Skip Header

Contribute Send feedback
Read comments (?) or add your own

P16227 (UROK_PAPCY) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. 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
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

Cleaved into the following 3 chains:

  1. Urokinase-type plasminogen activator long chain A
  2. Urokinase-type plasminogen activator short chain A
  3. Urokinase-type plasminogen activator chain B
Gene names
Name:PLAU
OrganismPapio cynocephalus (Yellow baboon)
Taxonomic identifier9556 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Papio

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

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.

Post-translational modification

Phosphorylation of Ser-157 and Ser-325 abolishes proadhesive ability but does not interfere with receptor binding 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
Glycoprotein
Phosphoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-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 – 2020 Potential
Chain21 – 433413Urokinase-type plasminogen activator
PRO_0000028326
Chain21 – 176156Urokinase-type plasminogen activator long chain A By similarity
PRO_0000028327
Chain155 – 17622Urokinase-type plasminogen activator short chain A By similarity
PRO_0000028328
Chain178 – 433256Urokinase-type plasminogen activator chain B By similarity
PRO_0000028329

Regions

Domain26 – 6237EGF-like
Domain69 – 15082Kringle
Domain178 – 426249Peptidase S1
Region33 – 5624Binds urokinase plasminogen activator surface receptor By similarity
Region151 – 17727Connecting peptide

Sites

Active site2231Charge relay system
Active site2741Charge relay system
Active site3781Charge relay system

Amino acid modifications

Modified residue1571Phosphoserine By similarity
Modified residue3251Phosphoserine By similarity
Glycosylation3241N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 38 By similarity
Disulfide bond32 ↔ 50 By similarity
Disulfide bond52 ↔ 61 By similarity
Disulfide bond69 ↔ 150 By similarity
Disulfide bond90 ↔ 132 By similarity
Disulfide bond121 ↔ 145 By similarity
Disulfide bond167 ↔ 298Interchain (between A and B chains) By similarity
Disulfide bond208 ↔ 224 By similarity
Disulfide bond216 ↔ 287 By similarity
Disulfide bond315 ↔ 384 By similarity
Disulfide bond347 ↔ 363 By similarity
Disulfide bond374 ↔ 402 By similarity

Sequences

Sequence LengthMass (Da)Tools
P16227 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 816D22DFEDDC8792

FASTA43348,595
        10         20         30         40         50         60 
MRALLAHLLL CVLVVSASKG SRELQVPSDC GCLNGGTCMS NKYFSSIHWC NCPKKFGGQH 

        70         80         90        100        110        120 
CEIDKSKTCY EGNGHFYRGK ASTDTMGRSC LAWNSATVLQ QTYHAHRSDA LQLGLGKHNY 

       130        140        150        160        170        180 
CRNPDNRRRP WCYVQVGLKQ RVQECMVHNC ADGKKPSSPP EELQFQCGQR TLRPRFKIVG 

       190        200        210        220        230        240 
GEFTTIENQP WFAAIYRRHR GGSVTYVCGG SLISPCWVVS ATHCFINYPK KEDYIVYLGR 

       250        260        270        280        290        300 
SRLNSNTQGE MKFEVENLIL HEDYSADTLA HHNDIALLKI RSKEGRCAQP SRTIQTICLP 

       310        320        330        340        350        360 
SMYNDPNDPP FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSHQKCQQP HYYGSEVTTK 

       370        380        390        400        410        420 
MLCAADPQWE TDSCQGDSGG PLVCSIQGHM TLTGIVSWGR GCALKDKPGV YTRVSRFLPW 

       430 
IHSHTREQNG LAL

« Hide

References

[1]"Nucleotide and deduced amino acid sequences of baboon urokinase-type plasminogen activator."
Au Y.P.T., Wang T.W., Clowes A.W.
Nucleic Acids Res. 18:3411-3411(1990) [PubMed: 2113276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thoracic aorta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51935 mRNA. Translation: CAA36200.1.
PIRUKBAY. S14687.

3D structure databases

ProteinModelPortalP16227.
SMRP16227. Positions 25-154, 165-428.
ModBaseSearch...

Protein family/group databases

MEROPSS01.231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008633.

Family and domain databases

InterProIPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 1 hit.
PfamPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
SMARTSM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00022. 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. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUROK_PAPCY
AccessionPrimary (citable) accession number: P16227
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents