Reviewed,
UniProtKB/Swiss-Prot P29598 (UROK_RAT)
Last modified
January 19, 2010.
Version 96.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Urokinase-type plasminogen activator Short name=uPA Short name=U-plasminogen activator EC=3.4.21.73 Cleaved into the following 3 chains: 1- Recommended name: Urokinase-type plasminogen activator long chain A 2- Recommended name: Urokinase-type plasminogen activator short chain A 3- Recommended name: Urokinase-type plasminogen activator 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 | 432 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 | Specifically cleave the zymogen plasminogen to form the active enzyme plasmin. |
| Catalytic activity | Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin. |
| Subunit structure | Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR By similarity. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 EGF-like domain. Contains 1 kringle domain. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Plasminogen activation |
| Cellular component | Secreted |
| Domain | EGF-like domain Kringle Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Gene Ontology (GO) | |
| Biological process | angiogenesis Inferred from mutant phenotype. Source: RGD chemotaxisTraceable author statement. Source: RGD embryo implantationInferred from expression pattern. Source: RGD proteolysisTraceable author statement. Source: RGD signal transductionTraceable author statement. Source: RGD skeletal muscle tissue regenerationInferred from mutant phenotype. Source: RGD |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 432 | 413 | Urokinase-type plasminogen activator | PRO_0000028333 | |||||||
| Chain | 20 – 177 | 158 | Urokinase-type plasminogen activator long chain A By similarity | PRO_0000028334 | |||||||
| Chain | 156 – 177 | 22 | Urokinase-type plasminogen activator short chain A By similarity | PRO_0000028335 | |||||||
| Chain | 179 – 432 | 254 | Urokinase-type plasminogen activator chain B By similarity | PRO_0000028336 | |||||||
Regions | |||||||||||
| Domain | 27 – 63 | 37 | EGF-like | ||||||||
| Domain | 70 – 151 | 82 | Kringle | ||||||||
| Domain | 179 – 425 | 247 | Peptidase S1 | ||||||||
| Region | 34 – 57 | 24 | Binds urokinase plasminogen activator surface receptor | ||||||||
| Region | 152 – 178 | 27 | Connecting peptide | ||||||||
Sites | |||||||||||
| Active site | 225 | 1 | Charge relay system | ||||||||
| Active site | 276 | 1 | Charge relay system | ||||||||
| Active site | 377 | 1 | Charge relay system | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 31 ↔ 39 | By similarity | |||||||||
| Disulfide bond | 33 ↔ 51 | By similarity | |||||||||
| Disulfide bond | 53 ↔ 62 | By similarity | |||||||||
| Disulfide bond | 70 ↔ 151 | By similarity | |||||||||
| Disulfide bond | 91 ↔ 133 | By similarity | |||||||||
| Disulfide bond | 122 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 168 ↔ 300 | Interchain (between A and B chains) By similarity | |||||||||
| Disulfide bond | 210 ↔ 226 | By similarity | |||||||||
| Disulfide bond | 218 ↔ 289 | By similarity | |||||||||
| Disulfide bond | 314 ↔ 383 | By similarity | |||||||||
| Disulfide bond | 346 ↔ 362 | By similarity | |||||||||
| Disulfide bond | 373 ↔ 401 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | N → H in CAA46601. Ref.2 | ||||||||
| Sequence conflict | 24 | 1 | E → G in CAA46601. Ref.2 | ||||||||
| Sequence conflict | 332 | 1 | D → N in CAA46601. Ref.2 | ||||||||
Sequences
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References
| [1] | "Transcriptional and posttranscriptional activation of urokinase plasminogen activator gene expression in metastatic tumor cells." Henderson B.R., Tansey W.P., Phillips S.M., Ramshaw I.A., Kefford R.F. Cancer Res. 52:2489-2496(1992) [PubMed: 1568219] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer 344. |
| [2] | Rabbani S.A. Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney. |
| [3] | "The receptor for the plasminogen activator of urokinase type is up-regulated in transformed rat thyroid cells." Ragno P., Cassano S., Degen J., Kessler C., Blasi F., Rossi G. FEBS Lett. 306:193-198(1992) [PubMed: 1321734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-62, IDENTIFICATION OF UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR BINDING DOMAIN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X63434 mRNA. Translation: CAA45028.1. X65651 mRNA. Translation: CAA46601.1. X66907 Genomic DNA. Translation: CAA47356.1. |
| IPI | IPI00205838. |
| PIR | S18932. S24604. |
| UniGene | Rn.6064 |
3D structure databases | |
| SMR | P29598. Positions 29-155, 166-427. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P29598. |
Protein family/group databases | |
| MEROPS | S01.231. |
PTM databases | |
| PhosphoSite | P29598. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000014273; ENSRNOP00000014273; ENSRNOG00000010516; Rattus norvegicus. [Genome view] |
Organism-specific databases | |
| RGD | 3343. Plau. |
Phylogenomic databases | |
| eggNOG | roNOG07876. |
| HOVERGEN | P29598. |
| InParanoid | P29598. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.73. 248. |
Gene expression databases | |
| ArrayExpress | P29598. |
| Genevestigator | P29598. |
| GermOnline | ENSRNOG00000010516. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR000001. Kringle. IPR013806. Kringle-like. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR009003. Ser/Cys_Pept_Trypsin-like. [Graphical view] |
| Gene3D | G3DSA:2.40.20.10. Kringle. 1 hit. |
| Pfam | PF00051. Kringle. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. PR00018. KRINGLE. |
| SMART | SM00181. EGF. 1 hit. SM00130. KR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS00022. EGF_1. 1 hit. PS01186. EGF_2. False negative. PS50026. EGF_3. 1 hit. PS00021. KRINGLE_1. 1 hit. PS50070. KRINGLE_2. 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 | UROK_RAT | ||||||||
| Accession | Primary (citable) accession number: P29598 Secondary accession number(s): Q6LBK5 | ||||||||
| 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


