PLMN_MOUSE
ID PLMN_MOUSE Reviewed; 812 AA.
AC P20918; Q8CIS2; Q91WJ5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Plasminogen;
DE EC=3.4.21.7;
DE Contains:
DE RecName: Full=Plasmin heavy chain A;
DE Contains:
DE RecName: Full=Activation peptide;
DE Contains:
DE RecName: Full=Angiostatin;
DE Contains:
DE RecName: Full=Plasmin heavy chain A, short form;
DE Contains:
DE RecName: Full=Plasmin light chain B;
DE Flags: Precursor;
GN Name=Plg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2081600; DOI=10.1016/0888-7543(90)90225-j;
RA Degen S.J., Bell S.M., Schaefer L.A., Elliott R.W.;
RT "Characterization of the cDNA coding for mouse plasminogen and localization
RT of the gene to mouse chromosome 17.";
RL Genomics 8:49-61(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=12149246; DOI=10.1074/jbc.m202509200;
RA Bannach F.G., Gutierrez A., Fowler B.J., Bugge T.H., Degen J.L.,
RA Parmer R.J., Miles L.A.;
RT "Localization of regulatory elements mediating constitutive and cytokine-
RT stimulated plasminogen gene expression.";
RL J. Biol. Chem. 277:38579-38588(2002).
RN [6]
RP CHARACTERIZATION OF ANGIOSTATIN, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7525077; DOI=10.1016/0092-8674(94)90200-3;
RA O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M.,
RA Lane W.S., Cao Y., Sage E.H., Folkman J.;
RT "Angiostatin: a novel angiogenesis inhibitor that mediates the suppression
RT of metastases by a Lewis lung carcinoma.";
RL Cell 79:315-328(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a
CC proteolytic factor in a variety of other processes including embryonic
CC development, tissue remodeling, tumor invasion, and inflammation. In
CC ovulation, weakens the walls of the Graafian follicle. It activates the
CC urokinase-type plasminogen activator, collagenases and several
CC complement zymogens, such as C1 and C5. Cleavage of fibronectin and
CC laminin leads to cell detachment and apoptosis. Also cleaves fibrin,
CC thrombospondin and von Willebrand factor. Its role in tissue remodeling
CC and tumor invasion may be modulated by CSPG4. Binds to cells (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks
CC neovascularization and growth of experimental primary and metastatic
CC tumors in vivo.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher
CC selectivity than trypsin. Converts fibrin into soluble products.;
CC EC=3.4.21.7;
CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators,
CC both plasminogen and its activator being bound to fibrin. Cannot be
CC activated with streptokinase.
CC -!- SUBUNIT: Interacts (both mature PLG and the angiostatin peptide) with
CC AMOT and CSPG4. Interacts (via the Kringle domains) with HRG; the
CC interaction tethers PLG to the cell surface and enhances its
CC activation. Interacts (via Kringle 4 domain) with ADA; the interaction
CC stimulates PLG activation when in complex with DPP4. Angiostatin:
CC Interacts with ATP5F1A; the interaction inhibits most of the angiogenic
CC effects of angiostatin. {ECO:0000250|UniProtKB:P00747}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell
CC surface where it is proteolytically cleaved to produce the active
CC plasmin. Interaction with HRG tethers it to the cell surface (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Kringle domains mediate interaction with CSPG4. {ECO:0000250}.
CC -!- PTM: In the presence of the inhibitor, the activation involves only
CC cleavage after Arg-581, yielding two chains held together by two
CC disulfide bonds. In the absence of the inhibitor, the activation
CC involves additionally the removal of the activation peptide (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin
CC immediately after dissociation from the clot.
CC -!- MISCELLANEOUS: In the presence of the inhibitor, the activation
CC involves only cleavage after Arg-581, resulting in 2 chains held
CC together by 2 disulfide bonds. Without the inhibitor, the activation
CC involves also removal of the activation peptide.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; J04766; AAA50168.1; -; mRNA.
DR EMBL; AF481053; AAM22156.1; -; Genomic_DNA.
DR EMBL; AC087901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014773; AAH14773.1; -; mRNA.
DR EMBL; BC057186; AAH57186.1; -; mRNA.
DR EMBL; AY134430; AAN15805.1; -; Genomic_DNA.
DR CCDS; CCDS28390.1; -.
DR PIR; A38514; PLMS.
DR RefSeq; NP_032903.3; NM_008877.3.
DR AlphaFoldDB; P20918; -.
DR SMR; P20918; -.
DR BioGRID; 202248; 10.
DR IntAct; P20918; 3.
DR MINT; P20918; -.
DR STRING; 10090.ENSMUSP00000014578; -.
DR BindingDB; P20918; -.
DR ChEMBL; CHEMBL1075299; -.
DR MEROPS; S01.233; -.
DR iPTMnet; P20918; -.
DR PhosphoSitePlus; P20918; -.
DR SwissPalm; P20918; -.
DR REPRODUCTION-2DPAGE; P20918; -.
DR CPTAC; non-CPTAC-3345; -.
DR jPOST; P20918; -.
DR MaxQB; P20918; -.
DR PaxDb; P20918; -.
DR PeptideAtlas; P20918; -.
DR PRIDE; P20918; -.
DR ProteomicsDB; 289622; -.
DR DNASU; 18815; -.
DR Ensembl; ENSMUST00000014578; ENSMUSP00000014578; ENSMUSG00000059481.
DR GeneID; 18815; -.
DR KEGG; mmu:18815; -.
