM: (Microbial infection) The Y.pestis Pla protein cleaves between CC Arg-580 and Val-581, generating plasmin which facilitates bacterial CC migration and infection (PubMed:22645135). CC {ECO:0000269|PubMed:22645135}. CC -!- DISEASE: Plasminogen deficiency (PLGD) [MIM:217090]: A disorder CC characterized by decreased serum plasminogen activity. Two forms of the CC disorder are distinguished: type 1 deficiency is additionally CC characterized by decreased plasminogen antigen levels and clinical CC symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, CC is characterized by normal, or slightly reduced antigen levels, and CC absence of clinical manifestations. Plasminogen deficiency type 1 CC results in markedly impaired extracellular fibrinolysis and chronic CC mucosal pseudomembranous lesions due to subepithelial fibrin deposition CC and inflammation. The most common clinical manifestation of type 1 CC deficiency is ligneous conjunctivitis in which pseudomembranes CC formation on the palpebral surfaces of the eye progresses to white, CC yellow-white, or red thick masses with a wood-like consistency that CC replace the normal mucosa. {ECO:0000269|PubMed:10233898, CC ECO:0000269|PubMed:1427790, ECO:0000269|PubMed:1986355, CC ECO:0000269|PubMed:6216475, ECO:0000269|PubMed:6238949, CC ECO:0000269|PubMed:8392398, ECO:0000269|PubMed:9242524, CC ECO:0000269|PubMed:9858247}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Angioedema, hereditary, 4 (HAE4) [MIM:619360]: A form of CC angioedema, a disorder characterized by episodic local swelling CC involving subcutaneous or submucous tissue of the upper respiratory and CC gastrointestinal tracts, face, extremities, and genitalia. HAE4 is an CC autosomal dominant form with incomplete penetrance, variable CC expressivity, and female predominance. {ECO:0000269|PubMed:28795768, CC ECO:0000269|PubMed:29548426, ECO:0000269|PubMed:29952006, CC ECO:0000269|PubMed:29987869, ECO:0000269|PubMed:33114181, CC ECO:0000269|PubMed:33799813}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin CC immediately after dissociation from the clot. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Plasmin entry; CC URL="https://en.wikipedia.org/wiki/Plasmin"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/plg/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34276; AAA60113.1; -; Genomic_DNA. DR EMBL; M33272; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33274; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33275; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33278; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33279; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33280; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33282; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33283; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33284; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33285; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33286; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33287; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33288; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33289; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M33290; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M34272; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M34273; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; M34275; AAA60113.1; JOINED; Genomic_DNA. DR EMBL; X05199; CAA28831.1; -; mRNA. DR EMBL; M74220; AAA36451.1; -; mRNA. DR EMBL; AY192161; AAN85555.1; -; Genomic_DNA. DR EMBL; AL109933; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC060513; AAH60513.1; -; mRNA. DR EMBL; K02922; AAA60124.1; -; mRNA. DR CCDS; CCDS5279.1; -. DR PIR; A35229; PLHU. DR RefSeq; NP_000292.1; NM_000301.3. DR PDB; 1B2I; NMR; -; A=181-263. DR PDB; 1BML; X-ray; 2.90 A; A/B=561-810. DR PDB; 1BUI; X-ray; 2.65 A; A/B=561-810. DR PDB; 1CEA; X-ray; 2.06 A; A/B=100-187. DR PDB; 1CEB; X-ray; 2.07 A; A/B=100-187. DR PDB; 1DDJ; X-ray; 2.00 A; A/B/C/D=564-810. DR PDB; 1HPJ; NMR; -; A=103-181. DR PDB; 1HPK; NMR; -; A=103-181. DR PDB; 1I5K; X-ray; 2.70 A; A/B=184-262. DR PDB; 1KI0; X-ray; 1.75 A; A=100-352. DR PDB; 1KRN; X-ray; 1.67 A; A=374-461. DR PDB; 1L4D; X-ray; 2.30 A; A=562-810. DR PDB; 1L4Z; X-ray; 2.80 A; A=563-810. DR PDB; 1PK4; X-ray; 1.90 A; A=376-454. DR PDB; 1PKR; X-ray; 2.48 A; A=101-181. DR PDB; 1PMK; X-ray; 2.25 A; A/B=374-461. DR PDB; 1QRZ; X-ray; 2.00 A; A/B/C/D=565-810. DR PDB; 1RJX; X-ray; 2.30 A; B=564-810. DR PDB; 2DOH; X-ray; 2.30 A; X=100-333. DR PDB; 2DOI; X-ray; 3.10 A; A/X=100-333. DR PDB; 2KNF; NMR; -; A=480-562. DR PDB; 2L0S; NMR; -; A=272-354. DR PDB; 2PK4; X-ray; 2.25 A; A=375-454. DR PDB; 3UIR; X-ray; 2.78 A; A/B=564-810. DR PDB; 4A5T; X-ray; 3.49 A; S=20-810. DR PDB; 4CIK; X-ray; 1.78 A; A=101-181. DR PDB; 4DCB; X-ray; 2.03 A; F=576-585. DR PDB; 4DUR; X-ray; 2.45 A; A/B=20-810. DR PDB; 4DUU; X-ray; 5.20 A; A=20-810. DR PDB; 5HPG; X-ray; 1.66 A; A/B=480-563. DR PDB; 5UGD; X-ray; 1.38 A; A=562-810. DR PDB; 5UGG; X-ray; 1.20 A; A=562-810. DR PDB; 6D3X; X-ray; 1.80 A; A/B=565-810. DR PDB; 6D3Y; X-ray; 1.32 A; A=564-810. DR PDB; 6D3Z; X-ray; 2.00 A; A=565-810. DR PDB; 6D40; X-ray; 1.43 A; A=563-810. DR PDB; 6OG4; X-ray; 1.70 A; A/B=183-264. DR PDB; 6OQJ; NMR; -; A=179-262. DR PDB; 6OQK; NMR; -; A=179-262. DR PDB; 6Q1U; X-ray; 2.35 A; A/B=562-810. DR PDB; 6UZ4; NMR; -; A=185-262. DR PDB; 6UZ5; NMR; -; A=185-262. DR PDB; 7E50; X-ray; 1.95 A; B=564-810. DR PDB; 7THS; X-ray; 1.80 A; A/B=561-810. DR PDB; 7UAH; X-ray; 1.57 A; A/B=561-810. DR PDB; 8F7U; X-ray; 1.47 A; A/B=561-810. DR PDB; 8F7V; X-ray; 1.65 A; A/B=561-810. DR PDBsum; 1B2I; -. DR PDBsum; 1BML; -. DR PDBsum; 1BUI; -. DR PDBsum; 1CEA; -. DR PDBsum; 1CEB; -. DR PDBsum; 1DDJ; -. DR PDBsum; 1HPJ; -. DR PDBsum; 1HPK; -. DR PDBsum; 1I5K; -. DR PDBsum; 1KI0; -. DR PDBsum; 1KRN; -. DR PDBsum; 1L4D; -. DR PDBsum; 1L4Z; -. DR PDBsum; 1PK4; -. DR PDBsum; 1PKR; -. DR PDBsum; 1PMK; -. DR PDBsum; 1QRZ; -. DR PDBsum; 1RJX; -. DR PDBsum; 2DOH; -. DR PDBsum; 2DOI; -. DR PDBsum; 2KNF; -. DR PDBsum; 2L0S; -. DR PDBsum; 2PK4; -. DR PDBsum; 3UIR; -. DR PDBsum; 4A5T; -. DR PDBsum; 4CIK; -. DR PDBsum; 4DCB; -. DR PDBsum; 4DUR; -. DR PDBsum; 4DUU; -. DR PDBsum; 5HPG; -. DR PDBsum; 5UGD; -. DR PDBsum; 5UGG; -. DR PDBsum; 6D3X; -. DR PDBsum; 6D3Y; -. DR PDBsum; 6D3Z; -. DR PDBsum; 6D40; -. DR PDBsum; 6OG4; -. DR PDBsum; 6OQJ; -. DR PDBsum; 6OQK; -. DR PDBsum; 6Q1U; -. DR PDBsum; 6UZ4; -. DR PDBsum; 6UZ5; -. DR PDBsum; 7E50; -. DR PDBsum; 7THS; -. DR PDBsum; 7UAH; -. DR PDBsum; 8F7U; -. DR PDBsum; 8F7V; -. DR AlphaFoldDB; P00747; -. DR SMR; P00747; -. DR BioGRID; 111356; 76. DR CORUM; P00747; -. DR IntAct; P00747; 55. DR MINT; P00747; -. DR STRING; 9606.ENSP00000308938; -. DR BindingDB; P00747; -. DR ChEMBL; CHEMBL1801; -. DR DrugBank; DB00009; Alteplase. DR DrugBank; DB00513; Aminocaproic acid. DR DrugBank; DB00029; Anistreplase. DR DrugBank; DB06692; Aprotinin. DR DrugBank; DB03709; Bicine. DR DrugBank; DB09130; Copper. DR DrugBank; DB04925; Desmoteplase. DR DrugBank; DB12831; Gabexate. DR DrugBank; DB00015; Reteplase. DR DrugBank; DB00086; Streptokinase. DR DrugBank; DB00031; Tenecteplase. DR DrugBank; DB00302; Tranexamic acid. DR DrugBank; DB00013; Urokinase. DR DrugCentral; P00747; -. DR GuidetoPHARMACOLOGY; 2394; -. DR MEROPS; S01.233; -. DR GlyConnect; 502; 33 N-Linked glycans (3 sites), 2 O-Linked glycans (2 sites). DR GlyCosmos; P00747; 15 sites, 64 glycans. DR GlyGen; P00747; 16 sites, 54 N-linked glycans (4 sites), 13 O-linked glycans (13 sites). DR iPTMnet; P00747; -. DR PhosphoSitePlus; P00747; -. DR BioMuta; PLG; -. DR DMDM; 130316; -. DR CPTAC; non-CPTAC-1151; -. DR jPOST; P00747; -. DR MassIVE; P00747; -. DR MaxQB; P00747; -. DR PaxDb; 9606-ENSP00000308938; -. DR PeptideAtlas; P00747; -. DR ProteomicsDB; 51277; -. DR Pumba; P00747; -. DR Antibodypedia; 3285; 1373 antibodies from 41 providers. DR DNASU; 5340; -. DR