Canmetcon
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Identification
HMDB Protein ID HMDBP01984
Secondary Accession Numbers
  • 7422
Name Plasminogen
Synonyms
  1. Activation peptide
  2. Angiostatin
  3. Plasmin heavy chain A
  4. Plasmin heavy chain A, short form
  5. Plasmin light chain B
Gene Name PLG
Protein Type Enzyme
Biological Properties
General Function Involved in serine-type endopeptidase activity
Specific Function Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo
Pathways
  • Acenocoumarol Action Pathway
  • Alteplase Action Pathway
  • Aminocaproic Acid Action Pathway
  • Anistreplase Action Pathway
  • Aprotinin Action Pathway
  • Ardeparin Action Pathway
  • Argatroban Action Pathway
  • Bivalirudin Action Pathway
  • Coagulation
  • Dicoumarol Action Pathway
  • Dicumarol Action Pathway
  • Enoxaparin Action Pathway
  • Fondaparinux Action Pathway
  • Heparin Action Pathway
  • Lepirudin Action Pathway
  • Phenindione Action Pathway
  • Phenprocoumon Action Pathway
  • Reteplase Action Pathway
  • Streptokinase Action Pathway
  • Tenecteplase Action Pathway
  • Tranexamic Acid Action Pathway
  • Urokinase Action Pathway
  • Warfarin Action Pathway
  • Ximelagatran Action Pathway
Reactions Not Available
GO Classification
Function
endopeptidase activity
serine-type endopeptidase activity
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
Process
blood coagulation
metabolic process
multicellular organismal process
macromolecule metabolic process
protein metabolic process
proteolysis
regulation of body fluid levels
hemostasis
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:6
Locus 6q26
SNPs PLG
Gene Sequence
>2433 bp
ATGGAACATAAGGAAGTGGTTCTTCTACTTCTTTTATTTCTGAAATCAGGTCAAGGAGAG
CCTCTGGATGACTATGTGAATACCCAGGGGGCTTCACTGTTCAGTGTCACTAAGAAGCAG
CTGGGAGCAGGAAGTATAGAAGAATGTGCAGCAAAATGTGAGGAGGACGAAGAATTCACC
TGCAGGGCATTCCAATATCACAGTAAAGAGCAACAATGTGTGATAATGGCTGAAAACAGG
AAGTCCTCCATAATCATTAGGATGAGAGATGTAGTTTTATTTGAAAAGAAAGTGTATCTC
TCAGAGTGCAAGACTGGGAATGGAAAGAACTACAGAGGGACGATGTCCAAAACAAAAAAT
GGCATCACCTGTCAAAAATGGAGTTCCACTTCTCCCCACAGACCTAGATTCTCACCTGCT
ACACACCCCTCAGAGGGACTGGAGGAGAACTACTGCAGGAATCCAGACAACGATCCGCAG
GGGCCCTGGTGCTATACTACTGATCCAGAAAAGAGATATGACTACTGCGACATTCTTGAG
TGTGAAGAGGAATGTATGCATTGCAGTGGAGAAAACTATGACGGCAAAATTTCCAAGACC
ATGTCTGGACTGGAATGCCAGGCCTGGGACTCTCAGAGCCCACACGCTCATGGATACATT
CCTTCCAAATTTCCAAACAAGAACCTGAAGAAGAATTACTGTCGTAACCCCGATAGGGAG
CTGCGGCCTTGGTGTTTCACCACCGACCCCAACAAGCGCTGGGAACTTTGCGACATCCCC
CGCTGCACAACACCTCCACCATCTTCTGGTCCCACCTACCAGTGTCTGAAGGGAACAGGT
GAAAACTATCGCGGGAATGTGGCTGTTACCGTTTCCGGGCACACCTGTCAGCACTGGAGT
GCACAGACCCCTCACACACATAACAGGACACCAGAAAACTTCCCCTGCAAAAATTTGGAT
GAAAACTACTGCCGCAATCCTGACGGAAAAAGGGCCCCATGGTGCCATACAACCAACAGC
CAAGTGCGGTGGGAGTACTGTAAGATACCGTCCTGTGACTCCTCCCCAGTATCCACGGAA
CAATTGGCTCCCACAGCACCACCTGAGCTAACCCCTGTGGTCCAGGACTGCTACCATGGT
GATGGACAGAGCTACCGAGGCACATCCTCCACCACCACCACAGGAAAGAAGTGTCAGTCT
TGGTCATCTATGACACCACACCGGCACCAGAAGACCCCAGAAAACTACCCAAATGCTGGC
CTGACAATGAACTACTGCAGGAATCCAGATGCCGATAAAGGCCCCTGGTGTTTTACCACA
GACCCCAGCGTCAGGTGGGAGTACTGCAACCTGAAAAAATGCTCAGGAACAGAAGCGAGT
GTTGTAGCACCTCCGCCTGTTGTCCTGCTTCCAGATGTAGAGACTCCTTCCGAAGAAGAC
TGTATGTTTGGGAATGGGAAAGGATACCGAGGCAAGAGGGCGACCACTGTTACTGGGACG
CCATGCCAGGACTGGGCTGCCCAGGAGCCCCATAGACACAGCATTTTCACTCCAGAGACA
AATCCACGGGCGGGTCTGGAAAAAAATTACTGCCGTAACCCTGATGGTGATGTAGGTGGT
CCCTGGTGCTACACGACAAATCCAAGAAAACTTTACGACTACTGTGATGTCCCTCAGTGT
GCGGCCCCTTCATTTGATTGTGGGAAGCCTCAAGTGGAGCCGAAGAAATGTCCTGGAAGG
GTTGTGGGGGGGTGTGTGGCCCACCCACATTCCTGGCCCTGGCAAGTCAGTCTTAGAACA
AGGTTTGGAATGCACTTCTGTGGAGGCACCTTGATATCCCCAGAGTGGGTGTTGACTGCT
GCCCACTGCTTGGAGAAGTCCCCAAGGCCTTCATCCTACAAGGTCATCCTGGGTGCACAC
