Annotation for this protein is in progress - please check future releases for more complete information



DP00191: PlasminogenFASTA viewXML view

General information
DisProt:DP00191
Name:Plasminogen
Synonym(s):PLMN_HUMAN
EC=3.4.21.7
Plasmin heavy chain A [cleavage product 1]
Activation peptide [cleavage product 2]
Angiostatin [cleavage product 3]
Plasmin heavy chain A, short form [cleavage product 4]
Plasmin light chain B [cleavage product 5]
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P00747
UniGene:Hs.143436
SwissProt: PLMN_HUMAN
TrEMBL:  
NCBI (GI): 130316
Source organism:Homo sapiens (Human)
Sequence length:810
Percent disordered:1%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA AKCEEDEEFT - 60
CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTKN - 120
GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE - 180
CEEECMHCSG ENYDGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE - 240
LRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS - 300
AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP SCDSSPVSTE - 360
QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHRHQ KTPENYPNAG - 420
LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEAS VVAPPPVVLL PDVETPSEED - 480
CMFGNGKGYR GKRATTVTGT PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG - 540
PWCYTTNPRK LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT - 600
RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ EIEVSRLFLE - 660
PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF ITGWGETQGT FGAGLLKEAQ - 720
LPVIENKVCN RYEFLNGRVQ STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW - 780
GLGCARPNKP GVYVRVSRFV TWIEGVMRNN



Functional narrative    

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 it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. Kringle 4 is a domain of the human plasminogen protein. Kringle domains are present throughout various proteins that pertain to blood coagulation and fibrinolytic pathways. Kringles, in general, function mainly as recognition domains. Specifically, kringle 4 functions to bind various fibrin fragments, lysine, and zwitterions. Kringle 4 corresponds to amino acids 375-454. Human plasminogen is present in plasma and other extracellular fluids and also excreted.

Region 1: 384-384 Region 2: 389-389 Region 3: 391-391 Region 4: 400-400 Region 5: 402-402 Region 6: 403-403 Region 7: 423-423 Region 11: 426-426 Region 10: 443-443 Region 8: 449-449 Region 9: 453-453

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:384 - 384
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
 



Region 2
Type:Disordered
Name: 
Location:389 - 389
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
 



Region 3
Type:Disordered
Name: 
Location:391 - 391
Length:1
Region sequence:

T

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
This residue is part of the first disordered residue patch on the surface of the protein.




Region 4
Type:Disordered
Name: 
Location:400 - 400
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
This residue is part of the second disordered residue patch on the surface of the protein.




Region 5
Type:Disordered
Name: 
Location:402 - 402
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
This residue is part of the second disordered residue patch on the surface of the protein.




Region 6
Type:Disordered
Name: 
Location:403 - 403
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
This residue is part of the second disordered residue patch on the surface of the protein.




Region 7
Type:Disordered
Name: 
Location:423 - 423
Length:1
Region sequence:

M

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
The carbonyl group of this residue is associated with serine 91 via a strong water-mediated hydrogen bond to the nitrogen atom of the amide group.


This residue is part of the second disordered residue patch on the surface of the protein.




Region 8
Type:Disordered
Name: 
Location:449 - 449
Length:1
Region sequence:

C

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
Part of a disordered disulfide bridge (with residue 426).




Region 9
Type:Disordered
Name: 
Location:453 - 453
Length:1
Region sequence:

K

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
 



Region 10
Type:Disordered
Name: 
Location:443 - 443
Length:1
Region sequence:

S

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. X-ray crystallography (277 K; pH: 6; 1.68 (Angstroms); 22% PEG in reservoir (equilibrated against); CAC Buffer 50 mM; PEG (10% concentration); stabilized at (10% BASA))

References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
 



Region 11
Type:Disordered
Name: 
Location:426 - 426
Length:1
Region sequence:

C

Modification type: Fragment
PDB: 1KRN:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
 
References:
  1. 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; 53(Pt 2): 169-178. PubMed: 15299951

Comments:
Part of a disordered disulfide bridge (with residue 449).




References

  1. Mulichak AM, Tulinsky A, Ravichandran KG. "Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution." Biochemistry. 1991; 30(43): 10576-10588. PubMed: 1657148

  2. 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; 53(Pt 2): 169-178. PubMed: 15299951



Comments


Some of the disordered residues combine together, forming patches on the surface of the protein, which may be relevant to quaternary assemblage of proteins with kringle domains.



Disordered residues lie within the regions corresponding to cleavage products 1, 3, and 4, however, there is no experimental evidence to show that these products are disordered.


If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


Disprot-footer
Contact us