PLMN_HUMAN
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 03-AUG-2022, entry version 260.
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 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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 [66]
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 [67]
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 [68]
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 -!- 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 -!- 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 -!- 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/";
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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 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 AlphaFoldDB; P00747; -.
DR SMR; P00747; -.
DR BioGRID; 111356; 72.
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 GlyGen; P00747; 16 sites, 54 N-linked glycans (4 sites), 12 O-linked glycans (12 sites).
DR iPTMnet; P00747; -.
DR PhosphoSitePlus; P00747; -.
DR BioMuta; PLG; -.
DR DMDM; 130316; -.
DR SWISS-2DPAGE; P00747; -.
DR CPTAC; non-CPTAC-1151; -.
DR jPOST; P00747; -.
DR MassIVE; P00747; -.
DR MaxQB; P00747; -.
DR PaxDb; P00747; -.
DR PeptideAtlas; P00747; -.
DR PRIDE; P00747; -.
DR ProteomicsDB; 51277; -.
DR Antibodypedia; 3285; 1318 antibodies from 41 providers.
DR DNASU; 5340; -.
DR Ensembl; ENST00000308192.14; ENSP00000308938.9; ENSG00000122194.19.
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 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; 164039at2759; -.
DR PhylomeDB; P00747; -.
DR TreeFam; TF329901; -.
DR BioCyc; MetaCyc:HS04553-MON; -.
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; 39 hits in 1070 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 101 other tissues.
DR ExpressionAtlas; P00747; baseline and differential.
DR Genevisible; P00747; HS.
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: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:0031232; C:extrinsic component of external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
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:0051087; F:chaperone binding; IPI:CAFA.
DR GO; GO:0004175; F:endopeptidase activity; IDA:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
DR GO; GO:1990405; F:protein antigen binding; IPI:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
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; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 4.
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 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 SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 5.
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.
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"
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)"
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; may be associated with
FT susceptibility to thrombosis; 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; may be
FT associated with susceptibility to thrombosis;
FT 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; unknown pathological significance)"
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..710
FT /evidence="ECO:0007829|PDB:1DDJ"
FT TURN 711..714
FT /evidence="ECO:0007829|PDB:1DDJ"
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 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