CAAGAAGTGAATCTCGAACCGCATGTTCAGGAAATAGAAGTGTCTAGGCTGTTCTTGGAG
CCCACACGAAAAGATATTGCCTTGCTAAAGCTAAGCAGTCCTGCCGTCATCACTGACAAA
GTAATCCCAGCTTGTCTGCCATCCCCAAATTATGTGGTCGCTGACCGGACCGAATGTTTC
ATCACTGGCTGGGGAGAAACCCAAGGTACTTTTGGAGCTGGCCTTCTCAAGGAAGCCCAG
CTCCCTGTGATTGAGAATAAAGTGTGCAATCGCTATGAGTTTCTGAATGGAAGAGTCCAA
TCCACCGAACTCTGTGCTGGGCATTTGGCCGGAGGCACTGACAGTTGCCAGGGTGACAGT
GGAGGTCCTCTGGTTTGCTTCGAGAAGGACAAATACATTTTACAAGGAGTCACTTCTTGG
GGTCTTGGCTGTGCACGCCCCAATAAGCCTGGTGTCTATGTTCGTGTTTCAAGGTTTGTT
ACTTGGATTGAGGGAGTGATGAGAAATAATTAA
Protein Properties
Number of Residues 810
Molecular Weight 90568.4
Theoretical pI 7.25
Pfam Domain Function
Signals
  • 1-19
Transmembrane Regions
  • None
Protein Sequence
>Plasminogen
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFT
CRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKN
GITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILE
CEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRE
LRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWS
AQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTE
QLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAG
LTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEED
CMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGG
PWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRT
RFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLE
PTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQ
LPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSW
GLGCARPNKPGVYVRVSRFVTWIEGVMRNN
GenBank ID Protein 35531
UniProtKB/Swiss-Prot ID P00747
UniProtKB/Swiss-Prot Entry Name PLMN_HUMAN
PDB IDs
GenBank Gene ID X05199
GeneCard ID PLG
GenAtlas ID PLG
HGNC ID HGNC:9071
References
General References
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  5. Petersen TE, Martzen MR, Ichinose A, Davie EW: Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system. J Biol Chem. 1990 Apr 15;265(11):6104-11. [PubMed:2318848 ]
  6. Forsgren M, Raden B, Israelsson M, Larsson K, Heden LO: Molecular cloning and characterization of a full-length cDNA clone for human plasminogen. FEBS Lett. 1987 Mar 23;213(2):254-60. [PubMed:3030813 ]
  7. 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. 1975 Jan 15;50(3):489-94. [PubMed:122932 ]
  8. Malinowski DP, Sadler JE, Davie EW: Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen. Biochemistry. 1984 Aug 28;23(18):4243-50. [PubMed:6148961 ]
  9. 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. 1975 Oct 15;58(2):539-47. [PubMed:126863 ]
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  12. Groskopf WR, Summaria L, Robbins KC: Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J Biol Chem. 1969 Jul 10;244(13):3590-7. [PubMed:4240117 ]
  13. 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. 1982 Jul 10;257(13):7401-6. [PubMed:6919539 ]
  14. 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. 1984 Nov 25;259(22):13690-4. [PubMed:6094526 ]
  15. Wang H, Prorok M, Bretthauer RK, Castellino FJ: Serine-578 is a major phosphorylation locus in human plasma plasminogen. Biochemistry. 1997 Jul 1;36(26):8100-6. [PubMed:9201958 ]
  16. Marti T, Schaller J, Rickli EE, Schmid K, Kamerling JP, Gerwig GJ, van Halbeek H, Vliegenthart JF: 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. 1988 Apr 5;173(1):57-63. [PubMed:3356193 ]
  17. Pirie-Shepherd SR, Stevens RD, Andon NL, Enghild JJ, Pizzo SV: Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2. J Biol Chem. 1997 Mar 14;272(11):7408-11. [PubMed:9054441 ]
  18. O'Reilly MS, Holmgren L, Shing Y, Chen C, Rosenthal RA, Moses M, Lane WS, Cao Y, Sage EH, Folkman J: Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell. 1994 Oct 21;79(2):315-28. [PubMed:7525077 ]
