PLMN_HORSE
ID PLMN_HORSE Reviewed; 338 AA.
AC P80010;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Plasminogen;
DE EC=3.4.21.7;
DE Contains:
DE RecName: Full=Plasmin heavy chain A;
DE Contains:
DE RecName: Full=Plasmin light chain B;
DE Flags: Fragment;
GN Name=PLG;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Plasma;
RX PubMed=1946332;
RA Schaller J., Straub C., Kaempfer U., Rickli E.E.;
RT "Complete amino acid sequence of equine miniplasminogen.";
RL Protein Seq. Data Anal. 4:69-74(1991).
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. Activated
CC with catalytic amounts of streptokinase.
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.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; A61545; A61545.
DR AlphaFoldDB; P80010; -.
DR SMR; P80010; -.
DR STRING; 9796.ENSECAP00000034982; -.
DR MEROPS; S01.233; -.
DR PaxDb; P80010; -.
DR PeptideAtlas; P80010; -.
DR PRIDE; P80010; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; P80010; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 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; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 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; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW Hemostasis; Hydrolase; Kringle; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Serine protease; Tissue remodeling; Zymogen.
FT CHAIN <1..108
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028051"
FT CHAIN 109..338
FT /note="Plasmin light chain B"
FT /id="PRO_0000028052"
FT DOMAIN 9..88
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 109..336
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 191
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 269
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 282
FT /note="Site of substrate specificity"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT DISULFID 9..88
FT /evidence="ECO:0000250"
FT DISULFID 30..71
FT /evidence="ECO:0000250"
FT DISULFID 59..83
FT /evidence="ECO:0000250"
FT DISULFID 95..213
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 105..113
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 135..151
FT /evidence="ECO:0000250"
FT DISULFID 227..294
FT /evidence="ECO:0000250"
FT DISULFID 257..273
FT /evidence="ECO:0000250"
FT DISULFID 284..312
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 338 AA; 37132 MW; 8E9E56B5C5CDBE01 CRC64;
VQEPSEPDCM LGIGKGYQGK KATTVTGTRC QAWAAQEPHR HSIFTPEANP WANLEKNYCR
NPDGDVNGPW CYTMNPQKLF DYCDVPQCES SPFDCGKPKV EPKKCSGRIV GGCVAIAHSW
PWQISLRTRF GRHFCGGTLI SPEWVLTAAH CLERSSRPST YKVVLGTHHE LRLAAGAQQI
DVSKLFLEPS RADIALLKLS SPAIITQNVI PACLPPADYV VANWAECFVT GWGETQDSSN
AGVLKEAQLP VIENKVCNRY EYLNGRVKST ELCAGHLVGG VDSCQGDSGG PLVCFEKDKY
ILQGVTSWGL GCARPNKPGV YVRVSSFINW IERIMQSN
