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Reviewed, UniProtKB/Swiss-Prot Q5RF29 (UROK_PONAB)

Last modified June 16, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
Name: PLAU
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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.

Post-translational modification

Phosphorylation of Ser-158 and Ser-323 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.

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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: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 431411Urokinase-type plasminogen activator
PRO_0000285896
Chain21 – 177157Urokinase-type plasminogen activator long chain A By similarity
PRO_0000285897
Chain156 – 17722Urokinase-type plasminogen activator short chain A By similarity
PRO_0000285898
Chain179 – 431253Urokinase-type plasminogen activator chain B By similarity
PRO_0000285899

Regions

Domain27 – 6337EGF-like
Domain69 – 15183Kringle
Domain179 – 424246Peptidase S1
Region34 – 5724Binds urokinase plasminogen activator surface receptor By similarity
Region152 – 17827Connecting peptide By similarity

Sites

Active site2241Charge relay system By similarity
Active site2751Charge relay system By similarity
Active site3761Charge relay system By similarity

Amino acid modifications

Modified residue1581Phosphoserine By similarity
Modified residue3231Phosphoserine By similarity
Glycosylation3221N-linked (GlcNAc...) Potential
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 ↔ 299Interchain (between A and B chains) By similarity
Disulfide bond209 ↔ 225 By similarity
Disulfide bond217 ↔ 288 By similarity
Disulfide bond313 ↔ 382 By similarity
Disulfide bond345 ↔ 361 By similarity
Disulfide bond372 ↔ 400 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5RF29-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 62E7E952C870408F

FASTA43148,482
        10         20         30         40         50         60 
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ 

        70         80         90        100        110        120 
HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLAWNSATVL QQTYHAHRSD ALQLGLGKHN 

       130        140        150        160        170        180 
YCRNPDNRWR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKIV 

       190        200        210        220        230        240 
GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVV SATHCFIDYP KKEDYIVYLG 

       250        260        270        280        290        300 
RSRLNSHTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IHSKEGRCAQ PSRTIQTICL 

       310        320        330        340        350        360 
PSMYNDPPFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML 

       370        380        390        400        410        420 
CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSYFLPWIR 

       430 
SHTKEENGLA L

« Hide

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

CR857332 mRNA. Translation: CAH89628.1.
RefSeqNP_001124729.1.
UniGenePab.19463

3D structure databases

SMRQ5RF29. Positions 26-152, 179-426.
ModBaseSearch...

Protein family/group databases

MEROPSS01.231.

Genome annotation databases

GeneID100171578.

Phylogenomic databases

HOVERGENQ5RF29.
OMAQ5RF29. QPWFAAI.

Enzyme and pathway databases

BRENDA3.4.21.73. 269192.

Family and domain databases

InterProIPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
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.
ProDomPD000395. Kringle. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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...

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Entry information

Entry nameUROK_PONAB
AccessionPrimary (citable) accession number: Q5RF29
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents