ID E1B726_BOVIN Unreviewed; 812 AA.
AC E1B726;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043, ECO:0000256|PIRNR:PIRNR001150};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184, ECO:0000256|PIRNR:PIRNR001150};
GN Name=PLG {ECO:0000313|Ensembl:ENSBTAP00000001674.5};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000001674.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000001674.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001674.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000001674.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001674.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00025229, ECO:0000256|PIRNR:PIRNR001150}.
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; Evidence={ECO:0000256|ARBA:ARBA00000717,
CC ECO:0000256|PIRNR:PIRNR001150};
CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators,
CC both plasminogen and its activator being bound to fibrin.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SUBUNIT: Interacts with CSPG4 and AMOT. Interacts (via the Kringle
CC domains) with HRG; the interaction tethers PLG to the cell surface and
CC enhances its activation. Interacts (via Kringle 4 domain) with ADA; the
CC interaction stimulates PLG activation when in complex with DPP4.
CC Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of
CC the angiogenic effects of angiostatin. {ECO:0000256|ARBA:ARBA00038571}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; E1B726; -.
DR SMR; E1B726; -.
DR Ensembl; ENSBTAT00000001674.6; ENSBTAP00000001674.5; ENSBTAG00000001271.6.
DR VEuPathDB; HostDB:ENSBTAG00000001271; -.
DR GeneTree; ENSGT00940000155208; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; E1B726; -.
DR OMA; NSQTPHA; -.
DR TreeFam; TF329901; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-BTA-186797; Signaling by PDGF.
DR Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
DR Reactome; R-BTA-8964041; LDL remodeling.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000001271; Expressed in liver and 43 other cell types or tissues.
DR ExpressionAtlas; E1B726; baseline.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0071674; P:mononuclear cell migration; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
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:0043536; P:positive regulation of blood vessel endothelial cell migration; 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:0042246; P:tissue regeneration; IEA:Ensembl.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-UniRule.
DR GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR CDD; cd00108; KR; 5.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 PANTHER; PTHR24261:SF13; PLASMINOGEN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
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 PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 5.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Fibrinolysis {ECO:0000256|ARBA:ARBA00023281,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR001150};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001150, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|PIRNR:PIRNR001150, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Secreted {ECO:0000256|PIRNR:PIRNR001150};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001150,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148,
KW ECO:0000256|PIRNR:PIRNR001150}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..812
FT /note="Plasminogen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003143688"
FT DOMAIN 29..105
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 109..188
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 191..269
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 281..359
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 383..461
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 484..564
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 584..810
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 624
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 667
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 762
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 165
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 179
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 439
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 452
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 192..269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 213..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 241..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 282..359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 303..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 331..354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 384..461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 405..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 433..456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 812 AA; 91243 MW; E6EB24FC98CDB7CB CRC64;
MLPASPKMEH KAVVFLILLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG RSVEDCAAKC
EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL YEKRIYLLEC KTGNGQTYRG
TTAETKSGVT CQKWSATSPH VPKFSPEKFP LAGLEENYCR NPDNDENGPW CYTTDPDKRY
DYCDIPECED KCMHCSGENY EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPSKNLKMNY
CRNPDGEPRP WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSKVR WEYCTIPSCE
SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI TGRKCQSWSS MTPHRHLKTP
ENYPNAGLTM NYCRNPDADK SPWCYTTDPR VRWEFCNLKK CSETPEQVPA APQAPGVENP
PEADCMIGMG KSYRGKKATT VAGVPCQEWA AQEPHHHSIF TPETNPQSGL ERNYCRNPDG
DVNGPWCYTM NPRKLFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS VQEIPVSRLF
REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE CYITGWGETQ GTFGEGLLKE
AHLPVIENKV CNRNEYLDGR VKPTELCAGH LIGGTDSCQG DSGGPLVCFE KDKYILQGVT
SWGLGCARPN KPGVYVRVSP YVPWIEETMR RN
//
