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P06869

- UROK_MOUSE

UniProt

P06869 - UROK_MOUSE

Protein

Urokinase-type plasminogen activator

Gene

Plau

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by SERPINA5.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei226 – 2261Charge relay system
    Active sitei277 – 2771Charge relay system
    Active sitei378 – 3781Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. fibrinolysis Source: MGI
    2. regulation of cell adhesion mediated by integrin Source: Ensembl
    3. regulation of cell proliferation Source: MGI
    4. regulation of receptor activity Source: Ensembl
    5. regulation of smooth muscle cell-matrix adhesion Source: Ensembl
    6. regulation of smooth muscle cell migration Source: Ensembl
    7. response to hypoxia Source: MGI
    8. smooth muscle cell migration Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Plasminogen activation

    Protein family/group databases

    MEROPSiS01.231.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urokinase-type plasminogen activator (EC:3.4.21.73)
    Short name:
    U-plasminogen activator
    Short name:
    uPA
    Cleaved into the following 3 chains:
    Gene namesi
    Name:Plau
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:97611. Plau.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 433413Urokinase-type plasminogen activatorPRO_0000028322Add
    BLAST
    Chaini21 – 178158Urokinase-type plasminogen activator long chain ABy similarityPRO_0000028323Add
    BLAST
    Chaini157 – 17822Urokinase-type plasminogen activator short chain ABy similarityPRO_0000028324Add
    BLAST
    Chaini180 – 433254Urokinase-type plasminogen activator chain BBy similarityPRO_0000028325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 401 Publication
    Disulfide bondi34 ↔ 521 Publication
    Disulfide bondi54 ↔ 631 Publication
    Disulfide bondi71 ↔ 1521 Publication
    Disulfide bondi92 ↔ 1341 Publication
    Disulfide bondi123 ↔ 1471 Publication
    Modified residuei159 – 1591PhosphoserineBy similarity
    Disulfide bondi169 ↔ 301Interchain (between A and B chains)PROSITE-ProRule annotation
    Disulfide bondi211 ↔ 227By similarity
    Disulfide bondi219 ↔ 290By similarity
    Disulfide bondi315 ↔ 384By similarity
    Disulfide bondi347 ↔ 363By similarity
    Disulfide bondi374 ↔ 402By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP06869.
    PaxDbiP06869.
    PRIDEiP06869.

    PTM databases

    PhosphoSiteiP06869.

    Expressioni

    Gene expression databases

    ArrayExpressiP06869.
    BgeeiP06869.
    CleanExiMM_PLAU.
    GenevestigatoriP06869.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi202230. 1 interaction.
    IntActiP06869. 3 interactions.
    MINTiMINT-4139656.
    STRINGi10090.ENSMUSP00000022368.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 423
    Helixi44 – 463
    Beta strandi50 – 523
    Turni60 – 634
    Beta strandi65 – 684
    Helixi100 – 1023
    Beta strandi103 – 1064
    Turni110 – 1167
    Beta strandi118 – 1203
    Beta strandi133 – 1386
    Beta strandi141 – 1477

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LAQX-ray3.20A/B21-154[»]
    ProteinModelPortaliP06869.
    SMRiP06869. Positions 28-152, 180-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06869.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6437EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini71 – 15282KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini180 – 426247Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 5824Binds urokinase plasminogen activator surface receptorBy similarityAdd
    BLAST
    Regioni153 – 17927Connecting peptideAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Kringle, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000237314.
    HOVERGENiHBG008633.
    InParanoidiP06869.
    KOiK01348.
    OMAiKMLCAAD.
    OrthoDBiEOG75B84T.
    PhylomeDBiP06869.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 1 hit.
    InterProiIPR000742. 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]
    PfamiPF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00181. EGF. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEiPS00022. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06869-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVWLASLFL CALVVKNSEG GSVLGAPDES NCGCQNGGVC VSYKYFSRIR    50
    RCSCPRKFQG EHCEIDASKT CYHGNGDSYR GKANTDTKGR PCLAWNAPAV 100
    LQKPYNAHRP DAISLGLGKH NYCRNPDNQK RPWCYVQIGL RQFVQECMVH 150
    DCSLSKKPSS SVDQQGFQCG QKALRPRFKI VGGEFTEVEN QPWFAAIYQK 200
    NKGGSPPSFK CGGSLISPCW VASAAHCFIQ LPKKENYVVY LGQSKESSYN 250
    PGEMKFEVEQ LILHEYYRED SLAYHNDIAL LKIRTSTGQC AQPSRSIQTI 300
    CLPPRFTDAP FGSDCEITGF GKESESDYLY PKNLKMSVVK LVSHEQCMQP 350
    HYYGSEINYK MLCAADPEWK TDSCKGDSGG PLICNIEGRP TLSGIVSWGR 400
    GCAEKNKPGV YTRVSHFLDW IQSHIGEEKG LAF 433
    Length:433
    Mass (Da):48,268
    Last modified:January 1, 1988 - v1
    Checksum:iA99C35F6250443F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02389 mRNA. Translation: CAA26231.1.
    M17922 Genomic DNA. Translation: AAA40539.1.
    CCDSiCCDS26858.1.
    PIRiA29420. UKMS.
    RefSeqiNP_032899.1. NM_008873.3.
    UniGeneiMm.4183.

    Genome annotation databases

    EnsembliENSMUST00000022368; ENSMUSP00000022368; ENSMUSG00000021822.
    GeneIDi18792.
    KEGGimmu:18792.
    UCSCiuc007skx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02389 mRNA. Translation: CAA26231.1 .
    M17922 Genomic DNA. Translation: AAA40539.1 .
    CCDSi CCDS26858.1.
    PIRi A29420. UKMS.
    RefSeqi NP_032899.1. NM_008873.3.
    UniGenei Mm.4183.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LAQ X-ray 3.20 A/B 21-154 [» ]
    ProteinModelPortali P06869.
    SMRi P06869. Positions 28-152, 180-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202230. 1 interaction.
    IntActi P06869. 3 interactions.
    MINTi MINT-4139656.
    STRINGi 10090.ENSMUSP00000022368.

    Chemistry

    ChEMBLi CHEMBL1075311.

    Protein family/group databases

    MEROPSi S01.231.

    PTM databases

    PhosphoSitei P06869.

    Proteomic databases

    MaxQBi P06869.
    PaxDbi P06869.
    PRIDEi P06869.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022368 ; ENSMUSP00000022368 ; ENSMUSG00000021822 .
    GeneIDi 18792.
    KEGGi mmu:18792.
    UCSCi uc007skx.2. mouse.

    Organism-specific databases

    CTDi 5328.
    MGIi MGI:97611. Plau.

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000237314.
    HOVERGENi HBG008633.
    InParanoidi P06869.
    KOi K01348.
    OMAi KMLCAAD.
    OrthoDBi EOG75B84T.
    PhylomeDBi P06869.
    TreeFami TF329901.

    Miscellaneous databases

    EvolutionaryTracei P06869.
    NextBioi 295072.
    PROi P06869.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06869.
    Bgeei P06869.
    CleanExi MM_PLAU.
    Genevestigatori P06869.

    Family and domain databases

    Gene3Di 2.40.20.10. 1 hit.
    InterProi IPR000742. 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 ]
    Pfami PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00181. EGF. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEi PS00022. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator."
      Belin D., Vassalli J.-D., Combepine C., Godeau F., Nagamine Y., Reich E., Kocher H.P., Duvoisin R.M.
      Eur. J. Biochem. 148:225-232(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The murine urokinase-type plasminogen activator gene."
      Degen S.J.F., Heckel J.L., Reich E., Degen J.L.
      Biochemistry 26:8270-8279(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: implication for preclinical cancer therapy."
      Lin L., Gardsvoll H., Huai Q., Huang M., Ploug M.
      J. Biol. Chem. 285:10982-10992(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 21-154 IN COMPLEX WITH PLAUR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiUROK_MOUSE
    AccessioniPrimary (citable) accession number: P06869
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3