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Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B]

 PLMN_HUMAN              Reviewed;         810 AA.
P00747; Q15146; Q5TEH4; Q6PA00;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
30-AUG-2017, entry version 223.
RecName: Full=Plasminogen;
EC=3.4.21.7;
Contains:
RecName: Full=Plasmin heavy chain A;
Contains:
RecName: Full=Activation peptide;
Contains:
RecName: Full=Angiostatin;
Contains:
RecName: Full=Plasmin heavy chain A, short form;
Contains:
RecName: Full=Plasmin light chain B;
Flags: Precursor;
Name=PLG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-472.
PubMed=2318848;
Petersen T.E., Martzen M.R., Ichinose A., Davie E.W.;
"Characterization of the gene for human plasminogen, a key proenzyme
in the fibrinolytic system.";
J. Biol. Chem. 265:6104-6111(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3030813; DOI=10.1016/0014-5793(87)81501-6;
Forsgren M., Raden B., Israelsson M., Larsson K., Heden L.-O.;
"Molecular cloning and characterization of a full-length cDNA clone
for human plasminogen.";
FEBS Lett. 213:254-260(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Browne M.J., Chapman C.G., Dodd I., Carey J.E., Lawrence G.M.P.,
Mitchell D., Robinson J.H.;
"Expression of recombinant human plasminogen and aglycoplasminogen in
HeLa cells.";
Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-57; GLN-133;
HIS-261; TRP-408; ASN-472; VAL-494 AND TRP-523.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-676.
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 20-810, AND VARIANT ASN-472.
Sottrup-Jensen L., Petersen T.E., Magnusson S.;
Submitted (JUL-1977) to the PIR data bank.
[8]
PROTEIN SEQUENCE OF 20-100.
PubMed=122932; DOI=10.1111/j.1432-1033.1975.tb09887.x;
Wiman B., Wallen P.;
"Structural relationship between 'glutamic acid' and 'lysine' forms of
human plasminogen and their interaction with the NH2-terminal
activation peptide as studied by affinity chromatography.";
Eur. J. Biochem. 50:489-494(1975).
[9]
PROTEIN SEQUENCE OF 95-580; 581-626; 657-700 AND 732-810, AND VARIANT
ASN-472.
Sottrup-Jensen L., Claeys H., Zajdel M., Petersen T.E., Magnusson S.;
"The primary structure of human plasminogen.";
(In) Davidson J.F., Rowan R.M., Samama M.M., Desnoyers P.C. (eds.);
Progress in chemical fibrinolysis and thrombolysis, pp.3:191-209,
Raven Press, New York (1978).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 292-810.
PubMed=6148961; DOI=10.1021/bi00313a035;
Malinowski D.P., Sadler J.E., Davie E.W.;
"Characterization of a complementary deoxyribonucleic acid coding for
human and bovine plasminogen.";
Biochemistry 23:4243-4250(1984).
[11]
PROTEIN SEQUENCE OF 483-604.
PubMed=126863; DOI=10.1111/j.1432-1033.1975.tb02403.x;
Wiman B., Wallen P.;
"Amino-acid sequence of the cyanogen-bromide fragment from human
plasminogen that forms the linkage between the plasmin chains.";
Eur. J. Biochem. 58:539-547(1975).
[12]
PROTEIN SEQUENCE OF 581-810.
PubMed=142009; DOI=10.1111/j.1432-1033.1977.tb11578.x;
Wiman B.;
"Primary structure of the B-chain of human plasmin.";
Eur. J. Biochem. 76:129-137(1977).
[13]
ACTIVE SITE.
PubMed=4694729;
Robbins K.C., Bernabe P., Arzadon L., Summaria L.;
"The primary structure of human plasminogen. II. The histidine loop of
human plasmin: light (B) chain active center histidine sequence.";
J. Biol. Chem. 248:1631-1633(1973).
[14]
ACTIVE SITE.
PubMed=4240117;
Groskopf W.R., Summaria L., Robbins K.C.;
"Studies on the active center of human plasmin. Partial amino acid
sequence of a peptide containing the active center serine residue.";
J. Biol. Chem. 244:3590-3597(1969).
[15]
OMEGA-AMINOCARBOXYLIC ACID-BINDING SITES.
PubMed=6919539;
Trexler M., Vali Z., Patthy L.;
"Structure of the omega-aminocarboxylic acid-binding sites of human
plasminogen. Arginine 70 and aspartic acid 56 are essential for
binding of ligand by kringle 4.";
J. Biol. Chem. 257:7401-7406(1982).
[16]
FIBRIN AND OMEGA-AMINOCARBOXYLIC ACID BINDING SITES.
PubMed=6094526;
Vali Z., Patthy L.;
"The fibrin-binding site of human plasminogen. Arginines 32 and 34 are
essential for fibrin affinity of the kringle 1 domain.";
J. Biol. Chem. 259:13690-13694(1984).
[17]
PHOSPHORYLATION AT SER-597.
PubMed=9201958; DOI=10.1021/bi970328d;
Wang H., Prorok M., Bretthauer R.K., Castellino F.J.;
"Serine-578 is a major phosphorylation locus in human plasma
plasminogen.";
Biochemistry 36:8100-8106(1997).
[18]
GLYCOSYLATION AT SER-268; ASN-308 AND THR-365, AND STRUCTURE OF
CARBOHYDRATES.
PubMed=3356193; DOI=10.1111/j.1432-1033.1988.tb13966.x;
Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P.,
Gerwig G.J., van Halbeek H., Vliegenthart J.F.G.;
"The N- and O-linked carbohydrate chains of human, bovine and porcine
plasminogen. Species specificity in relation to sialylation and
fucosylation patterns.";
Eur. J. Biochem. 173:57-63(1988).
[19]
INTERACTION WITH HRG.
PubMed=9102401; DOI=10.1074/jbc.272.9.5718;
Borza D.B., Morgan W.T.;
"Acceleration of plasminogen activation by tissue plasminogen
activator on surface-bound histidine-proline-rich glycoprotein.";
J. Biol. Chem. 272:5718-5726(1997).
[20]
GLYCOSYLATION AT SER-268.
PubMed=9054441; DOI=10.1074/jbc.272.11.7408;
Pirie-Shepherd S.R., Stevens R.D., Andon N.L., Enghild J.J.,
Pizzo S.V.;
"Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of
human plasminogen 2.";
J. Biol. Chem. 272:7408-7411(1997).
[21]
CHARACTERIZATION OF ANGIOSTATIN, AND PARTIAL PROTEIN SEQUENCE.
PubMed=7525077; DOI=10.1016/0092-8674(94)90200-3;
O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A.,
Moses M., Lane W.S., Cao Y., Sage E.H., Folkman J.;
"Angiostatin: a novel angiogenesis inhibitor that mediates the
suppression of metastases by a Lewis lung carcinoma.";
Cell 79:315-328(1994).
[22]
CHARACTERIZATION OF ANGIOSTATIN.
PubMed=9102221;
Sim B.K., O'Reilly M.S., Liang H., Fortier A.H., He W., Madsen J.W.,
Lapcevich R., Nacy C.A.;
"A recombinant human angiostatin protein inhibits experimental primary
and metastatic cancer.";
Cancer Res. 57:1329-1334(1997).
[23]
PROTEOLYTIC CLEAVAGE.
PubMed=9548733; DOI=10.1021/bi9731798;
Lijnen H.R., Ugwu F., Bini A., Collen D.;
"Generation of an angiostatin-like fragment from plasminogen by
stromelysin-1 (MMP-3).";
Biochemistry 37:4699-4702(1998).
[24]
INTERACTION WITH ATP5A1, AND SUBCELLULAR LOCATION.
PubMed=10077593; DOI=10.1073/pnas.96.6.2811;
Moser T.L., Stack M.S., Asplin I., Enghild J.J., Hojrup P.,
Everitt L., Hubchak S., Schnaper H.W., Pizzo S.V.;
"Angiostatin binds ATP synthase on the surface of human endothelial
cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:2811-2816(1999).
[25]
INTERACTION WITH CSPG4, AND DOMAIN.
PubMed=10889192; DOI=10.1074/jbc.M002290200;
Goretzki L., Lombardo C.R., Stallcup W.B.;
"Binding of the NG2 proteoglycan to kringle domains modulates the
functional properties of angiostatin and plasmin(ogen).";
J. Biol. Chem. 275:28625-28633(2000).
[26]
PROTEOLYTIC PROCESSING, ENZYME REGULATION, SUBCELLULAR LOCATION,
FUNCTION OF PLASMIN, AND MUTAGENESIS OF SER-741.
PubMed=14699093; DOI=10.1074/jbc.M310964200;
Rossignol P., Ho-Tin-Noe B., Vranckx R., Bouton M.C., Meilhac O.,
Lijnen H.R., Guillin M.C., Michel J.B., Angles-Cano E.;
"Protease nexin-1 inhibits plasminogen activation-induced apoptosis of
adherent cells.";
J. Biol. Chem. 279:10346-10356(2004).
[27]
INTERACTION WITH ADA.
PubMed=15016824; DOI=10.1074/jbc.M401023200;
Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.;
"Cell surface adenosine deaminase binds and stimulates plasminogen
activation on 1-LN human prostate cancer cells.";
J. Biol. Chem. 279:20993-20998(2004).
[28]
INTERACTION WITH AMOT.
PubMed=16043488; DOI=10.1074/jbc.M503915200;
Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M.,
Holmgren L.;
"Angiomotin regulates endothelial cell-cell junctions and cell
motility.";
J. Biol. Chem. 280:34859-34869(2005).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[30]
CATALYTIC ACTIVITY.
PubMed=2143188;
Kirschbaum N.E., Budzynski A.Z.;
"A unique proteolytic fragment of human fibrinogen containing the A
alpha COOH-terminal domain of the native molecule.";
J. Biol. Chem. 265:13669-13676(1990).
[31]
INTERACTION WITH HRG.
PubMed=19712047; DOI=10.1042/BJ20090794;
Poon I.K., Olsson A.K., Hulett M.D., Parish C.R.;
"Regulation of histidine-rich glycoprotein (HRG) function via plasmin-
mediated proteolytic cleavage.";
Biochem. J. 424:27-37(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461.
PubMed=1657148; DOI=10.1021/bi00107a029;
Mulichak A.M., Tulinsky A., Ravichandran K.G.;
"Crystal and molecular structure of human plasminogen kringle 4
refined at 1.9-A resolution.";
Biochemistry 30:10576-10588(1991).
[34]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461.
PubMed=1657149; DOI=10.1021/bi00107a030;
Wu T.-P., Padmanabhan K., Tulinsky A., Mulichak A.M.;
"The refined structure of the epsilon-aminocaproic acid complex of
human plasminogen kringle 4.";
Biochemistry 30:10589-10594(1991).
[35]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 101-181.
PubMed=8054447;
Wu T.-P., Padmanabhan K.P., Tulinsky A.;
"The structure of recombinant plasminogen kringle 1 and the fibrin
binding site.";
Blood Coagul. Fibrinolysis 5:157-166(1994).
[36]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181.
PubMed=8611560; DOI=10.1021/bi9521351;
Mathews I.I., Vanderhoff-Hanaver P., Castellino F.J., Tulinsky A.;
"Crystal structures of the recombinant kringle 1 domain of human
plasminogen in complexes with the ligands epsilon-aminocaproic acid
and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid.";
Biochemistry 35:2567-2576(1996).
[37]
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454.
PubMed=15299951; DOI=10.1107/S0907444996012267;
Stec B., Yamano A., Whitlow M., Teeter M.M.;
"Structure of human plasminogen kringle 4 at 1.68 Angstrom and 277 K.
A possible structural role of disordered residues.";
Acta Crystallogr. D 53:169-178(1997).
[38]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 561-810, AND DISULFIDE
BONDS.
PubMed=9783753; DOI=10.1038/2359;
Parry M.A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K.P.,
Schlott B., Guehrs K.H., Bode W.;
"The ternary microplasmin-staphylokinase-microplasmin complex is a
proteinase-cofactor-substrate complex in action.";
Nat. Struct. Biol. 5:917-923(1998).
[39]
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563.
PubMed=9521645; DOI=10.1021/bi972284e;
Chang Y., Mochalkin I., McCance S.G., Cheng B., Tulinsky A.,
Castellino F.J.;
"Structure and ligand binding determinants of the recombinant kringle
5 domain of human plasminogen.";
Biochemistry 37:3258-3271(1998).
[40]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 564-810, AND DISULFIDE BONDS.
PubMed=10656799; DOI=10.1006/jmbi.1999.3397;
Wang X., Terzyan S., Tang J., Loy J.A., Lin X., Zhang X.C.;
"Human plasminogen catalytic domain undergoes an unusual
conformational change upon activation.";
J. Mol. Biol. 295:903-914(2000).
[41]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 183-262.
PubMed=11350170; DOI=10.1006/jmbi.2001.4646;
Rios-Steiner J.L., Schenone M., Mochalkin I., Tulinsky A.,
Castellino F.J.;
"Structure and binding determinants of the recombinant kringle-2
domain of human plasminogen to an internal peptide from a group A
Streptococcal surface protein.";
J. Mol. Biol. 308:705-719(2001).
[42]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 100-352, AND DISULFIDE
BONDS.
PubMed=12054798; DOI=10.1016/S0022-2836(02)00211-5;
Abad M.C., Arni R.K., Grella D.K., Castellino F.J., Tulinsky A.,
Geiger J.H.;
"The X-ray crystallographic structure of the angiogenesis inhibitor
angiostatin.";
J. Mol. Biol. 318:1009-1017(2002).
[43]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 562-810.
PubMed=12456874; DOI=10.1093/protein/15.9.753;
Wakeham N., Terzyan S., Zhai P., Loy J.A., Tang J., Zhang X.C.;
"Effects of deletion of streptokinase residues 48-59 on plasminogen
activation.";
Protein Eng. 15:753-761(2002).
[44]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 564-810.
PubMed=15211511; DOI=10.1002/prot.20070;
Terzyan S., Wakeham N., Zhai P., Rodgers K., Zhang X.C.;
"Characterization of Lys-698-to-Met substitution in human plasminogen
catalytic domain.";
Proteins 56:277-284(2004).
[45]
X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 564-810 IN COMPLEX WITH THE
SNAKE VENOM PROTEASE INHIBITOR TEXTILININ-1, AND DISULFIDE BOND.
PubMed=23335990; DOI=10.1371/journal.pone.0054104;
Millers E.K., Johnson L.A., Birrell G.W., Masci P.P., Lavin M.F.,
de Jersey J., Guddat L.W.;
"The structure of human microplasmin in complex with textilinin-1, an
aprotinin-like inhibitor from the Australian brown snake.";
PLoS ONE 8:E54104-E54104(2013).
[46]
STRUCTURE BY NMR OF 374-461.
PubMed=2157850; DOI=10.1016/0022-2836(90)90330-O;
Atkinson R.A., Williams R.J.P.;
"Solution structure of the kringle 4 domain from human plasminogen by
1H nuclear magnetic resonance spectroscopy and distance geometry.";
J. Mol. Biol. 212:541-552(1990).
[47]
STRUCTURE BY NMR OF 96-184.
PubMed=8181475; DOI=10.1111/j.1432-1033.1994.tb18808.x;
Rejante M.R., Llinas M.;
"1H-NMR assignments and secondary structure of human plasminogen
kringle 1.";
Eur. J. Biochem. 221:927-937(1994).
[48]
STRUCTURE BY NMR OF 96-184.
PubMed=8181476; DOI=10.1111/j.1432-1033.1994.tb18809.x;
Rejante M.R., Llinas M.;
"Solution structure of the epsilon-aminohexanoic acid complex of human
plasminogen kringle 1.";
Eur. J. Biochem. 221:939-949(1994).
[49]
STRUCTURE BY NMR OF 183-354.
PubMed=8652577; DOI=10.1021/bi9520949;
Soehndel S., Hu C.-K., Marti D., Affolter M., Schaller J., Llinas M.,
Rickli E.E.;
"Recombinant gene expression and 1H NMR characteristics of the kringle
(2 + 3) supermodule: spectroscopic/functional individuality of
plasminogen kringle domains.";
Biochemistry 35:2357-2364(1996).
[50]
STRUCTURE BY NMR OF 183-263.
PubMed=9305949; DOI=10.1021/bi971316v;
Marti D.N., Hu C.K., An S.S., von Haller P., Schaller J., Llinas M.;
"Ligand preferences of kringle 2 and homologous domains of human
plasminogen: canvassing weak, intermediate, and high-affinity binding
sites by 1H-NMR.";
Biochemistry 36:11591-11604(1997).
[51]
VARIANTS PLGD PHE-374 AND THR-620.
PubMed=1986355; DOI=10.1073/pnas.88.1.115;
Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K.,
Maruyama I., Petersen T.E., Davie E.W.;
"Two types of abnormal genes for plasminogen in families with a
predisposition for thrombosis.";
Proc. Natl. Acad. Sci. U.S.A. 88:115-119(1991).
[52]
ERRATUM.
Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K.,
Maruyama I., Petersen T.E., Davie E.W.;
Proc. Natl. Acad. Sci. U.S.A. 88:2067-2067(1991).
[53]
VARIANT PLGD PRO-591.
PubMed=8392398;
Azuma H., Uno Y., Shigekiyo T., Saito S.;
"Congenital plasminogen deficiency caused by a Ser-572 to Pro
mutation.";
Blood 82:475-480(1993).
[54]
VARIANT PLGD THR-620.
PubMed=6216475; DOI=10.1073/pnas.79.20.6132;
Miyata T., Iwanaga S., Sakata Y., Aoki N.;
"Plasminogen Tochigi: inactive plasmin resulting from replacement of
alanine-600 by threonine in the active site.";
Proc. Natl. Acad. Sci. U.S.A. 79:6132-6136(1982).
[55]
VARIANT PLGD THR-620.
PubMed=6238949;
Miyata T., Iwanaga S., Sakata Y., Aoki N., Takamatsu J., Kamiya T.;
"Plasminogens Tochigi II and Nagoya: two additional molecular defects
with Ala-600-->Thr replacement found in plasmin light chain
variants.";
J. Biochem. 96:277-287(1984).
[56]
VARIANT PLGD THR-620.
PubMed=1427790; DOI=10.1007/BF00210737;
Kikuchi S., Yamanouchi Y., Li L., Kobayashi K., Ijima H., Miyazaki R.,
Tsuchiya S., Hamaguchi H.;
"Plasminogen with type-I mutation is polymorphic in the Japanese
population.";
Hum. Genet. 90:7-11(1992).
[57]
VARIANT PLGD HIS-235.
PubMed=9242524;
Schuster V., Mingers A.-M., Seidenspinner S., Nuessgens Z., Pukrop T.,
Kreth H.W.;
"Homozygous mutations in the plasminogen gene of two unrelated girls
with ligneous conjunctivitis.";
Blood 90:958-966(1997).
[58]
VARIANT PLGD ARG-751.
PubMed=9858247; DOI=10.1046/j.1365-2141.1998.01074.x;
Higuchi Y., Furihata K., Ueno I., Ishikawa S., Okumura N., Tozuka M.,
Sakurai N.;
"Plasminogen Kanagawa-I, a novel missense mutation, is caused by the
amino acid substitution G732R.";
Br. J. Haematol. 103:867-870(1998).
[59]
VARIANTS PLGD GLU-38; PRO-147 AND HIS-532.
PubMed=10233898;
Schuster V., Seidenspinner S., Zeitler P., Escher C., Pleyer U.,
Bernauer W., Stiehm E.R., Isenberg S., Seregard S., Olsson T.,
Mingers A.-M., Schambeck C., Kreth H.W.;
"Compound-heterozygous mutations in the plasminogen gene predispose to
the development of ligneous conjunctivitis.";
Blood 93:3457-3466(1999).
-!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as
a proteolytic factor in a variety of other processes including
embryonic development, tissue remodeling, tumor invasion, and
inflammation. In ovulation, weakens the walls of the Graafian
follicle. It activates the urokinase-type plasminogen activator,
collagenases and several complement zymogens, such as C1 and C5.
Cleavage of fibronectin and laminin leads to cell detachment and
apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand
factor. Its role in tissue remodeling and tumor invasion may be
modulated by CSPG4. Binds to cells. {ECO:0000269|PubMed:14699093}.
-!- FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks
neovascularization and growth of experimental primary and
metastatic tumors in vivo. {ECO:0000269|PubMed:14699093}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa;
higher selectivity than trypsin. Converts fibrin into soluble
products. {ECO:0000269|PubMed:2143188}.
-!- ENZYME REGULATION: Converted into plasmin by plasminogen
activators, both plasminogen and its activator being bound to
fibrin. Activated with catalytic amounts of streptokinase. Plasmin
activity inhibited by SERPINE2. {ECO:0000269|PubMed:14699093}.
-!- SUBUNIT: Interacts (both mature PLG and the angiostatin peptide)
with CSPG4 and AMOT (PubMed:10889192, PubMed:16043488). Interacts
(via the Kringle domains) with HRG; the interaction tethers PLG to
the cell surface and enhances its activation (PubMed:9102401,
PubMed:19712047). Interacts (via Kringle 4 domain) with ADA; the
interaction stimulates PLG activation when in complex with DPP4
(PubMed:15016824). Angiostatin: Interacts with ATP5A1; the
interaction inhibits most of the angiogenic effects of angiostatin
(PubMed:10077593). {ECO:0000269|PubMed:10077593,
ECO:0000269|PubMed:10889192, ECO:0000269|PubMed:15016824,
ECO:0000269|PubMed:16043488, ECO:0000269|PubMed:19712047,
ECO:0000269|PubMed:9102401}.
-!- INTERACTION:
Q6V4L1:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984250;
Q6V4L4:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984286;
Q6V4L5:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984118;
Q6V4L9:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984197;
P02749:APOH; NbExp=2; IntAct=EBI-999394, EBI-2114682;
P75390:pdhA (xeno); NbExp=5; IntAct=EBI-999394, EBI-2259629;
P75391:pdhB (xeno); NbExp=11; IntAct=EBI-999394, EBI-2259621;
P75392:pdhC (xeno); NbExp=5; IntAct=EBI-999394, EBI-2259593;
P75393:pdhD (xeno); NbExp=3; IntAct=EBI-999394, EBI-2259617;
Q99SU7:sak (xeno); NbExp=7; IntAct=EBI-999394, EBI-7689378;
P00779:skc (xeno); NbExp=2; IntAct=EBI-999394, EBI-1035089;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077593,
ECO:0000269|PubMed:14699093}. Note=Locates to the cell surface
where it is proteolytically cleaved to produce the active plasmin.
Interaction with HRG tethers it to the cell surface.
-!- TISSUE SPECIFICITY: Present in plasma and many other extracellular
fluids. It is synthesized in the liver.
-!- DOMAIN: Kringle domains mediate interaction with CSPG4.