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  24. Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM: The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4. Biochemistry. 1991 Oct 29;30(43):10589-94. [PubMed:1657149 ]
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  26. Mathews II, Vanderhoff-Hanaver P, Castellino FJ, 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. 1996 Feb 27;35(8):2567-76. [PubMed:8611560 ]
  27. Stec B, Yamano A, Whitlow M, Teeter MM: Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues. Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):169-78. [PubMed:15299951 ]
  28. Parry MA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Guhrs KH, Bode W: The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action. Nat Struct Biol. 1998 Oct;5(10):917-23. [PubMed:9783753 ]
  29. Chang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ: Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry. 1998 Mar 10;37(10):3258-71. [PubMed:9521645 ]
  30. Wang X, Terzyan S, Tang J, Loy JA, Lin X, Zhang XC: Human plasminogen catalytic domain undergoes an unusual conformational change upon activation. J Mol Biol. 2000 Jan 28;295(4):903-14. [PubMed:10656799 ]
  31. Rios-Steiner JL, Schenone M, Mochalkin I, Tulinsky A, Castellino FJ: 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. 2001 May 11;308(4):705-19. [PubMed:11350170 ]
  32. Abad MC, Arni RK, Grella DK, Castellino FJ, Tulinsky A, Geiger JH: The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin. J Mol Biol. 2002 May 10;318(4):1009-17. [PubMed:12054798 ]
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  36. Rejante MR, Llinas M: 1H-NMR assignments and secondary structure of human plasminogen kringle 1. Eur J Biochem. 1994 May 1;221(3):927-37. [PubMed:8181475 ]
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  38. Sohndel S, Hu CK, Marti D, Affolter M, Schaller J, Llinas M, Rickli EE: Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains. Biochemistry. 1996 Feb 20;35(7):2357-64. [PubMed:8652577 ]
  39. Marti DN, Hu CK, An SS, 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. 1997 Sep 30;36(39):11591-604. [PubMed:9305949 ]
  40. Ichinose A, Espling ES, Takamatsu J, Saito H, Shinmyozu K, Maruyama I, Petersen TE, Davie EW: Two types of abnormal genes for plasminogen in families with a predisposition for thrombosis. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):115-9. [PubMed:1986355 ]
  41. Azuma H, Uno Y, Shigekiyo T, Saito S: Congenital plasminogen deficiency caused by a Ser572 to Pro mutation. Blood. 1993 Jul 15;82(2):475-80. [PubMed:8392398 ]
  42. 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. 1982 Oct;79(20):6132-6. [PubMed:6216475 ]
  43. 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. 1984 Aug;96(2):277-87. [PubMed:6238949 ]
  44. 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. 1992 Sep-Oct;90(1-2):7-11. [PubMed:1427790 ]
  45. Schuster V, Mingers AM, Seidenspinner S, Nussgens Z, Pukrop T, Kreth HW: Homozygous mutations in the plasminogen gene of two unrelated girls with ligneous conjunctivitis. Blood. 1997 Aug 1;90(3):958-66. [PubMed:9242524 ]
  46. 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. 1998 Dec;103(3):867-70. [PubMed:9858247 ]
  47. Schuster V, Seidenspinner S, Zeitler P, Escher C, Pleyer U, Bernauer W, Stiehm ER, Isenberg S, Seregard S, Olsson T, Mingers AM, Schambeck C, Kreth HW: Compound-heterozygous mutations in the plasminogen gene predispose to the development of ligneous conjunctivitis. Blood. 1999 May 15;93(10):3457-66. [PubMed:10233898 ]