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P20918

- PLMN_MOUSE

UniProt

P20918 - PLMN_MOUSE

Protein

Plasminogen

Gene

Plg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells By similarity.By similarity
    Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.

    Catalytic activityi

    Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.

    Enzyme regulationi

    Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei624 – 6241Charge relay systemBy similarity
    Active sitei667 – 6671Charge relay systemBy similarity
    Active sitei762 – 7621Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. blood coagulation Source: HGNC
    2. extracellular matrix disassembly Source: Ensembl
    3. fibrinolysis Source: UniProtKB-KW
    4. labyrinthine layer blood vessel development Source: MGI
    5. mononuclear cell migration Source: MGI
    6. muscle cell cellular homeostasis Source: MGI
    7. myoblast differentiation Source: MGI
    8. negative regulation of angiogenesis Source: MGI
    9. negative regulation of cell-substrate adhesion Source: Ensembl
    10. negative regulation of fibrinolysis Source: Ensembl
    11. positive regulation of fibrinolysis Source: Ensembl
    12. proteolysis involved in cellular protein catabolic process Source: Ensembl
    13. tissue regeneration Source: MGI
    14. tissue remodeling Source: UniProtKB-KW
    15. trophoblast giant cell differentiation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

    Enzyme and pathway databases

    ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_222614. LDL-mediated lipid transport.

    Protein family/group databases

    MEROPSiS01.233.

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:Plg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97620. Plg.

    Subcellular locationi

    Secreted By similarity
    Note: Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface By similarity.By similarity

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: HGNC
    3. extrinsic component of external side of plasma membrane Source: Ensembl
    4. extrinsic component of plasma membrane Source: MGI
    5. intracellular membrane-bounded organelle Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Chaini20 – 812793PlasminogenPRO_0000028069Add
    BLAST
    Chaini20 – 581562Plasmin heavy chain APRO_0000028070Add
    BLAST
    Peptidei20 – 9778Activation peptidePRO_0000028071Add
    BLAST
    Chaini98 – 581484Plasmin heavy chain A, short formPRO_0000028072Add
    BLAST
    Chaini98 – ?436339AngiostatinPRO_0000028073Add
    BLAST
    Chaini582 – 812231Plasmin light chain BPRO_0000028074Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 73By similarity
    Disulfide bondi53 ↔ 61By similarity
    Disulfide bondi103 ↔ 181By similarity
    Disulfide bondi124 ↔ 164By similarity
    Disulfide bondi152 ↔ 176By similarity
    Disulfide bondi185 ↔ 262By similarity
    Disulfide bondi188 ↔ 316By similarity
    Disulfide bondi206 ↔ 245By similarity
    Disulfide bondi234 ↔ 257By similarity
    Disulfide bondi275 ↔ 352By similarity
    Disulfide bondi296 ↔ 335By similarity
    Disulfide bondi324 ↔ 347By similarity
    Disulfide bondi377 ↔ 454By similarity
    Disulfide bondi398 ↔ 437By similarity
    Disulfide bondi426 ↔ 449By similarity
    Disulfide bondi481 ↔ 560By similarity
    Disulfide bondi502 ↔ 543By similarity
    Disulfide bondi531 ↔ 555By similarity
    Disulfide bondi568 ↔ 687Interchain (between A and B chains)By similarity
    Disulfide bondi578 ↔ 586Interchain (between A and B chains)By similarity
    Modified residuei598 – 5981PhosphoserineBy similarity
    Disulfide bondi609 ↔ 625By similarity
    Disulfide bondi701 ↔ 768By similarity
    Disulfide bondi731 ↔ 747By similarity
    Disulfide bondi758 ↔ 786By similarity

    Post-translational modificationi

    In the presence of the inhibitor, the activation involves only cleavage after Arg-581, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP20918.
    PaxDbiP20918.
    PRIDEiP20918.

    2D gel databases

    REPRODUCTION-2DPAGEP20918.

    PTM databases

    PhosphoSiteiP20918.

    Miscellaneous databases

    PMAP-CutDBP20918.

