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Protein

Plasminogen

Gene

Plg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity
Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.

Miscellaneous

Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
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.

Catalytic activityi

Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.

Activity regulationi

Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei624Charge relay systemBy similarity1
Active sitei667Charge relay systemBy similarity1
Active sitei762Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1592389 Activation of Matrix Metalloproteinases
R-MMU-186797 Signaling by PDGF
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-75205 Dissolution of Fibrin Clot
R-MMU-8964041 LDL remodeling

Protein family/group databases

MEROPSiS01.233

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Plg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:97620 Plg

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075299

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
ChainiPRO_000002806920 – 812PlasminogenAdd BLAST793
ChainiPRO_000002807020 – 581Plasmin heavy chain AAdd BLAST562
PeptideiPRO_000002807120 – 97Activation peptideAdd BLAST78
ChainiPRO_000002807298 – 581Plasmin heavy chain A, short formAdd BLAST484
ChainiPRO_000002807398 – ?436AngiostatinAdd BLAST339
ChainiPRO_0000028074582 – 812Plasmin light chain BAdd BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 73By similarity
Disulfide bondi53 ↔ 61By similarity
Disulfide bondi103 ↔ 181By similarity
Disulfide bondi124 ↔ 164By similarity
Disulfide bondi152 ↔ 176By similarity
Disulfide bondi185 ↔ 262By similarity
Disulfide bondi188 ↔ 316By similarity
Disulfide bondi206 ↔ 245By similarity
Disulfide bondi234 ↔ 257By similarity
Disulfide bondi275 ↔ 352By similarity
Disulfide bondi296 ↔ 335By similarity
Disulfide bondi324 ↔ 347By similarity
Disulfide bondi377 ↔ 454By similarity
Disulfide bondi398 ↔ 437By similarity
Disulfide bondi426 ↔ 449By similarity
Disulfide bondi481 ↔ 560By similarity
Disulfide bondi502 ↔ 543By similarity
Disulfide bondi531 ↔ 555By similarity
Disulfide bondi568 ↔ 687Interchain (between A and B chains)By similarity
Disulfide bondi578 ↔ 586Interchain (between A and B chains)By similarity
Modified residuei598PhosphoserineBy similarity1
Disulfide bondi609 ↔ 625By similarity
Modified residuei690PhosphoserineBy similarity1
Disulfide bondi701 ↔ 768By similarity
Disulfide bondi731 ↔ 747By similarity
Disulfide bondi758 ↔ 786By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP20918
PaxDbiP20918
PeptideAtlasiP20918
PRIDEiP20918

2D gel databases

REPRODUCTION-2DPAGEiP20918

PTM databases

iPTMnetiP20918
PhosphoSitePlusiP20918
SwissPalmiP20918

Miscellaneous databases

PMAP-CutDBiP20918

Expressioni

Gene expression databases

BgeeiENSMUSG00000059481 Expressed in 67 organ(s), highest expression level in liver
CleanExiMM_PLG
GenevisibleiP20918 MM

Interactioni

Subunit structurei

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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUMiP20918
IntActiP20918, 5 interactors
MINTiP20918
STRINGi10090.ENSMUSP00000014578

Chemistry databases

BindingDBiP20918

Structurei

3D structure databases

ProteinModelPortaliP20918
SMRiP20918
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 98PANPROSITE-ProRule annotationAdd BLAST79
Domaini103 – 181Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini184 – 262Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini275 – 352Kringle 3PROSITE-ProRule annotationAdd BLAST78
Domaini377 – 454Kringle 4PROSITE-ProRule annotationAdd BLAST78
Domaini481 – 560Kringle 5PROSITE-ProRule annotationAdd BLAST80
Domaini582 – 810Peptidase S1PROSITE-ProRule annotationAdd BLAST229

Domaini

Kringle domains mediate interaction with CSPG4.By similarity

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IDXR Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000119133
HOGENOMiHOG000112892
HOVERGENiHBG004381
InParanoidiP20918
KOiK01315
OMAiCEDECMH
OrthoDBiEOG091G0AH5
TreeFamiTF329901

