PLMN_CANLF
ID PLMN_CANLF Reviewed; 333 AA.
AC P80009;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Plasma;
RX PubMed=2626424;
RA Schaller J., Straub C., Kaempfer U., Rickli E.E.;
RT "Complete amino acid sequence of canine miniplasminogen.";
RL Protein Seq. Data Anal. 2:445-450(1989).
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 urokinase and high concentrations 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P80009; -.
DR SMR; P80009; -.
DR STRING; 9612.ENSCAFP00000001078; -.
DR MEROPS; S01.233; -.
DR PaxDb; P80009; -.
DR PRIDE; P80009; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR InParanoid; P80009; -.
DR Proteomes; UP000002254; 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..103
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028044"
FT CHAIN 104..333
FT /note="Plasmin light chain B"
FT /id="PRO_0000028045"
FT DOMAIN 4..83
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 104..331
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 152
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 186
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 264
FT /note="Interaction with streptokinase"
FT /evidence="ECO:0000305"
FT SITE 277
FT /note="Site of substrate specificity"
FT /evidence="ECO:0000250"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00747"
FT DISULFID 4..83
FT /evidence="ECO:0000250"
FT DISULFID 25..66
FT /evidence="ECO:0000250"
FT DISULFID 54..78
FT /evidence="ECO:0000250"
FT DISULFID 90..208
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 100..108
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 130..146
FT /evidence="ECO:0000250"
FT DISULFID 222..289
FT /evidence="ECO:0000250"
FT DISULFID 252..268
FT /evidence="ECO:0000250"
FT DISULFID 279..307
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 333 AA; 36678 MW; C8C0271B6C6AC8D4 CRC64;
ASDCMFGNGK GYRGKKATTV MGIPCQEWAA QEPHRHSIFT PETNPQAGLE KNYCRNPDGD
VNGPWCYTMN QRKLFDYCDV PQCVSTSFDC GKPQVEPKKC PGRVVGGCVA NPHSWPWQIS
LRTRYGKHFC GGTLISPEWV LTAAHCLERS SRPASYKVIL GAHKEVNLES DVQEIEVYKL
FLEPTRADIA LLKLSSPAVI TSKVIPACLP PPNYVVADRT LCYITGWGET QGTYGAGLLK
EAQLPVIENK VCNRYEYLNG RVKSTELCAG NLAGGTDSCQ GDSGGPLVCF EKDKYILQGV
TSWGLGCARP NKPGVYVRVS RFVTWIEGIM RNN
