Reviewed,
UniProtKB/Swiss-Prot P33574 (PLMN_PETMA)
Last modified
June 16, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Plasminogen EC=3.4.21.7 |
| Organism | Petromyzon marinus (Sea lamprey) |
| Taxonomic identifier | 7757 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Hyperoartia › Petromyzontiformes › Petromyzontidae › Petromyzon |
Protein attributes
| Sequence length | 325 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S1 family. Plasminogen subfamily. Contains at least 2 kringle domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation Fibrinolysis Tissue remodeling |
| Cellular component | Secreted |
| Domain | Kringle |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Technical term | Direct protein sequencing |
| 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: InterPro 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›325 | ›325 | Plasminogen | PRO_0000088706 | |||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 81 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 102 ↔ 135 | By similarity | |||||||||
| Disulfide bond | 124 ↔ 141 | By similarity | |||||||||
| Disulfide bond | 188 ↔ 212 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-adjacent residues | 15 – 16 | 2 | |||||||||
| Non-adjacent residues | 34 – 35 | 2 | |||||||||
| Non-adjacent residues | 44 – 45 | 2 | |||||||||
| Non-adjacent residues | 76 – 77 | 2 | |||||||||
| Non-adjacent residues | 111 – 112 | 2 | |||||||||
| Non-adjacent residues | 138 – 139 | 2 | |||||||||
| Non-adjacent residues | 158 – 159 | 2 | |||||||||
| Non-adjacent residues | 178 – 179 | 2 | |||||||||
| Non-adjacent residues | 216 – 217 | 2 | |||||||||
| Non-adjacent residues | 236 – 237 | 2 | |||||||||
| Non-adjacent residues | 267 – 268 | 2 | |||||||||
| Non-adjacent residues | 282 – 283 | 2 | |||||||||
| Non-adjacent residues | 295 – 296 | 2 | |||||||||
| Non-adjacent residues | 307 – 308 | 2 | |||||||||
| Non-adjacent residues | 315 – 316 | 2 | |||||||||
| Non-terminal residue | 325 | 1 | |||||||||
Sequences
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References
| [1] | "Isolation, characterization and partial amino acid sequence of lamprey plasminogen." Affolter M., Schaller J., Rickli E.E. Protein Seq. Data Anal. 5:207-211(1993) Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S33879. |
3D structure databases | |
| HSSP | HSSP built from PDB template 5HPG based on UniProtKB P00747. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.233. |
Phylogenomic databases | |
| HOVERGEN | P33574. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.7. 276373. |
Family and domain databases | |
| InterPro | IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. [Graphical view] |
| Gene3D | G3DSA:2.40.20.10. Kringle. 2 hits. |
| Pfam | PF00051. Kringle. 2 hits. [Graphical view] |
| PRINTS | PR00018. KRINGLE. |
| ProDom | PD000395. Kringle. 3 hits. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00130. KR. 2 hits. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS00021. KRINGLE_1. 2 hits. PS50070. KRINGLE_2. 2 hits. PS50240. TRYPSIN_DOM. Partial match. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLMN_PETMA | ||||||||
| Accession | Primary (citable) accession number: P33574 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


