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Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B]

 PLMN_RAT                Reviewed;         812 AA.
Q01177; Q5BKB6; Q9R0W3;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
12-SEP-2018, entry version 159.
RecName: Full=Plasminogen;
EC=3.4.21.7;
Contains:
RecName: Full=Plasmin heavy chain A;
Contains:
RecName: Full=Activation peptide;
Contains:
RecName: Full=Angiostatin;
Contains:
RecName: Full=Plasmin heavy chain A, short form;
Contains:
RecName: Full=Plasmin light chain B;
Flags: Precursor;
Name=Plg;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Bangert K., Johnsen A.H., Thorsen S.;
"Rat plasminogen: cDNA and gene structure.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 343-511.
TISSUE=Liver;
PubMed=1645711;
Kanalas J.J., Makker S.P.;
"Identification of the rat Heymann nephritis autoantigen (GP330) as a
receptor site for plasminogen.";
J. Biol. Chem. 266:10825-10829(1991).
-!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as
a proteolytic factor in a variety of other processes including
embryonic development, tissue remodeling, tumor invasion, and
inflammation. In ovulation, weakens the walls of the Graafian
follicle. It activates the urokinase-type plasminogen activator,
collagenases and several complement zymogens, such as C1 and C5.
Cleavage of fibronectin and laminin leads to cell detachment and
apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand
factor. Its role in tissue remodeling and tumor invasion may be
modulated by CSPG4. Binds to cells (By similarity). {ECO:0000250}.
-!- FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks
neovascularization and growth of experimental primary and
metastatic tumors in vivo. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa;
higher selectivity than trypsin. Converts fibrin into soluble
products.
-!- ACTIVITY REGULATION: Converted into plasmin by plasminogen
activators, both plasminogen and its activator being bound to
fibrin. Cannot be activated with streptokinase.
-!- SUBUNIT: Interacts (both mature PLG and the angiostatin peptide)
with AMOT and CSPG4. Interacts (via the Kringle domains) with HRG;
the interaction tethers PLG to the cell surface and enhances its
activation. Interacts (via Kringle 4 domain) with ADA; the
interaction stimulates PLG activation when in complex with DPP4.
Angiostatin: Interacts with ATP5F1A; the interaction inhibits most
of the angiogenic effects of angiostatin.
{ECO:0000250|UniProtKB:P00747}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the
cell surface where it is proteolytically cleaved to produce the
active plasmin. Interaction with HRG tethers it to the cell
surface (By similarity). {ECO:0000250}.
-!- DOMAIN: Kringle domains mediate interaction with CSPG4.
{ECO:0000250}.
-!- PTM: In the presence of the inhibitor, the activation involves
only cleavage after Arg-581, yielding two chains held together by
two disulfide bonds. In the absence of the inhibitor, the
activation involves additionally the removal of the activation
peptide (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin
immediately after dissociation from the clot.
-!- MISCELLANEOUS: In the presence of the inhibitor, the activation
involves only cleavage after Arg-581, resulting in 2 chains held
together by 2 disulfide bonds. Without the inhibitor, the
activation involves also removal of the activation peptide (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; AJ242649; CAB46014.1; -; mRNA.
EMBL; BC091135; AAH91135.1; -; mRNA.
EMBL; M62832; AAA41884.1; -; mRNA.
PIR; A40522; A40522.
RefSeq; NP_445943.1; NM_053491.2.
UniGene; Rn.20178; -.
ProteinModelPortal; Q01177; -.
SMR; Q01177; -.
BioGrid; 250057; 1.
STRING; 10116.ENSRNOP00000023370; -.
BindingDB; Q01177; -.
ChEMBL; CHEMBL3204; -.
MEROPS; S01.233; -.
PaxDb; Q01177; -.
PRIDE; Q01177; -.
Ensembl; ENSRNOT00000023368; ENSRNOP00000023370; ENSRNOG00000017223.
GeneID; 85253; -.
KEGG; rno:85253; -.
CTD; 5340; -.
RGD; 619893; Plg.
eggNOG; ENOG410IDXR; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000112892; -.
HOVERGEN; HBG004381; -.
InParanoid; Q01177; -.
KO; K01315; -.
OMA; CEDECMH; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; Q01177; -.
TreeFam; TF329901; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-RNO-186797; Signaling by PDGF.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
Reactome; R-RNO-8964041; LDL remodeling.
PRO; PR:Q01177; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000017223; Expressed in 9 organ(s), highest expression level in liver.
ExpressionAtlas; Q01177; baseline and differential.
Genevisible; Q01177; RN.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
GO; GO:0071674; P:mononuclear cell migration; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:RGD.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
CDD; cd00108; KR; 5.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 4.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR003609; Pan_app.
InterPro; IPR023317; Pept_S1A_plasmin.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00051; Kringle; 5.
Pfam; PF00024; PAN_1; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001150; Plasmin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00130; KR; 5.
SMART; SM00473; PAN_AP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 5.
PROSITE; PS00021; KRINGLE_1; 5.
PROSITE; PS50070; KRINGLE_2; 5.
PROSITE; PS50948; PAN; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Blood coagulation; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Fibrinolysis; Hemostasis;
Hydrolase; Kringle; Phosphoprotein; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Tissue remodeling; Zymogen.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 812 Plasminogen.
/FTId=PRO_0000028079.
CHAIN 20 581 Plasmin heavy chain A.
/FTId=PRO_0000028080.
PEPTIDE 20 97 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028081.
CHAIN 98 581 Plasmin heavy chain A, short form.
/FTId=PRO_0000028082.
CHAIN 98 ?436 Angiostatin.
/FTId=PRO_0000028083.
CHAIN 582 812 Plasmin light chain B.
/FTId=PRO_0000028084.
DOMAIN 20 98 PAN. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 102 181 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 184 262 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 274 352 Kringle 3. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 375 454 Kringle 4. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 480 560 Kringle 5. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 582 810 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 624 624 Charge relay system. {ECO:0000250}.
ACT_SITE 667 667 Charge relay system. {ECO:0000250}.
ACT_SITE 762 762 Charge relay system. {ECO:0000250}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:P00747}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000250|UniProtKB:P00747}.
DISULFID 49 73 {ECO:0000250}.
DISULFID 53 61 {ECO:0000250}.
DISULFID 103 181 {ECO:0000250}.
DISULFID 124 164 {ECO:0000250}.
DISULFID 152 176 {ECO:0000250}.
DISULFID 185 262 {ECO:0000250}.
DISULFID 188 316 {ECO:0000250}.
DISULFID 206 245 {ECO:0000250}.
DISULFID 234 257 {ECO:0000250}.
DISULFID 275 352 {ECO:0000250}.
DISULFID 296 335 {ECO:0000250}.
DISULFID 324 347 {ECO:0000250}.
DISULFID 376 454 {ECO:0000250}.
DISULFID 397 437 {ECO:0000250}.
DISULFID 425 449 {ECO:0000250}.
DISULFID 481 560 {ECO:0000250}.
DISULFID 502 543 {ECO:0000250}.
DISULFID 531 555 {ECO:0000250}.
DISULFID 568 687 Interchain (between A and B chains).
{ECO:0000250}.
DISULFID 578 586 Interchain (between A and B chains).
{ECO:0000250}.
DISULFID 609 625 {ECO:0000250}.
DISULFID 701 768 {ECO:0000250}.
DISULFID 731 747 {ECO:0000250}.
DISULFID 758 786 {ECO:0000250}.
CONFLICT 418 418 A -> S (in Ref. 3; AAA41884).
{ECO:0000305}.
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


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