P06867 (PLMN_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Plasminogen EC=3.4.21.7 Cleaved into the following 4 chains: | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) [Reference proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus![]() |
Protein attributes
| Sequence length | 809 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products. |
| Enzyme regulation | Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase. |
| Subunit structure | Interacts with CSPG4 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation By similarity. |
| Subcellular location | Secreted By similarity. 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 By similarity. |
| Domain | Kringle domains mediate interaction with CSPG4 By similarity. |
| Post-translational modification | N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after Arg-579, 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 By similarity. |
| Miscellaneous | Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot. |
| Sequence similarities | Belongs to the peptidase S1 family. Plasminogen subfamily. Contains 5 kringle domains. Contains 1 PAN domain. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation Fibrinolysis Hemostasis Tissue remodeling |
| Cellular component | Secreted |
| Domain | Kringle Repeat Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Zymogen |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysisInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW tissue remodelingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.2 | ||||||||
| Chain | 20 – 809 | 790 | Plasminogen | PRO_0000285882 | |||||||
| Chain | 20 – 579 | 560 | Plasmin heavy chain A | PRO_0000028075 | |||||||
| Peptide | 20 – 97 | 78 | Activation peptide By similarity | PRO_0000028076 | |||||||
| Chain | 98 – 579 | 482 | Plasmin heavy chain A, short form | PRO_0000028077 | |||||||
| Chain | 580 – 809 | 230 | Plasmin light chain B | PRO_0000028078 | |||||||
Regions | |||||||||||
| Domain | 20 – 98 | 79 | PAN | ||||||||
| Domain | 103 – 181 | 79 | Kringle 1 | ||||||||
| Domain | 185 – 262 | 78 | Kringle 2 | ||||||||
| Domain | 275 – 352 | 78 | Kringle 3 | ||||||||
| Domain | 377 – 454 | 78 | Kringle 4 | ||||||||
| Domain | 480 – 559 | 80 | Kringle 5 | ||||||||
| Domain | 580 – 807 | 228 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 621 | 1 | Charge relay system | ||||||||
| Active site | 664 | 1 | Charge relay system | ||||||||
| Active site | 759 | 1 | Charge relay system | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 596 | 1 | Phosphoserine By similarity | ||||||||
| Glycosylation | 308 | 1 | N-linked (GlcNAc...) Ref.4 | CAR_000019 | |||||||
| Glycosylation | 359 | 1 | O-linked (GalNAc...) Ref.4 | CAR_000020 | |||||||
| Disulfide bond | 49 ↔ 73 | By similarity | |||||||||
| Disulfide bond | 53 ↔ 61 | By similarity | |||||||||
| Disulfide bond | 103 ↔ 181 | By similarity | |||||||||
| Disulfide bond | 124 ↔ 164 | By similarity | |||||||||
| Disulfide bond | 152 ↔ 176 | By similarity | |||||||||
| Disulfide bond | 185 ↔ 262 | By similarity | |||||||||
| Disulfide bond | 188 ↔ 316 | By similarity | |||||||||
| Disulfide bond | 206 ↔ 245 | By similarity | |||||||||
| Disulfide bond | 234 ↔ 257 | By similarity | |||||||||
| Disulfide bond | 275 ↔ 352 | By similarity | |||||||||
| Disulfide bond | 296 ↔ 335 | By similarity | |||||||||
| Disulfide bond | 324 ↔ 347 | By similarity | |||||||||
| Disulfide bond | 377 ↔ 454 | By similarity | |||||||||
| Disulfide bond | 398 ↔ 437 | By similarity | |||||||||
| Disulfide bond | 426 ↔ 449 | By similarity | |||||||||
| Disulfide bond | 480 ↔ 559 | By similarity | |||||||||
| Disulfide bond | 501 ↔ 542 | By similarity | |||||||||
| Disulfide bond | 530 ↔ 554 | By similarity | |||||||||
| Disulfide bond | 566 ↔ 684 | Interchain (between A and B chains) By similarity | |||||||||
| Disulfide bond | 576 ↔ 584 | Interchain (between A and B chains) By similarity | |||||||||
| Disulfide bond | 606 ↔ 622 | By similarity | |||||||||
| Disulfide bond | 698 ↔ 765 | By similarity | |||||||||
| Disulfide bond | 728 ↔ 744 | By similarity | |||||||||
| Disulfide bond | 755 ↔ 783 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 361 | 1 | Y → H AA sequence Ref.2 | ||||||||
| Sequence conflict | 599 | 1 | H → Y AA sequence Ref.3 | ||||||||
| Sequence conflict | 602 | 1 | G → R AA sequence Ref.3 | ||||||||
| Sequence conflict | 675 | 1 | I → V AA sequence Ref.3 | ||||||||
Sequences
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References
| [1] | Chen Y., Tan W., Cheng J. Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Amino acid sequence of the heavy chain of porcine plasmin. Comparison of the carbohydrate attachment sites with the human and bovine species." Schaller J., Marti T., Roesselet S.J., Kaempfer U., Rickli E.E. Fibrinolysis 1:91-102(1987) Cited for: PROTEIN SEQUENCE OF 20-579. |
| [3] | "Determination of the complete amino-acid sequence of porcine miniplasminogen." Marti T., Schaller J., Rickli E.E. Eur. J. Biochem. 149:279-285(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 469-809. |
| [4] | "The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns." Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., Vliegenthart J.F.G. Eur. J. Biochem. 173:57-63(1988) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-308 AND THR-359, STRUCTURE OF CARBOHYDRATES. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ530369 mRNA. Translation: ABF82358.1. |
| PIR | PLPG. S03733. |
| RefSeq | NP_001038055.1. NM_001044590.2. |
| UniGene | Ssc.65489. |
3D structure databases | |
| ProteinModelPortal | P06867. |
| SMR | P06867. Positions 100-352, 376-458, 479-559, 563-809. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9823.ENSSSCP00000004364. |
Protein family/group databases | |
| MEROPS | S01.233. |
PTM databases | |
| GlycoSuiteDB | P06867. |
Proteomic databases | |
| PaxDb | P06867. |
| PRIDE | P06867. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 733660. |
| KEGG | ssc:733660. |
Organism-specific databases | |
| CTD | 5340. |
Phylogenomic databases | |
| eggNOG | COG5640. |
| HOGENOM | HOG000112892. |
| HOVERGEN | HBG004381. |
| KO | K01315. |
| OrthoDB | EOG4RR6GQ. |
Family and domain databases | |
| Gene3D | 2.40.20.10. 5 hits. |
| InterPro | IPR000001. Kringle. IPR013806. Kringle-like. IPR018056. Kringle_CS. IPR003014. PAN-1_domain. IPR003609. Pan_app. IPR023317. Pept_S1A_plasmin. IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF00051. Kringle. 5 hits. PF00024. PAN_1. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view] |
| PIRSF | PIRSF001150. Plasmin. 1 hit. |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00130. KR. 5 hits. SM00473. PAN_AP. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF57440. Kringle-like. 5 hits. SSF50494. Pept_Ser_Cys. 1 hit. |
| PROSITE | PS00021. KRINGLE_1. 5 hits. PS50070. KRINGLE_2. 5 hits. PS50948. PAN. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLMN_PIG | ||||||||
| Accession | Primary (citable) accession number: P06867 Secondary accession number(s): Q19AZ9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