{ECO:0000269|PubMed:10889192}.
-!- PTM: N-linked glycan contains N-acetyllactosamine and sialic acid.
O-linked glycans consist of Gal-GalNAc disaccharide modified with
up to 2 sialic acid residues (microheterogeneity).
{ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193,
ECO:0000269|PubMed:9054441}.
-!- PTM: In the presence of the inhibitor, the activation involves
only cleavage after Arg-580, yielding two chains held together by
two disulfide bonds. In the absence of the inhibitor, the
activation involves additionally the removal of the activation
peptide. {ECO:0000269|PubMed:14699093,
ECO:0000269|PubMed:9548733}.
-!- DISEASE: Plasminogen deficiency (PLGD) [MIM:217090]: A disorder
characterized by decreased serum plasminogen activity. Two forms
of the disorder are distinguished: type 1 deficiency is
additionally characterized by decreased plasminogen antigen levels
and clinical symptoms, whereas type 2 deficiency, also known as
dysplasminogenemia, is characterized by normal, or slightly
reduced antigen levels, and absence of clinical manifestations.
Plasminogen deficiency type 1 results in markedly impaired
extracellular fibrinolysis and chronic mucosal pseudomembranous
lesions due to subepithelial fibrin deposition and inflammation.
The most common clinical manifestation of type 1 deficiency is
ligneous conjunctivitis in which pseudomembranes formation on the
palpebral surfaces of the eye progresses to white, yellow-white,
or red thick masses with a wood-like consistency that replace the
normal mucosa. {ECO:0000269|PubMed:10233898,
ECO:0000269|PubMed:1427790, ECO:0000269|PubMed:1986355,
ECO:0000269|PubMed:6216475, ECO:0000269|PubMed:6238949,
ECO:0000269|PubMed:8392398, ECO:0000269|PubMed:9242524,
ECO:0000269|PubMed:9858247}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin
immediately after dissociation from the clot.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Plasmin entry;
URL="https://en.wikipedia.org/wiki/Plasmin";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/plg/";
-----------------------------------------------------------------------
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EMBL; M34276; AAA60113.1; -; Genomic_DNA.
EMBL; M33272; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33274; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33275; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33278; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33279; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33280; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33282; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33283; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33284; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33285; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33286; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33287; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33288; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33289; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M33290; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M34272; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M34273; AAA60113.1; JOINED; Genomic_DNA.
EMBL; M34275; AAA60113.1; JOINED; Genomic_DNA.
EMBL; X05199; CAA28831.1; -; mRNA.
EMBL; M74220; AAA36451.1; -; mRNA.
EMBL; AY192161; AAN85555.1; -; Genomic_DNA.
EMBL; AL109933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC060513; AAH60513.1; -; mRNA.
EMBL; K02922; AAA60124.1; -; mRNA.
CCDS; CCDS5279.1; -.
PIR; A35229; PLHU.
RefSeq; NP_000292.1; NM_000301.3.
UniGene; Hs.143436; -.
PDB; 1B2I; NMR; -; A=181-263.
PDB; 1BML; X-ray; 2.90 A; A/B=561-810.
PDB; 1BUI; X-ray; 2.65 A; A/B=561-810.
PDB; 1CEA; X-ray; 2.06 A; A/B=100-187.
PDB; 1CEB; X-ray; 2.07 A; A/B=100-187.
PDB; 1DDJ; X-ray; 2.00 A; A/B/C/D=564-810.
PDB; 1HPJ; NMR; -; A=103-181.
PDB; 1HPK; NMR; -; A=103-181.
PDB; 1I5K; X-ray; 2.70 A; A/B=184-262.
PDB; 1KI0; X-ray; 1.75 A; A=100-352.
PDB; 1KRN; X-ray; 1.67 A; A=374-461.
PDB; 1L4D; X-ray; 2.30 A; A=562-810.
PDB; 1L4Z; X-ray; 2.80 A; A=563-810.
PDB; 1PK4; X-ray; 1.90 A; A=376-454.
PDB; 1PKR; X-ray; 2.48 A; A=101-181.
PDB; 1PMK; X-ray; 2.25 A; A/B=374-461.
PDB; 1QRZ; X-ray; 2.00 A; A/B/C/D=565-810.
PDB; 1RJX; X-ray; 2.30 A; B=564-810.
PDB; 2DOH; X-ray; 2.30 A; X=100-333.
PDB; 2DOI; X-ray; 3.10 A; A/X=100-333.
PDB; 2KNF; NMR; -; A=480-562.
PDB; 2L0S; NMR; -; A=272-354.
PDB; 2PK4; X-ray; 2.25 A; A=375-454.
PDB; 3UIR; X-ray; 2.78 A; A/B=564-810.
PDB; 4A5T; X-ray; 3.49 A; S=20-810.
PDB; 4CIK; X-ray; 1.78 A; A=101-181.
PDB; 4DCB; X-ray; 2.03 A; F=576-585.
PDB; 4DUR; X-ray; 2.45 A; A/B=20-810.
PDB; 4DUU; X-ray; 5.20 A; A=20-810.
PDB; 5HPG; X-ray; 1.66 A; A/B=480-563.
PDB; 5UGD; X-ray; 1.38 A; A=562-810.
PDB; 5UGG; X-ray; 1.20 A; A=562-810.
PDBsum; 1B2I; -.
PDBsum; 1BML; -.
PDBsum; 1BUI; -.
PDBsum; 1CEA; -.
PDBsum; 1CEB; -.
PDBsum; 1DDJ; -.
PDBsum; 1HPJ; -.
PDBsum; 1HPK; -.
PDBsum; 1I5K; -.
PDBsum; 1KI0; -.
PDBsum; 1KRN; -.
PDBsum; 1L4D; -.
PDBsum; 1L4Z; -.
PDBsum; 1PK4; -.
PDBsum; 1PKR; -.