Ensembl; ENST00000308192.14; ENSP00000308938.9; ENSG00000122194.20. DR GeneID; 5340; -. DR KEGG; hsa:5340; -. DR MANE-Select; ENST00000308192.14; ENSP00000308938.9; NM_000301.5; NP_000292.1. DR UCSC; uc003qtm.5; human. DR AGR; HGNC:9071; -. DR CTD; 5340; -. DR DisGeNET; 5340; -. DR GeneCards; PLG; -. DR HGNC; HGNC:9071; PLG. DR HPA; ENSG00000122194; Tissue enriched (liver). DR MalaCards; PLG; -. DR MIM; 173350; gene. DR MIM; 217090; phenotype. DR MIM; 619360; phenotype. DR neXtProt; NX_P00747; -. DR OpenTargets; ENSG00000122194; -. DR Orphanet; 722; Hypoplasminogenemia. DR Orphanet; 537072; PLG-related hereditary angioedema with normal C1Inh. DR PharmGKB; PA33405; -. DR VEuPathDB; HostDB:ENSG00000122194; -. DR eggNOG; ENOG502QVNP; Eukaryota. DR GeneTree; ENSGT00940000155208; -. DR HOGENOM; CLU_017565_0_0_1; -. DR InParanoid; P00747; -. DR OMA; NSQTPHA; -. DR OrthoDB; 211181at2759; -. DR PhylomeDB; P00747; -. DR TreeFam; TF329901; -. DR BioCyc; MetaCyc:HS04553-MONOMER; -. DR BRENDA; 3.4.21.7; 2681. DR PathwayCommons; P00747; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot. DR SABIO-RK; P00747; -. DR SignaLink; P00747; -. DR SIGNOR; P00747; -. DR BioGRID-ORCS; 5340; 40 hits in 1154 CRISPR screens. DR ChiTaRS; PLG; human. DR EvolutionaryTrace; P00747; -. DR GeneWiki; Plasmin; -. DR GeneWiki; Plasminogen_activator; -. DR GenomeRNAi; 5340; -. DR Pharos; P00747; Tclin. DR PRO; PR:P00747; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P00747; Protein. DR Bgee; ENSG00000122194; Expressed in right lobe of liver and 103 other cell types or tissues. DR ExpressionAtlas; P00747; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:CAFA. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL. DR GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:CAFA. DR GO; GO:0019900; F:kinase binding; IPI:CAFA. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:1990405; F:protein antigen binding; IPI:CAFA. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:CAFA. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:CAFA. DR GO; GO:0008236; F:serine-type peptidase activity; TAS:AgBase. DR GO; GO:0005102; F:signaling receptor binding; IPI:AgBase. DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IDA:CAFA. DR GO; GO:0007596; P:blood coagulation; IMP:HGNC-UCL. DR GO; GO:0022617; P:extracellular matrix disassembly; IDA:BHF-UCL. DR GO; GO:0042730; P:fibrinolysis; IDA:CAFA. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl. DR GO; GO:0071674; P:mononuclear cell migration; IEA:Ensembl. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl. DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; TAS:BHF-UCL. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:BHF-UCL. DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:CAFA. DR GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase. DR GO; GO:0006508; P:proteolysis; IDA:CAFA. DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl. DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW. DR GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; IEA:Ensembl. DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl. DR CDD; cd00108; KR; 5. DR CDD; cd01099; PAN_AP_HGF; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1. DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR003609; Pan_app. DR InterPro; IPR023317; Pept_S1A_plasmin. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24261:SF13; PLASMINOGEN; 1. DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1. DR Pfam; PF00051; Kringle; 5. DR Pfam; PF00024; PAN_1; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001150; Plasmin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00018; KRINGLE. DR SMART; SM00130; KR; 5. DR SMART; SM00473; PAN_AP; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1. DR SUPFAM; SSF57440; Kringle-like; 5. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00021; KRINGLE_1; 5. DR PROSITE; PS50070; KRINGLE_2; 5. DR PROSITE; PS50948; PAN; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR SWISS-2DPAGE; P00747; -. DR Genevisible; P00747; HS. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation; Cleavage on pair of basic residues; KW Direct protein sequencing; Disease variant; Disulfide bond; Fibrinolysis; KW Glycoprotein; Hemostasis; Hydrolase; Kringle; Phosphoprotein; Protease; KW Reference proteome; Repeat; Secreted; Serine protease; Signal; KW Thrombophilia; Tissue remodeling; Zymogen. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:122932, ECO:0000269|Ref.7" FT CHAIN 20..810 FT /note="Plasminogen" FT /id="PRO_0000028053" FT CHAIN 20..580 FT /note="Plasmin heavy chain A" FT /id="PRO_0000028054" FT PEPTIDE 20..97 FT /note="Activation peptide" FT /id="PRO_0000028055" FT CHAIN 79..466 FT /note="Angiostatin" FT /id="PRO_0000028057" FT CHAIN 98..580 FT /note="Plasmin heavy chain A, short form" FT /id="PRO_0000028056" FT CHAIN 581..810 FT /note="Plasmin light chain B" FT /id="PRO_0000028058" FT DOMAIN 20..98 FT /note="PAN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315" FT DOMAIN 103..181 FT /note="Kringle 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 184..262 FT /note="Kringle 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 275..352 FT /note="Kringle 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 377..454 FT /note="Kringle 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 481..560 FT /note="Kringle 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 581..808 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 126..145 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 622 FT /note="Charge relay system" FT ACT_SITE 665 FT /note="Charge relay system" FT ACT_SITE 760 FT /note="Charge relay system" FT BINDING 136 FT /ligand="L-lysine" FT /ligand_id="ChEBI:CHEBI:32551" FT BINDING 158 FT /ligand="L-lysine" FT /ligand_id="ChEBI:CHEBI:32551" FT BINDING 172 FT /ligand="L-lysine" FT /ligand_id="ChEBI:CHEBI:32551" FT BINDING 432 FT /ligand="L-lysine" FT /ligand_id="ChEBI:CHEBI:32551" FT BINDING 445 FT /ligand="L-lysine" FT /ligand_id="ChEBI:CHEBI:32551" FT SITE 78..79 FT /note="Cleavage; by stromelysin-1" FT SITE 134 FT /note="Interacts with fibrin" FT SITE 136 FT /note="Interacts with fibrin" FT SITE 466..467 FT /note="Cleavage; by stromelysin-19" FT SITE 580..581 FT /note="Cleavage; by plasminogen activator" FT MOD_RES 597 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:9201958" FT MOD_RES 688 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 268 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:3356193, FT ECO:0000269|PubMed:9054441" FT /id="CAR_000016" FT CARBOHYD 308 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:3356193" FT /id="CAR_000017" FT CARBOHYD 365 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:3356193" FT /id="CAR_000018" FT DISULFID 49..73 FT DISULFID 53..61 FT DISULFID 103..181 FT DISULFID 124..164 FT DISULFID 152..176 FT DISULFID 185..262 FT DISULFID 188..316 FT DISULFID 206..245 FT DISULFID 234..257 FT DISULFID 275..352 FT DISULFID 296..335 FT DISULFID 324..347 FT DISULFID 377..454 FT DISULFID 398..437 FT DISULFID 426..449 FT DISULFID 481..560 FT DISULFID 502..543 FT DISULFID 531..555 FT DISULFID 567..685 FT /note="Interchain (between A and B chains)" FT DISULFID 577..585 FT /note="Interchain (between A and B chains)" FT DISULFID 607..623 FT DISULFID 699..766 FT DISULFID 729..745 FT DISULFID 756..784 FT VARIANT 38 FT /note="K -> E (in PLGD; common mutation; dbSNP:rs73015965)" FT /evidence="ECO:0000269|PubMed:10233898" FT /id="VAR_018657" FT VARIANT 46 FT /note="I -> R (in dbSNP:rs1049573)" FT /id="VAR_011779" FT VARIANT 57 FT /note="E -> K (in dbSNP:rs4252070)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016287" FT VARIANT 89 FT /note="R -> K (in dbSNP:rs143079629)" FT /evidence="ECO:0000269|PubMed:33114181" FT /id="VAR_085811" FT VARIANT 133 FT /note="H -> Q (in dbSNP:rs4252186)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016288" FT VARIANT 147 FT /note="L -> P (in