    Expressioni

    Gene expression databases

    BgeeiP20918.
    CleanExiMM_PLG.
    GenevestigatoriP20918.

    Interactioni

    Subunit structurei

    Interacts (both mature PLG and the angiostatin peptide) with AMOT and CSPG4. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation. Interacts (the angiostatin peptide) with ATP5A1; the interaction inhibits most of the angiogenic effects of angiostatin By similarity.By similarity

    Protein-protein interaction databases

    IntActiP20918. 4 interactions.
    MINTiMINT-4107912.

    Structurei

    3D structure databases

    ProteinModelPortaliP20918.
    SMRiP20918. Positions 20-812.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 9879PANPROSITE-ProRule annotationAdd
    BLAST
    Domaini103 – 18179Kringle 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 26279Kringle 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini275 – 35278Kringle 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini377 – 45478Kringle 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini481 – 56080Kringle 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini582 – 810229Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Kringle domains mediate interaction with CSPG4.By similarity

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
    Contains 5 kringle domains.PROSITE-ProRule annotation
    Contains 1 PAN domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00740000115022.
    HOGENOMiHOG000112892.
    HOVERGENiHBG004381.
    InParanoidiP20918.
    KOiK01315.
    OMAiEGLEENY.
    OrthoDBiEOG75B84T.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 5 hits.
    InterProiIPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR023317. Pept_S1A_plasmin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00051. Kringle. 5 hits.
    PF00024. PAN_1. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001150. Plasmin. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00130. KR. 5 hits.
    SM00473. PAN_AP. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 5 hits.
    PROSITEiPS00021. KRINGLE_1. 5 hits.
    PS50070. KRINGLE_2. 5 hits.
    PS50948. PAN. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 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.

    P20918-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDHKEVILLF LLLLKPGQGD SLDGYISTQG ASLFSLTKKQ LAAGGVSDCL    50
    AKCEGETDFV CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL 100
    SECKTGIGNG YRGTMSRTKS GVACQKWGAT FPHVPNYSPS THPNEGLEEN 150
    YCRNPDNDEQ GPWCYTTDPD KRYDYCNIPE CEEECMYCSG EKYEGKISKT 200
    MSGLDCQAWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE PRPWCFTTDP 250
    TKRWEYCDIP RCTTPPPPPS PTYQCLKGRG ENYRGTVSVT VSGKTCQRWS 300
    EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP 350
    SCESSASPDQ SDSSVPPEEQ TPVVQECYQS DGQSYRGTSS TTITGKKCQS 400
    WAAMFPHRHS KTPENFPDAG LEMNYCRNPD GDKGPWCYTT DPSVRWEYCN 450
    LKRCSETGGS VVELPTVSQE PSGPSDSETD CMYGNGKDYR GKTAVTAAGT 500
    PCQGWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDVNG PWCYTTNPRK 550
    LYDYCDIPLC ASASSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR 600
    TRFTGQHFCG GTLIAPEWVL TAAHCLEKSS RPEFYKVILG AHEEYIRGLD 650
    VQEISVAKLI LEPNNRDIAL LKLSRPATIT DKVIPACLPS PNYMVADRTI 700
    CYITGWGETQ GTFGAGRLKE AQLPVIENKV CNRVEYLNNR VKSTELCAGQ 750
    LAGGVDSCQG DSGGPLVCFE KDKYILQGVT SWGLGCARPN KPGVYVRVSR 800
    FVDWIEREMR NN 812
    Length:812
    Mass (Da):90,808
    Last modified:June 28, 2011 - v3
    Checksum:iE70E1AC8E52844E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2351R → H in AAA50168. (PubMed:2081600)Curated
    Sequence conflicti525 – 5251G → D in AAA50168. (PubMed:2081600)Curated
    Sequence conflicti649 – 6491L → S in AAM22156. 1 PublicationCurated
    Sequence conflicti649 – 6491L → S in AAH14773. (PubMed:15489334)Curated
    Sequence conflicti649 – 6491L → S in AAH57186. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04766 mRNA. Translation: AAA50168.1.
    AF481053 Genomic DNA. Translation: AAM22156.1.
    AC087901 Genomic DNA. No translation available.
    BC014773 mRNA. Translation: AAH14773.1.
    BC057186 mRNA. Translation: AAH57186.1.
    AY134430 Genomic DNA. Translation: AAN15805.1.
    CCDSiCCDS28390.1.
    PIRiA38514. PLMS.
    RefSeqiNP_032903.3. NM_008877.3.
    UniGeneiMm.971.