PDBsum; 1PMK; -.
PDBsum; 1QRZ; -.
PDBsum; 1RJX; -.
PDBsum; 2DOH; -.
PDBsum; 2DOI; -.
PDBsum; 2KNF; -.
PDBsum; 2L0S; -.
PDBsum; 2PK4; -.
PDBsum; 3UIR; -.
PDBsum; 4A5T; -.
PDBsum; 4CIK; -.
PDBsum; 4DCB; -.
PDBsum; 4DUR; -.
PDBsum; 4DUU; -.
PDBsum; 5HPG; -.
PDBsum; 5UGD; -.
PDBsum; 5UGG; -.
DisProt; DP00191; -.
ProteinModelPortal; P00747; -.
SMR; P00747; -.
BioGrid; 111356; 38.
IntAct; P00747; 41.
STRING; 9606.ENSP00000308938; -.
BindingDB; P00747; -.
ChEMBL; CHEMBL1801; -.
DrugBank; DB00009; Alteplase.
DrugBank; DB00513; Aminocaproic Acid.
DrugBank; DB00029; Anistreplase.
DrugBank; DB06692; Aprotinin.
DrugBank; DB03709; Bicine.
DrugBank; DB04925; Desmoteplase.
DrugBank; DB00015; Reteplase.
DrugBank; DB00086; Streptokinase.
DrugBank; DB00031; Tenecteplase.
DrugBank; DB00302; Tranexamic Acid.
DrugBank; DB00013; Urokinase.
GuidetoPHARMACOLOGY; 2394; -.
MEROPS; S01.233; -.
iPTMnet; P00747; -.
PhosphoSitePlus; P00747; -.
UniCarbKB; P00747; -.
BioMuta; PLG; -.
DMDM; 130316; -.
SWISS-2DPAGE; P00747; -.
EPD; P00747; -.
MaxQB; P00747; -.
PaxDb; P00747; -.
PeptideAtlas; P00747; -.
PRIDE; P00747; -.
Ensembl; ENST00000308192; ENSP00000308938; ENSG00000122194.
GeneID; 5340; -.
KEGG; hsa:5340; -.
UCSC; uc003qtm.5; human.
CTD; 5340; -.
DisGeNET; 5340; -.
GeneCards; PLG; -.
HGNC; HGNC:9071; PLG.
HPA; CAB000668; -.
HPA; CAB016678; -.
HPA; HPA021602; -.
HPA; HPA048823; -.
HPA; HPA053770; -.
MalaCards; PLG; -.
MIM; 173350; gene.
MIM; 217090; phenotype.
neXtProt; NX_P00747; -.
OpenTargets; ENSG00000122194; -.
Orphanet; 722; Hypoplasminogenemia.
Orphanet; 97231; Ligneous conjunctivitis.
PharmGKB; PA33405; -.
eggNOG; ENOG410IDXR; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000112892; -.
HOVERGEN; HBG004381; -.
InParanoid; P00747; -.
KO; K01315; -.
OMA; PTYQCLK; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00747; -.
TreeFam; TF329901; -.
BioCyc; MetaCyc:HS04553-MONOMER; -.
BRENDA; 3.4.21.7; 2681.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
SABIO-RK; P00747; -.
ChiTaRS; PLG; human.
EvolutionaryTrace; P00747; -.
GeneWiki; Plasmin; -.
GeneWiki; Plasminogen_activator; -.
GenomeRNAi; 5340; -.
PMAP-CutDB; P00747; -.
PRO; PR:P00747; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000122194; -.
CleanEx; HS_PLG; -.
ExpressionAtlas; P00747; baseline and differential.
Genevisible; P00747; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0044218; C:other organism cell membrane; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IPI:CAFA.
GO; GO:0004175; F:endopeptidase activity; IDA:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0019900; F:kinase binding; IPI:CAFA.
GO; GO:1904854; F:proteasome core complex binding; IPI:CAFA.
GO; GO:1990405; F:protein antigen binding; IPI:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:AgBase.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:CAFA.
GO; GO:0008236; F:serine-type peptidase activity; TAS:AgBase.
GO; GO:0007596; P:blood coagulation; IMP:HGNC.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; IDA:BHF-UCL.
GO; GO:0042730; P:fibrinolysis; IDA:CAFA.
GO; GO:0051702; P:interaction with symbiont; IDA:CAFA.
GO; GO:0052213; P:interaction with symbiont via secreted substance involved in symbiotic interaction; IDA:CAFA.
GO; GO:0052182; P:modification by host of symbiont morphology or physiology via secreted substance; IDA:CAFA.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; TAS:BHF-UCL.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:BHF-UCL.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:CAFA.
GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR003609; Pan_app.
InterPro; IPR023317; Pept_S1A_plasmin.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00051; Kringle; 5.
Pfam; PF00024; PAN_1; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001150; Plasmin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00130; KR; 5.
SMART; SM00473; PAN_AP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 5.
PROSITE; PS00021; KRINGLE_1; 5.
PROSITE; PS50070; KRINGLE_2; 5.
PROSITE; PS50948; PAN; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
Kringle; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Thrombophilia;
Tissue remodeling; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:122932,
ECO:0000269|Ref.7}.
CHAIN 20 810 Plasminogen.
/FTId=PRO_0000028053.
CHAIN 20 580 Plasmin heavy chain A.
/FTId=PRO_0000028054.
PEPTIDE 20 97 Activation peptide.
/FTId=PRO_0000028055.
CHAIN 79 466 Angiostatin.
/FTId=PRO_0000028057.
CHAIN 98 580 Plasmin heavy chain A, short form.
/FTId=PRO_0000028056.
CHAIN 581 810 Plasmin light chain B.
/FTId=PRO_0000028058.
DOMAIN 20 98 PAN. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 103 181 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 184 262 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 275 352 Kringle 3. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 377 454 Kringle 4. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 481 560 Kringle 5. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 581 808 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 622 622 Charge relay system.