DR UCSC; uc008akt.2; mouse.
DR CTD; 5340; -.
DR MGI; MGI:97620; Plg.
DR VEuPathDB; HostDB:ENSMUSG00000059481; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR GeneTree; ENSGT00940000155208; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; P20918; -.
DR OMA; NSQTPHA; -.
DR OrthoDB; 164039at2759; -.
DR PhylomeDB; P20918; -.
DR TreeFam; TF329901; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR Reactome; R-MMU-8964041; LDL remodeling.
DR BioGRID-ORCS; 18815; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Plg; mouse.
DR PRO; PR:P20918; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P20918; protein.
DR Bgee; ENSMUSG00000059481; Expressed in left lobe of liver and 51 other tissues.
DR Genevisible; P20918; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0034358; C:plasma lipoprotein particle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; ISS:HGNC-UCL.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0071674; P:mononuclear cell migration; IMP:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:0045445; P:myoblast differentiation; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; TAS:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0042246; P:tissue regeneration; IMP:MGI.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR CDD; cd00108; KR; 5.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 4.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR023317; Pept_S1A_plasmin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00051; Kringle; 5.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001150; Plasmin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 5.
DR PROSITE; PS00021; KRINGLE_1; 5.
DR PROSITE; PS50070; KRINGLE_2; 5.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Fibrinolysis; Hemostasis;
KW Hydrolase; Kringle; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Tissue remodeling; Zymogen.
FT SIGNAL 1..19
FT CHAIN 20..812
FT /note="Plasminogen"
FT /id="PRO_0000028069"
FT CHAIN 20..581
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028070"
FT PEPTIDE 20..97
FT /note="Activation peptide"
FT /id="PRO_0000028071"
FT CHAIN 98..581
FT /note="Plasmin heavy chain A, short form"
FT /id="PRO_0000028072"
FT CHAIN 98..?436
FT /note="Angiostatin"
FT /id="PRO_0000028073"
FT CHAIN 582..812
FT /note="Plasmin light chain B"
FT /id="PRO_0000028074"
FT DOMAIN 20..98
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 103..181
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 184..262
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 275..352
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 377..454
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 481..560
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 582..810
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 624
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 667
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 762
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT DISULFID 49..73
FT /evidence="ECO:0000250"
FT DISULFID 53..61
FT /evidence="ECO:0000250"
FT DISULFID 103..181
FT /evidence="ECO:0000250"
FT DISULFID 124..164
FT /evidence="ECO:0000250"
FT DISULFID 152..176
FT /evidence="ECO:0000250"
FT DISULFID 185..262
FT /evidence="ECO:0000250"
FT DISULFID 188..316
FT /evidence="ECO:0000250"
FT DISULFID 206..245
FT /evidence="ECO:0000250"
FT DISULFID 234..257
FT /evidence="ECO:0000250"
FT DISULFID 275..352
FT /evidence="ECO:0000250"
FT DISULFID 296..335
FT /evidence="ECO:0000250"
FT DISULFID 324..347
FT /evidence="ECO:0000250"
FT DISULFID 377..454
FT /evidence="ECO:0000250"
FT DISULFID 398..437
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 481..560
FT /evidence="ECO:0000250"
FT DISULFID 502..543
FT /evidence="ECO:0000250"
FT DISULFID 531..555
FT /evidence="ECO:0000250"
FT DISULFID 568..687
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 578..586
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 609..625
FT /evidence="ECO:0000250"
FT DISULFID 701..768
FT /evidence="ECO:0000250"
FT DISULFID 731..747
FT /evidence="ECO:0000250"
FT DISULFID 758..786
FT /evidence="ECO:0000250"
FT CONFLICT 235
FT /note="R -> H (in Ref. 1; AAA50168)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="G -> D (in Ref. 1; AAA50168)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="L -> S (in Ref. 2; AAM22156 and 4; AAH14773/
FT AAH57186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 90808 MW; E70E1AC8E52844E9 CRC64;
MDHKEVILLF LLLLKPGQGD SLDGYISTQG ASLFSLTKKQ LAAGGVSDCL AKCEGETDFV
CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL SECKTGIGNG YRGTMSRTKS
GVACQKWGAT FPHVPNYSPS THPNEGLEEN YCRNPDNDEQ GPWCYTTDPD KRYDYCNIPE
CEEECMYCSG EKYEGKISKT MSGLDCQAWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE
PRPWCFTTDP TKRWEYCDIP RCTTPPPPPS PTYQCLKGRG ENYRGTVSVT VSGKTCQRWS
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP SCESSASPDQ
SDSSVPPEEQ TPVVQECYQS DGQSYRGTSS TTITGKKCQS WAAMFPHRHS KTPENFPDAG
LEMNYCRNPD GDKGPWCYTT DPSVRWEYCN LKRCSETGGS VVELPTVSQE PSGPSDSETD
CMYGNGKDYR GKTAVTAAGT PCQGWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDVNG
PWCYTTNPRK LYDYCDIPLC ASASSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR
TRFTGQHFCG GTLIAPEWVL TAAHCLEKSS RPEFYKVILG AHEEYIRGLD VQEISVAKLI
LEPNNRDIAL LKLSRPATIT DKVIPACLPS PNYMVADRTI CYITGWGETQ GTFGAGRLKE
AQLPVIENKV CNRVEYLNNR VKSTELCAGQ LAGGVDSCQG DSGGPLVCFE KDKYILQGVT
SWGLGCARPN KPGVYVRVSR FVDWIEREMR NN
