Reviewed,
UniProtKB/Swiss-Prot Q01177 (PLMN_RAT)
Last modified
June 16, 2009.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Plasminogen EC=3.4.21.7 Cleaved into the following 5 chains: 1- Recommended name: Plasmin heavy chain A 2- Recommended name: Activation peptide 3- Recommended name: Angiostatin 4- Recommended name: Plasmin heavy chain A, short form 5- Recommended name: Plasmin light chain B | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 812 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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 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 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 By similarity. |
| Subcellular location | |
| Domain | Kringle domains mediate interaction with CSPG4 By similarity. |
| Post-translational modification | In the presence of the inhibitor, the activation involves only cleavage after Arg-581, 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. In the presence of the inhibitor, the activation involves only cleavage after Arg-581, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide By similarity. |
| 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 Tissue remodeling |
| Cellular component | Secreted |
| Domain | Kringle Repeat Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Cleavage on pair of basic residues Disulfide bond Zymogen |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysisInferred from electronic annotation. Source: UniProtKB-KW proteolysis involved in cellular protein catabolic processInferred from direct assay. Source: RGD tissue remodelingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell microsomeInferred from direct assay. Source: RGD |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activityInferred 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 | By similarity | ||||||||
| Chain | 20 – 812 | 793 | Plasminogen | PRO_0000028079 | |||||||
| Chain | 20 – 581 | 562 | Plasmin heavy chain A | PRO_0000028080 | |||||||
| Peptide | 20 – 97 | 78 | Activation peptide By similarity | PRO_0000028081 | |||||||
| Chain | 98 – 581 | 484 | Plasmin heavy chain A, short form | PRO_0000028082 | |||||||
| Chain | 98 – ?436 | 339 | Angiostatin | PRO_0000028083 | |||||||
| Chain | 582 – 812 | 231 | Plasmin light chain B | PRO_0000028084 | |||||||
Regions | |||||||||||
| Domain | 20 – 98 | 79 | PAN | ||||||||
| Domain | 102 – 181 | 80 | Kringle 1 | ||||||||
| Domain | 184 – 262 | 79 | Kringle 2 | ||||||||
| Domain | 274 – 352 | 79 | Kringle 3 | ||||||||
| Domain | 375 – 454 | 80 | Kringle 4 | ||||||||
| Domain | 480 – 560 | 81 | Kringle 5 | ||||||||
| Domain | 582 – 810 | 229 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 624 | 1 | Charge relay system By similarity | ||||||||
| Active site | 667 | 1 | Charge relay system By similarity | ||||||||
| Active site | 762 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| 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 | 376 ↔ 454 | By similarity | |||||||||
| Disulfide bond | 397 ↔ 437 | By similarity | |||||||||
| Disulfide bond | 425 ↔ 449 | By similarity | |||||||||
| Disulfide bond | 481 ↔ 560 | By similarity | |||||||||
| Disulfide bond | 502 ↔ 543 | By similarity | |||||||||
| Disulfide bond | 531 ↔ 555 | By similarity | |||||||||
| Disulfide bond | 568 ↔ 687 | Interchain (between A and B chains) By similarity | |||||||||
| Disulfide bond | 578 ↔ 586 | Interchain (between A and B chains) By similarity | |||||||||
| Disulfide bond | 609 ↔ 625 | By similarity | |||||||||
| Disulfide bond | 701 ↔ 768 | By similarity | |||||||||
| Disulfide bond | 731 ↔ 747 | By similarity | |||||||||
| Disulfide bond | 758 ↔ 786 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 418 | 1 | A → S in AAA41884. Ref.3 | ||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Rat plasminogen: cDNA and gene structure." Bangert K., Johnsen A.H., Thorsen S. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
| [3] | "Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen." Kanalas J.J., Makker S.P. J. Biol. Chem. 266:10825-10829(1991) [PubMed: 1645711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-511. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| AJ242649 mRNA. Translation: CAB46014.1. BC091135 mRNA. Translation: AAH91135.1. M62832 mRNA. Translation: AAA41884.1. | |
| IPI | IPI00206780. |
| PIR | A40522. |
| RefSeq | NP_445943.1. |
| UniGene | Rn.20178 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PMK based on UniProtKB P00747. |
| SMR | Q01177. Positions 565-812. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.233. |
Proteomic databases | |
| PRIDE | Q01177. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000017223. Rattus norvegicus. [Contig view] |
| GeneID | 85253. |
| KEGG | rno:85253. |
| NMPDR | fig|10116.3.peg.463. |
Organism-specific databases | |
| RGD | 619893. Plg. |
Phylogenomic databases | |
| HOVERGEN | Q01177. |
| OMA | Q01177. ENKVCNR. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.7. 248. |
Gene expression databases | |
| ArrayExpress | Q01177. |
| GermOnline | ENSRNOG00000017223. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR003014. PAN-1_domain. IPR003609. Pan_app. IPR011358. Pept_S1A_Plasmin. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR003966. Peptidase_S1A_prothrombin. [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. PR00018. KRINGLE. PR01505. PROTHROMBIN. |
| ProDom | PD000395. Kringle. 5 hits. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00130. KR. 5 hits. SM00473. PAN_AP. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS00021. KRINGLE_1. 5 hits. PS50070. KRINGLE_2. 5 hits. PS50948. PAN. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 617350. |
Entry information
| Entry name | PLMN_RAT | ||||||||
| Accession | Primary (citable) accession number: Q01177 Secondary accession number(s): Q5BKB6, Q9R0W3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