ACT_SITE 665 665 Charge relay system.
ACT_SITE 760 760 Charge relay system.
BINDING 134 134 Fibrin.
BINDING 136 136 Fibrin.
BINDING 136 136 Omega-aminocarboxylic acids.
BINDING 158 158 Omega-aminocarboxylic acids.
BINDING 172 172 Omega-aminocarboxylic acids.
BINDING 432 432 Omega-aminocarboxylic acids.
BINDING 445 445 Omega-aminocarboxylic acids.
SITE 78 79 Cleavage; by stromelysin-1.
SITE 466 467 Cleavage; by stromelysin-19.
SITE 580 581 Cleavage; by plasminogen activator.
MOD_RES 597 597 Phosphoserine.
{ECO:0000269|PubMed:9201958}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 268 268 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3356193,
ECO:0000269|PubMed:9054441}.
/FTId=CAR_000016.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:3356193}.
/FTId=CAR_000017.
CARBOHYD 365 365 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3356193}.
/FTId=CAR_000018.
DISULFID 49 73
DISULFID 53 61
DISULFID 103 181
DISULFID 124 164
DISULFID 152 176
DISULFID 185 262
DISULFID 188 316
DISULFID 206 245
DISULFID 234 257
DISULFID 275 352
DISULFID 296 335
DISULFID 324 347
DISULFID 377 454
DISULFID 398 437
DISULFID 426 449
DISULFID 481 560
DISULFID 502 543
DISULFID 531 555
DISULFID 567 685 Interchain (between A and B chains).
DISULFID 577 585 Interchain (between A and B chains).
DISULFID 607 623
DISULFID 699 766
DISULFID 729 745
DISULFID 756 784
VARIANT 38 38 K -> E (in PLGD; common mutation;
dbSNP:rs73015965).
{ECO:0000269|PubMed:10233898}.
/FTId=VAR_018657.
VARIANT 46 46 I -> R (in dbSNP:rs1049573).
/FTId=VAR_011779.
VARIANT 57 57 E -> K (in dbSNP:rs4252070).
{ECO:0000269|Ref.4}.
/FTId=VAR_016287.
VARIANT 133 133 H -> Q (in dbSNP:rs4252186).
{ECO:0000269|Ref.4}.
/FTId=VAR_016288.
VARIANT 147 147 L -> P (in PLGD; dbSNP:rs770198253).
{ECO:0000269|PubMed:10233898}.
/FTId=VAR_018658.
VARIANT 235 235 R -> H (in PLGD; severe type 1
deficiency; dbSNP:rs121918030).
{ECO:0000269|PubMed:9242524}.
/FTId=VAR_018659.
VARIANT 261 261 R -> H (in dbSNP:rs4252187).
{ECO:0000269|Ref.4}.
/FTId=VAR_016289.
VARIANT 374 374 V -> F (in PLGD; Nagoya-1;
dbSNP:rs121918028).
{ECO:0000269|PubMed:1986355}.
/FTId=VAR_006627.
VARIANT 408 408 R -> W (in dbSNP:rs4252119).
{ECO:0000269|Ref.4}.
/FTId=VAR_016290.
VARIANT 453 453 K -> I (in dbSNP:rs1804181).
/FTId=VAR_011780.
VARIANT 472 472 D -> N (in dbSNP:rs4252125).
{ECO:0000269|PubMed:2318848,
ECO:0000269|Ref.4, ECO:0000269|Ref.7,
ECO:0000269|Ref.9}.
/FTId=VAR_016291.
VARIANT 494 494 A -> V (in dbSNP:rs4252128).
{ECO:0000269|Ref.4}.
/FTId=VAR_016292.
VARIANT 523 523 R -> W (in dbSNP:rs4252129).
{ECO:0000269|Ref.4}.
/FTId=VAR_016293.
VARIANT 532 532 R -> H (in PLGD).
{ECO:0000269|PubMed:10233898}.
/FTId=VAR_018660.
VARIANT 591 591 S -> P (in PLGD; may be associated with
susceptibility to thrombosis;
dbSNP:rs121918029).
{ECO:0000269|PubMed:8392398}.
/FTId=VAR_006628.
VARIANT 620 620 A -> T (in PLGD; type 2 plasminogen
deficiency; decreased activity; Nagoya-2/
Tochigi/Kagoshima; may be associated with
susceptibility to thrombosis;
dbSNP:rs121918027).
{ECO:0000269|PubMed:1427790,
ECO:0000269|PubMed:1986355,
ECO:0000269|PubMed:6216475,
ECO:0000269|PubMed:6238949}.
/FTId=VAR_006629.
VARIANT 676 676 V -> D (in dbSNP:rs17857492).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031213.
VARIANT 751 751 G -> R (in PLGD; Kanagawa-1; 50%
activity; dbSNP:rs121918033).
{ECO:0000269|PubMed:9858247}.
/FTId=VAR_006630.
MUTAGEN 741 741 S->A: Proteolytically cleaved, but
abolishes plasmin activity and cell
detachment.
{ECO:0000269|PubMed:14699093}.
CONFLICT 50 50 A -> AQ (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 72 72 Q -> E (in Ref. 7; AA sequence and 8; AA
sequence). {ECO:0000305}.
CONFLICT 86 86 Missing (in Ref. 7; AA sequence and 8; AA
sequence). {ECO:0000305}.
CONFLICT 361 361 Q -> E (in Ref. 7; AA sequence and 9; AA
sequence). {ECO:0000305}.
CONFLICT 701 701 I -> V (in Ref. 3; AAA36451).
{ECO:0000305}.
STRAND 25 33 {ECO:0000244|PDB:4DUR}.
STRAND 36 42 {ECO:0000244|PDB:4DUR}.
HELIX 46 55 {ECO:0000244|PDB:4DUR}.
