ID PLMN_RAT Reviewed; 812 AA.
AC Q01177; Q5BKB6; Q9R0W3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 27-MAR-2024, entry version 187.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Bangert K., Johnsen A.H., Thorsen S.;
RT "Rat plasminogen: cDNA and gene structure.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 343-511.
RC TISSUE=Liver;
RX PubMed=1645711; DOI=10.1016/s0021-9258(18)99093-9;
RA Kanalas J.J., Makker S.P.;
RT "Identification of the rat Heymann nephritis autoantigen (GP330) as a
RT receptor site for plasminogen.";
RL J. Biol. Chem. 266:10825-10829(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 -!- FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks
CC neovascularization and growth of experimental primary and metastatic
CC tumors in vivo. {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.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AJ242649; CAB46014.1; -; mRNA.
DR EMBL; BC091135; AAH91135.1; -; mRNA.
DR EMBL; M62832; AAA41884.1; -; mRNA.
DR PIR; A40522; A40522.
DR RefSeq; NP_445943.1; NM_053491.2.
DR AlphaFoldDB; Q01177; -.
DR SMR; Q01177; -.
DR BioGRID; 250057; 1.
DR IntAct; Q01177; 1.
DR STRING; 10116.ENSRNOP00000023370; -.
DR BindingDB; Q01177; -.
DR ChEMBL; CHEMBL3204; -.
DR DrugCentral; Q01177; -.
DR MEROPS; S01.233; -.
DR PhosphoSitePlus; Q01177; -.
DR SwissPalm; Q01177; -.
DR PaxDb; 10116-ENSRNOP00000023370; -.
DR Ensembl; ENSRNOT00000023368.6; ENSRNOP00000023370.3; ENSRNOG00000017223.8.
DR Ensembl; ENSRNOT00055048697; ENSRNOP00055040019; ENSRNOG00055027842.
DR Ensembl; ENSRNOT00060016838; ENSRNOP00060013160; ENSRNOG00060009885.
DR Ensembl; ENSRNOT00065050859; ENSRNOP00065041809; ENSRNOG00065029290.
DR GeneID; 85253; -.
DR KEGG; rno:85253; -.
DR AGR; RGD:619893; -.
DR CTD; 5340; -.
DR RGD; 619893; Plg.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR GeneTree; ENSGT00940000155208; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; Q01177; -.
DR OrthoDB; 211181at2759; -.
DR PhylomeDB; Q01177; -.
DR TreeFam; TF329901; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR Reactome; R-RNO-8964041; LDL remodeling.
DR PRO; PR:Q01177; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017223; Expressed in liver and 16 other cell types or tissues.
DR ExpressionAtlas; Q01177; baseline and differential.
DR Genevisible; Q01177; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:1990405; F:protein antigen binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0042730; P:fibrinolysis; ISO:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0071674; P:mononuclear cell migration; ISO:RGD.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; ISO:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:RGD.
DR GO; GO:0042246; P:tissue regeneration; ISO:RGD.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; ISO:RGD.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISO:RGD.
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 2: Evidence at transcript level;
KW Blood coagulation; Cleavage on pair of basic residues; Disulfide bond;
KW Fibrinolysis; Hemostasis; Hydrolase; Kringle; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Tissue remodeling; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..812
FT /note="Plasminogen"
FT /id="PRO_0000028079"
FT CHAIN 20..581
FT /note="Plasmin heavy chain A"
FT /id="PRO_0000028080"
FT PEPTIDE 20..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028081"
FT CHAIN 98..581
FT /note="Plasmin heavy chain A, short form"
FT /id="PRO_0000028082"
FT CHAIN 98..?436
FT /note="Angiostatin"
FT /id="PRO_0000028083"
FT CHAIN 582..812
FT /note="Plasmin light chain B"
FT /id="PRO_0000028084"
FT DOMAIN 20..98
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 102..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 274..352
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 375..454
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 480..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 376..454
FT /evidence="ECO:0000250"
FT DISULFID 397..437
FT /evidence="ECO:0000250"
FT DISULFID 425..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 418
FT /note="A -> S (in Ref. 3; AAA41884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 90536 MW; 8C703C51410EBC9E CRC64;
MDHKEIILLF LLFLKPGQGD SLDGYVSTQG ASLHSLTKKQ LAAGSIADCL AKCEGETDFI
CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL SECKTGIGKG YRGTMSKTKT
GVTCQKWSDT SPHVPKYSPS THPSEGLEEN YCRNPDNDEQ GPWCYTTDPD QRYEYCNIPE
CEEECMYCSG EKYEGKISKT MSGLDCQSWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE
PRPWCFTTDP NKRWEYCDIP RCTTPPPPPG PTYQCLKGRG ENYRGTVSVT ASGKTCQRWS
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP SCGSSVSPDQ
SDSSVLPEQT PVVQECYQGN GKSYRGTSST TNTGKKCQSW VSMTPHSHSK TPANFPDAGL
EMNYCRNPDN DQRGPWCFTT DPSVRWEYCN LKRCSETGGG VAESAIVPQV PSAPGTSETD
CMYGNGKEYR GKTAVTAAGT PCQEWAAQEP HSHRIFTPQT NPRAGLEKNY CRNPDGDVNG
PWCYTMNPRK LYDYCNIPLC ASLSSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR
TRFSGQHFCG GTLISPEWVL TAAHCLEKSS RPEFYKVILG AHEERILGSD VQQIAVTKLV
LEPNDADIAL LKLSRPATIT DNVIPACLPS PNYVVADRTL CYITGWGETK GTPGAGRLKE
AQLPVIENKV CNRAEYLNNR VKSTELCAGH LAGGIDSCQG DSGGPLVCFE KDKYILQGVT
SWGLGCARPN KPGVYVRVSR YVNWIEREMR ND
//
