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P29598 (UROK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urokinase-type plasminogen activator

Short name=U-plasminogen activator
Short name=uPA
EC=3.4.21.73
Gene names
Name:Plau
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

Catalytic activity

Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

Enzyme regulation

Inhibited by SERPINA5 By similarity.

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. Forms heterodimer with SERPINA5. 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 processPlasminogen activation
   Cellular componentSecreted
   DomainEGF-like domain
Kringle
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from mutant phenotype PubMed 15854129. Source: RGD

cellular response to fluid shear stress

Inferred from expression pattern PubMed 19166201. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 17953365. Source: RGD

cellular response to hepatocyte growth factor stimulus

Inferred from expression pattern PubMed 19834131. Source: RGD

cellular response to hypoxia

Inferred from expression pattern PubMed 19490965. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 19184369. Source: RGD

cellular response to organic substance

Inferred from expression pattern PubMed 20731662. Source: RGD

cellular response to staurosporine

Inferred from expression pattern PubMed 19137075. Source: RGD

embryo implantation

Inferred from expression pattern PubMed 15019809. Source: RGD

neuron death

Inferred from mutant phenotype PubMed 17939964. Source: RGD

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 16899994. Source: RGD

positive regulation of ovulation

Inferred from mutant phenotype PubMed 10727258. Source: RGD

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 16456094. Source: RGD

positive regulation of smooth muscle cell migration

Inferred from mutant phenotype PubMed 9315743. Source: RGD

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of hepatocyte proliferation

Inferred from mutant phenotype PubMed 17587687. Source: RGD

response to activity

Inferred from expression pattern PubMed 22592543. Source: RGD

response to hepatocyte growth factor

Inferred from expression pattern PubMed 21843593. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 19099788. Source: RGD

skeletal muscle tissue regeneration

Inferred from mutant phenotype PubMed 12919869. Source: RGD

spermatogenesis

Inferred from expression pattern PubMed 17712486. Source: RGD

wound healing

Inferred from mutant phenotype PubMed 15854129. Source: RGD

   Cellular_componentextracellular space

Inferred from direct assay PubMed 10727258. Source: RGD

membrane

Inferred from direct assay PubMed 17939964. Source: RGD

   Molecular_functionpeptidase activity

Inferred from direct assay PubMed 2509088. Source: RGD

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 432413Urokinase-type plasminogen activator
PRO_0000028333
Chain20 – 177158Urokinase-type plasminogen activator long chain A By similarity
PRO_0000028334
Chain156 – 17722Urokinase-type plasminogen activator short chain A By similarity
PRO_0000028335
Chain179 – 432254Urokinase-type plasminogen activator chain B By similarity
PRO_0000028336

Regions

Domain27 – 6337EGF-like
Domain70 – 15182Kringle
Domain179 – 425247Peptidase S1
Region34 – 5724Binds urokinase plasminogen activator surface receptor
Region152 – 17827Connecting peptide

Sites

Active site2251Charge relay system
Active site2761Charge relay system
Active site3771Charge relay system

Amino acid modifications

Modified residue1581Phosphoserine By similarity
Disulfide bond31 ↔ 39 By similarity
Disulfide bond33 ↔ 51 By similarity
Disulfide bond53 ↔ 62 By similarity
Disulfide bond70 ↔ 151 By similarity
Disulfide bond91 ↔ 133 By similarity
Disulfide bond122 ↔ 146 By similarity
Disulfide bond168 ↔ 300Interchain (between A and B chains) By similarity
Disulfide bond210 ↔ 226 By similarity
Disulfide bond218 ↔ 289 By similarity
Disulfide bond314 ↔ 383 By similarity
Disulfide bond346 ↔ 362 By similarity
Disulfide bond373 ↔ 401 By similarity

Experimental info

Sequence conflict161N → H in CAA46601. Ref.2
Sequence conflict241E → G in CAA46601. Ref.2
Sequence conflict3321D → N in CAA46601. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29598 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 4EB1B96C716244C8

FASTA43247,957
        10         20         30         40         50         60 
MRVWLASLFL CALVANSEGG SELEASDESN CGCQNGGVCV SYKYFSSIRR CSCPKKFKGE 

        70         80         90        100        110        120 
HCEIDTSKTC YHGNGQSYRG KANTDTKGRP CLAWNSPAVL QQTYNAHRSD ALSLGLGKHN 

       130        140        150        160        170        180 
YCRNPDNQRR PWCYVQIGLK QFVQECMVQD CSLSKKPSST VDQQGFQCGQ KALRPRFKIV 

       190        200        210        220        230        240 
GGEFTVVENQ PWFAAIYLKN KGGSPPSFKC GGSLISPCWV ASATHCFVNQ PKKEEYVVYL 

       250        260        270        280        290        300 
GQSKRNSYNP GEMKFEVEQL ILHEDFSDET LAFHNDIALL KIRTSTGQCA QPSRTIQTIC 

       310        320        330        340        350        360 
LPPRFGDAPF GSDCEITGFG QESATDYFYP KDLKMSVVKI ISHEQCKQPH YYGSEINYKM 

       370        380        390        400        410        420 
LCAADPEWKT DSCSGDSGGP LICNIDGRPT LSGIVSWGSG CAEKNKPGVY TRVSYFLNWI 

       430 
QSHIGEENGL AF 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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.
PIRS18932. S24604.
UniGeneRn.6064.

3D structure databases

ProteinModelPortalP29598.
SMRP29598. Positions 29-155, 166-427.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075245.

Protein family/group databases

MEROPSS01.231.

PTM databases

PhosphoSiteP29598.

Proteomic databases

PaxDbP29598.
PRIDEP29598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3343. rat.

Organism-specific databases

RGD3343. Plau.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000237314.
HOVERGENHBG008633.
InParanoidP29598.
PhylomeDBP29598.

Gene expression databases

GenevestigatorP29598.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP29598.

Entry information

Entry nameUROK_RAT
AccessionPrimary (citable) accession number: P29598
Secondary accession number(s): Q6LBK5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries