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
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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.
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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.
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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:
- 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:
- 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:
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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:
- 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:
- 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:
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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.
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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:
- 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:
- 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).
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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:
- 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:
- 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:
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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:
- 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:
- 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:
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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:
- 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).
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References |
- 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
- 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
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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.
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