ID   PLMN_CAPHI              Reviewed;         123 AA.
AC   Q7M323;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Plasminogen;
DE            EC=3.4.21.7;
DE   Flags: Fragment;
GN   Name=PLG;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3168975; DOI=10.1159/000469147;
RA   Schaller J., Rickli E.E.;
RT   "Structural aspects of the plasminogen of various species.";
RL   Enzyme 40:63-69(1988).
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   -!- 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 (By similarity). {ECO:0000250}.
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: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   -!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin
CC       immediately after dissociation from the clot. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC       {ECO:0000305}.
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DR   PIR; C61545; C61545.
DR   AlphaFoldDB; Q7M323; -.
DR   SMR; Q7M323; -.
DR   STRING; 9925.ENSCHIP00000007843; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR   CDD; cd00108; KR; 1.
DR   Gene3D; 2.40.20.10; -; 1.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   Pfam; PF00051; Kringle; 1.
DR   SMART; SM00130; KR; 1.
DR   SUPFAM; SSF57440; SSF57440; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW   Hemostasis; Hydrolase; Kringle; Protease; Reference proteome; Secreted;
KW   Serine protease; Tissue remodeling; Zymogen.
FT   CHAIN           <1..>123
FT                   /note="Plasminogen"
FT                   /id="PRO_0000088703"
FT   DOMAIN          40..118
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        41..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        62..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DISULFID        90..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   NON_TER         1
FT   NON_TER         123
SQ   SEQUENCE   123 AA;  13908 MW;  E53432C4DA0AC07C CRC64;
     DLLDDYVNTQ GASLLTLSRK KLAGRSVEDC AAKCEEEAQD CYHGNGQSYR GTSSTTVTGR
     KCQSWSSMIP HRHQKTPESY PNAGLTMNYC RNPDADKSPW CYTTDPRVRW EFCNLKKCSE
     DSE