PLGD; dbSNP:rs770198253)" FT /evidence="ECO:0000269|PubMed:10233898" FT /id="VAR_018658" FT VARIANT 235 FT /note="R -> H (in PLGD; severe type 1 deficiency; FT dbSNP:rs121918030)" FT /evidence="ECO:0000269|PubMed:9242524" FT /id="VAR_018659" FT VARIANT 261 FT /note="R -> H (in dbSNP:rs4252187)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016289" FT VARIANT 330 FT /note="K -> E (in HAE4; dbSNP:rs889957249)" FT /evidence="ECO:0000269|PubMed:28795768, FT ECO:0000269|PubMed:29548426, ECO:0000269|PubMed:29952006, FT ECO:0000269|PubMed:29987869, ECO:0000269|PubMed:33114181, FT ECO:0000269|PubMed:33799813" FT /id="VAR_085812" FT VARIANT 374 FT /note="V -> F (in PLGD; Nagoya-1; dbSNP:rs121918028)" FT /evidence="ECO:0000269|PubMed:1986355" FT /id="VAR_006627" FT VARIANT 408 FT /note="R -> W (in dbSNP:rs4252119)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016290" FT VARIANT 453 FT /note="K -> I (in dbSNP:rs1804181)" FT /id="VAR_011780" FT VARIANT 472 FT /note="D -> N (in dbSNP:rs4252125)" FT /evidence="ECO:0000269|PubMed:2318848, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7, ECO:0000269|Ref.9" FT /id="VAR_016291" FT VARIANT 494 FT /note="A -> V (in dbSNP:rs4252128)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016292" FT VARIANT 523 FT /note="R -> W (in dbSNP:rs4252129)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_016293" FT VARIANT 532 FT /note="R -> H (in PLGD)" FT /evidence="ECO:0000269|PubMed:10233898" FT /id="VAR_018660" FT VARIANT 591 FT /note="S -> P (in PLGD; risk factor for thrombosis; FT dbSNP:rs121918029)" FT /evidence="ECO:0000269|PubMed:8392398" FT /id="VAR_006628" FT VARIANT 620 FT /note="A -> T (in PLGD; type 2 plasminogen deficiency; FT decreased activity; Nagoya-2/Tochigi/Kagoshima; risk factor FT for thrombosis; dbSNP:rs121918027)" FT /evidence="ECO:0000269|PubMed:1427790, FT ECO:0000269|PubMed:1986355, ECO:0000269|PubMed:6216475, FT ECO:0000269|PubMed:6238949" FT /id="VAR_006629" FT VARIANT 676 FT /note="V -> D (in dbSNP:rs17857492)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031213" FT VARIANT 728 FT /note="V -> E (in HAE4; uncertain significance; FT dbSNP:rs1582955358)" FT /evidence="ECO:0000269|PubMed:33114181" FT /id="VAR_085813" FT VARIANT 751 FT /note="G -> R (in PLGD; Kanagawa-1; 50% activity; FT dbSNP:rs121918033)" FT /evidence="ECO:0000269|PubMed:9858247" FT /id="VAR_006630" FT MUTAGEN 741 FT /note="S->A: Proteolytically cleaved, but abolishes plasmin FT activity and cell detachment. Prevents invasion of the FT mosquito vector midgut by parasite P.falciparum ookinetes." FT /evidence="ECO:0000269|PubMed:14699093, FT ECO:0000269|PubMed:21949403" FT CONFLICT 50 FT /note="A -> AQ (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="Q -> E (in Ref. 7; AA sequence and 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="Missing (in Ref. 7; AA sequence and 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="Q -> E (in Ref. 7; AA sequence and 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 701 FT /note="I -> V (in Ref. 3; AAA36451)" FT /evidence="ECO:0000305" FT STRAND 25..33 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:4DUR" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:4DUR" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:4DUR" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 85..96 FT /evidence="ECO:0007829|PDB:4DUR" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:1HPJ" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:1HPJ" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:1HPJ" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1KI0" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:1KI0" FT TURN 143..146 FT /evidence="ECO:0007829|PDB:4CIK" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1HPJ" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:1HPK" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:2DOH" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:6OG4" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:1I5K" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:1B2I" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:6OG4" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:6OG4" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:6OG4" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:6OG4" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:6OG4" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:2L0S" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:2L0S" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:2L0S" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:1KI0" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 334..339 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:1KI0" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:1PK4" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:1KRN" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:2PK4" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:1PMK" FT STRAND 436..441 FT /evidence="ECO:0007829|PDB:1KRN" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:1KRN" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 481..483 FT /evidence="ECO:0007829|PDB:2KNF" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:5HPG" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:5HPG" FT TURN 518..520 FT /evidence="ECO:0007829|PDB:5HPG" FT TURN 522..525 FT /evidence="ECO:0007829|PDB:4DUR" FT STRAND 542..546 FT /evidence="ECO:0007829|PDB:5HPG" FT STRAND 552..554 FT /evidence="ECO:0007829|PDB:5HPG" FT STRAND 582..586 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 595..600 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 605..613 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 616..619 FT /evidence="ECO:0007829|PDB:5UGG" FT HELIX 621..623 FT /evidence="ECO:0007829|PDB:5UGG" FT TURN 624..626 FT /evidence="ECO:0007829|PDB:5UGG" FT HELIX 630..632 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 633..638 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 640..644 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 650..659 FT /evidence="ECO:0007829|PDB:5UGG" FT TURN 661..663 FT /evidence="ECO:0007829|PDB:1QRZ" FT STRAND 667..673 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 698..704 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 708..711 FT /evidence="ECO:0007829|PDB:7UAH" FT STRAND 717..724 FT /evidence="ECO:0007829|PDB:5UGG" FT HELIX 726..729 FT /evidence="ECO:0007829|PDB:5UGG" FT TURN 732..737 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 743..746 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 749..751 FT /evidence="ECO:0007829|PDB:1DDJ" FT STRAND 752..754 FT /evidence="ECO:0007829|PDB:1BML" FT HELIX 757..759 FT /evidence="ECO:0007829|PDB:8F7U" FT STRAND 763..768 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 771..780 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 782..785 FT /evidence="ECO:0007829|PDB:5UGG" FT STRAND 791..795 FT /evidence="ECO:0007829|PDB:5UGG" FT HELIX 796..799 FT /evidence="ECO:0007829|PDB:5UGG" FT HELIX 800..809 FT /evidence="ECO:0007829|PDB:5UGG" SQ SEQUENCE 810 AA; 90569 MW; 8B31CB877CCB3AB6 CRC64; MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA AKCEEDEEFT CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTKN GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE CEEECMHCSG ENYDGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE LRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP SCDSSPVSTE QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHRHQ KTPENYPNAG LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEAS VVAPPPVVLL PDVETPSEED CMFGNGKGYR GKRATTVTGT PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG PWCYTTNPRK LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ EIEVSRLFLE PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF ITGWGETQGT FGAGLLKEAQ LPVIENKVCN RYEFLNGRVQ STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW GLGCARPNKP GVYVRVSRFV TWIEGVMRNN //