STRAND 57 59 {ECO:0000244|PDB:4DUR}.
STRAND 63 67 {ECO:0000244|PDB:4DUR}.
TURN 68 71 {ECO:0000244|PDB:4DUR}.
STRAND 72 77 {ECO:0000244|PDB:4DUR}.
TURN 80 82 {ECO:0000244|PDB:4DUR}.
STRAND 85 96 {ECO:0000244|PDB:4DUR}.
HELIX 97 99 {ECO:0000244|PDB:4DUR}.
STRAND 102 104 {ECO:0000244|PDB:1KI0}.
STRAND 105 110 {ECO:0000244|PDB:1HPJ}.
HELIX 113 115 {ECO:0000244|PDB:1HPJ}.
TURN 119 121 {ECO:0000244|PDB:1HPJ}.
STRAND 131 133 {ECO:0000244|PDB:1KI0}.
TURN 139 141 {ECO:0000244|PDB:1KI0}.
TURN 143 146 {ECO:0000244|PDB:4CIK}.
STRAND 148 150 {ECO:0000244|PDB:1HPJ}.
STRAND 155 157 {ECO:0000244|PDB:1HPK}.
STRAND 163 167 {ECO:0000244|PDB:1KI0}.
STRAND 172 175 {ECO:0000244|PDB:1KI0}.
STRAND 180 182 {ECO:0000244|PDB:2DOH}.
STRAND 184 186 {ECO:0000244|PDB:1KI0}.
STRAND 205 207 {ECO:0000244|PDB:1I5K}.
STRAND 209 211 {ECO:0000244|PDB:1B2I}.
STRAND 213 215 {ECO:0000244|PDB:1KI0}.
TURN 221 223 {ECO:0000244|PDB:1KI0}.
HELIX 225 227 {ECO:0000244|PDB:2DOH}.
STRAND 237 239 {ECO:0000244|PDB:1KI0}.
STRAND 244 248 {ECO:0000244|PDB:1KI0}.
STRAND 253 256 {ECO:0000244|PDB:1KI0}.
STRAND 273 276 {ECO:0000244|PDB:1KI0}.
STRAND 281 283 {ECO:0000244|PDB:2L0S}.
STRAND 291 293 {ECO:0000244|PDB:2L0S}.
STRAND 295 297 {ECO:0000244|PDB:4DUR}.
STRAND 303 305 {ECO:0000244|PDB:2L0S}.
TURN 311 313 {ECO:0000244|PDB:1KI0}.
HELIX 315 317 {ECO:0000244|PDB:1KI0}.
STRAND 334 339 {ECO:0000244|PDB:1KI0}.
STRAND 343 346 {ECO:0000244|PDB:1KI0}.
STRAND 377 379 {ECO:0000244|PDB:4DUR}.
STRAND 382 384 {ECO:0000244|PDB:4DUR}.
STRAND 405 407 {ECO:0000244|PDB:1PK4}.
TURN 413 415 {ECO:0000244|PDB:1KRN}.
TURN 417 419 {ECO:0000244|PDB:2PK4}.
STRAND 429 431 {ECO:0000244|PDB:1PMK}.
STRAND 436 441 {ECO:0000244|PDB:1KRN}.
STRAND 446 450 {ECO:0000244|PDB:1KRN}.
STRAND 460 462 {ECO:0000244|PDB:4DUR}.
STRAND 481 483 {ECO:0000244|PDB:2KNF}.
STRAND 487 489 {ECO:0000244|PDB:4DUR}.
STRAND 509 511 {ECO:0000244|PDB:5HPG}.
STRAND 514 516 {ECO:0000244|PDB:5HPG}.
TURN 518 520 {ECO:0000244|PDB:5HPG}.
TURN 522 525 {ECO:0000244|PDB:4DUR}.
STRAND 542 546 {ECO:0000244|PDB:5HPG}.
STRAND 552 554 {ECO:0000244|PDB:5HPG}.
STRAND 582 586 {ECO:0000244|PDB:1BUI}.
STRAND 595 599 {ECO:0000244|PDB:1DDJ}.
STRAND 605 613 {ECO:0000244|PDB:1DDJ}.
STRAND 616 619 {ECO:0000244|PDB:1DDJ}.
HELIX 621 624 {ECO:0000244|PDB:1DDJ}.
HELIX 630 632 {ECO:0000244|PDB:1DDJ}.
STRAND 634 638 {ECO:0000244|PDB:1DDJ}.
STRAND 640 644 {ECO:0000244|PDB:1DDJ}.
STRAND 650 659 {ECO:0000244|PDB:1DDJ}.
TURN 661 663 {ECO:0000244|PDB:1QRZ}.
STRAND 667 673 {ECO:0000244|PDB:1DDJ}.
STRAND 698 703 {ECO:0000244|PDB:1DDJ}.
STRAND 708 710 {ECO:0000244|PDB:1DDJ}.
TURN 711 714 {ECO:0000244|PDB:1DDJ}.
STRAND 717 724 {ECO:0000244|PDB:1DDJ}.
HELIX 726 729 {ECO:0000244|PDB:1DDJ}.
TURN 732 737 {ECO:0000244|PDB:1DDJ}.
STRAND 743 747 {ECO:0000244|PDB:1DDJ}.
STRAND 749 751 {ECO:0000244|PDB:1DDJ}.
STRAND 752 754 {ECO:0000244|PDB:1BML}.
STRAND 763 767 {ECO:0000244|PDB:1DDJ}.
STRAND 769 778 {ECO:0000244|PDB:1DDJ}.
HELIX 780 782 {ECO:0000244|PDB:1DDJ}.
STRAND 791 795 {ECO:0000244|PDB:1DDJ}.
HELIX 796 798 {ECO:0000244|PDB:1DDJ}.
HELIX 800 808 {ECO:0000244|PDB:1DDJ}.
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


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