Family and domain databases

CDDicd00108 KR, 5 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 4 hits
InterProiView protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR003609 Pan_app
IPR023317 Pept_S1A_plasmin
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00051 Kringle, 5 hits
PF00024 PAN_1, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001150 Plasmin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00130 KR, 5 hits
SM00473 PAN_AP, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 5 hits
PROSITEiView protein in PROSITE
PS00021 KRINGLE_1, 5 hits
PS50070 KRINGLE_2, 5 hits
PS50948 PAN, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20918-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDHKEVILLF LLLLKPGQGD SLDGYISTQG ASLFSLTKKQ LAAGGVSDCL
60 70 80 90 100
AKCEGETDFV CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL
110 120 130 140 150
SECKTGIGNG YRGTMSRTKS GVACQKWGAT FPHVPNYSPS THPNEGLEEN
160 170 180 190 200
YCRNPDNDEQ GPWCYTTDPD KRYDYCNIPE CEEECMYCSG EKYEGKISKT
210 220 230 240 250
MSGLDCQAWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE PRPWCFTTDP
260 270 280 290 300
TKRWEYCDIP RCTTPPPPPS PTYQCLKGRG ENYRGTVSVT VSGKTCQRWS
310 320 330 340 350
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP
360 370 380 390 400
SCESSASPDQ SDSSVPPEEQ TPVVQECYQS DGQSYRGTSS TTITGKKCQS
410 420 430 440 450
WAAMFPHRHS KTPENFPDAG LEMNYCRNPD GDKGPWCYTT DPSVRWEYCN
460 470 480 490 500
LKRCSETGGS VVELPTVSQE PSGPSDSETD CMYGNGKDYR GKTAVTAAGT
510 520 530 540 550
PCQGWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDVNG PWCYTTNPRK
560 570 580 590 600
LYDYCDIPLC ASASSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR
610 620 630 640 650
TRFTGQHFCG GTLIAPEWVL TAAHCLEKSS RPEFYKVILG AHEEYIRGLD
660 670 680 690 700
VQEISVAKLI LEPNNRDIAL LKLSRPATIT DKVIPACLPS PNYMVADRTI
710 720 730 740 750
CYITGWGETQ GTFGAGRLKE AQLPVIENKV CNRVEYLNNR VKSTELCAGQ
760 770 780 790 800
LAGGVDSCQG DSGGPLVCFE KDKYILQGVT SWGLGCARPN KPGVYVRVSR
810
FVDWIEREMR NN
Length:812
Mass (Da):90,808
Last modified:June 28, 2011 - v3
Checksum:iE70E1AC8E52844E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti235R → H in AAA50168 (PubMed:2081600).Curated1
Sequence conflicti525G → D in AAA50168 (PubMed:2081600).Curated1
Sequence conflicti649L → S in AAM22156 (Ref. 2) Curated1
Sequence conflicti649L → S in AAH14773 (PubMed:15489334).Curated1
Sequence conflicti649L → S in AAH57186 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04766 mRNA Translation: AAA50168.1
AF481053 Genomic DNA Translation: AAM22156.1
AC087901 Genomic DNA No translation available.
BC014773 mRNA Translation: AAH14773.1
BC057186 mRNA Translation: AAH57186.1
AY134430 Genomic DNA Translation: AAN15805.1
CCDSiCCDS28390.1
PIRiA38514 PLMS
RefSeqiNP_032903.3, NM_008877.3
UniGeneiMm.971

Genome annotation databases

EnsembliENSMUST00000014578; ENSMUSP00000014578; ENSMUSG00000059481
GeneIDi18815
KEGGimmu:18815
UCSCiuc008akt.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04766 mRNA Translation: AAA50168.1
AF481053 Genomic DNA Translation: AAM22156.1
AC087901 Genomic DNA No translation available.
BC014773 mRNA Translation: AAH14773.1
BC057186 mRNA Translation: AAH57186.1
AY134430 Genomic DNA Translation: AAN15805.1
CCDSiCCDS28390.1
PIRiA38514 PLMS
RefSeqiNP_032903.3, NM_008877.3
UniGeneiMm.971

3D structure databases

ProteinModelPortaliP20918
SMRiP20918
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP20918
IntActiP20918, 5 interactors
MINTiP20918
STRINGi10090.ENSMUSP00000014578

Chemistry databases

BindingDBiP20918
ChEMBLiCHEMBL1075299

Protein family/group databases

MEROPSiS01.233

PTM databases

iPTMnetiP20918
PhosphoSitePlusiP20918
SwissPalmiP20918

2D gel databases

REPRODUCTION-2DPAGEiP20918

Proteomic databases

MaxQBiP20918
PaxDbiP20918
PeptideAtlasiP20918
PRIDEiP20918

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014578; ENSMUSP00000014578; ENSMUSG00000059481
GeneIDi18815
KEGGimmu:18815
UCSCiuc008akt.2 mouse

Organism-specific databases

CTDi5340
MGIiMGI:97620 Plg

Phylogenomic databases

eggNOGiENOG410IDXR Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000119133
HOGENOMiHOG000112892
HOVERGENiHBG004381
InParanoidiP20918
KOiK01315
OMAiCEDECMH
OrthoDBiEOG091G0AH5
TreeFamiTF329901

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1592389 Activation of Matrix Metalloproteinases
R-MMU-186797 Signaling by PDGF
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-75205 Dissolution of Fibrin Clot
R-MMU-8964041 LDL remodeling

Miscellaneous databases

ChiTaRSiPlg mouse
PMAP-CutDBiP20918
PROiPR:P20918
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000059481 Expressed in 67 organ(s), highest expression level in liver
CleanExiMM_PLG
GenevisibleiP20918 MM

Family and domain databases

CDDicd00108 KR, 5 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 4 hits
InterProiView protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR003609 Pan_app
IPR023317 Pept_S1A_plasmin
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00051 Kringle, 5 hits
PF00024 PAN_1, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001150 Plasmin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00130 KR, 5 hits
SM00473 PAN_AP, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 5 hits
PROSITEiView protein in PROSITE
PS00021 KRINGLE_1, 5 hits
PS50070 KRINGLE_2, 5 hits
PS50948 PAN, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPLMN_MOUSE
AccessioniPrimary (citable) accession number: P20918
Secondary accession number(s): Q8CIS2, Q91WJ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 28, 2011
Last modified: September 12, 2018
This is version 198 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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