    Genome annotation databases

    EnsembliENSMUST00000014578; ENSMUSP00000014578; ENSMUSG00000059481.
    GeneIDi18815.
    KEGGimmu:18815.
    UCSCiuc008akt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04766 mRNA. Translation: AAA50168.1 .
    AF481053 Genomic DNA. Translation: AAM22156.1 .
    AC087901 Genomic DNA. No translation available.
    BC014773 mRNA. Translation: AAH14773.1 .
    BC057186 mRNA. Translation: AAH57186.1 .
    AY134430 Genomic DNA. Translation: AAN15805.1 .
    CCDSi CCDS28390.1.
    PIRi A38514. PLMS.
    RefSeqi NP_032903.3. NM_008877.3.
    UniGenei Mm.971.

    3D structure databases

    ProteinModelPortali P20918.
    SMRi P20918. Positions 20-812.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P20918. 4 interactions.
    MINTi MINT-4107912.

    Chemistry

    ChEMBLi CHEMBL1075299.

    Protein family/group databases

    MEROPSi S01.233.

    PTM databases

    PhosphoSitei P20918.

    2D gel databases

    REPRODUCTION-2DPAGE P20918.

    Proteomic databases

    MaxQBi P20918.
    PaxDbi P20918.
    PRIDEi P20918.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000014578 ; ENSMUSP00000014578 ; ENSMUSG00000059481 .
    GeneIDi 18815.
    KEGGi mmu:18815.
    UCSCi uc008akt.2. mouse.

    Organism-specific databases

    CTDi 5340.
    MGIi MGI:97620. Plg.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00740000115022.
    HOGENOMi HOG000112892.
    HOVERGENi HBG004381.
    InParanoidi P20918.
    KOi K01315.
    OMAi EGLEENY.
    OrthoDBi EOG75B84T.
    TreeFami TF329901.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_222614. LDL-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi PLG. mouse.
    NextBioi 295166.
    PMAP-CutDB P20918.
    PROi P20918.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20918.
    CleanExi MM_PLG.
    Genevestigatori P20918.

    Family and domain databases

    Gene3Di 2.40.20.10. 5 hits.
    InterProi IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR023317. Pept_S1A_plasmin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00051. Kringle. 5 hits.
    PF00024. PAN_1. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001150. Plasmin. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00130. KR. 5 hits.
    SM00473. PAN_AP. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 5 hits.
    PROSITEi PS00021. KRINGLE_1. 5 hits.
    PS50070. KRINGLE_2. 5 hits.
    PS50948. PAN. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the cDNA coding for mouse plasminogen and localization of the gene to mouse chromosome 17."
      Degen S.J., Bell S.M., Schaefer L.A., Elliott R.W.
      Genomics 8:49-61(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic sequence analysis in the mouse T-complex region."
      Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129/Sv.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    5. "Localization of regulatory elements mediating constitutive and cytokine-stimulated plasminogen gene expression."
      Bannach F.G., Gutierrez A., Fowler B.J., Bugge T.H., Degen J.L., Parmer R.J., Miles L.A.
      J. Biol. Chem. 277:38579-38588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
      Strain: 129/SvJ.
      Tissue: Liver.
    6. "Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma."
      O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M., Lane W.S., Cao Y., Sage E.H., Folkman J.
      Cell 79:315-328(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiPLMN_MOUSE
    AccessioniPrimary (citable) accession number: P20918
    Secondary accession number(s): Q8CIS2, Q91WJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
    In the presence of the inhibitor, the activation involves only cleavage after Arg-581, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3