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Protein

Plasminogen

Gene

Plg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

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

Enzyme 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

  • blood coagulation Source: HGNC
  • extracellular matrix disassembly Source: MGI
  • fibrinolysis Source: UniProtKB-KW
  • labyrinthine layer blood vessel development Source: MGI
  • mononuclear cell migration Source: MGI
  • muscle cell cellular homeostasis Source: MGI
  • myoblast differentiation Source: MGI
  • negative regulation of angiogenesis Source: MGI
  • negative regulation of cell-substrate adhesion Source: MGI
  • negative regulation of fibrinolysis Source: MGI
  • positive regulation of fibrinolysis Source: MGI
  • proteolysis involved in cellular protein catabolic process Source: Ensembl
  • tissue regeneration Source: MGI
  • tissue remodeling Source: UniProtKB-KW
  • trophoblast giant cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood 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-171052. LDL-mediated lipid transport.
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.

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:97620. Plg.

Subcellular locationi

  • Secreted By similarity

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

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-2DPAGEP20918.

PTM databases

PhosphoSitePlusiP20918.
SwissPalmiP20918.

Miscellaneous databases

PMAP-CutDBP20918.

Expressioni

Gene expression databases

BgeeiENSMUSG00000059481.
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 ATP5A1; the interaction inhibits most of the angiogenic effects of angiostatin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP20918. 5 interactors.
MINTiMINT-4107912.
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
Contains 5 kringle domains.PROSITE-ProRule annotation
Contains 1 PAN domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP20918.
KOiK01315.
OMAiFPNKNLK.
OrthoDBiEOG091G0AH5.
TreeFamiTF329901.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001150. Plasmin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEiPS00021. 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.
[Graphical view]

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.

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

IntActiP20918. 5 interactors.
MINTiMINT-4107912.
STRINGi10090.ENSMUSP00000014578.

Chemistry databases

BindingDBiP20918.
ChEMBLiCHEMBL1075299.

Protein family/group databases

MEROPSiS01.233.

PTM databases

PhosphoSitePlusiP20918.
SwissPalmiP20918.

2D gel databases

REPRODUCTION-2DPAGEP20918.

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.
OMAiFPNKNLK.
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-171052. LDL-mediated lipid transport.
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.

Miscellaneous databases

PMAP-CutDBP20918.
PROiP20918.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000059481.
CleanExiMM_PLG.
GenevisibleiP20918. MM.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001150. Plasmin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEiPS00021. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLMN_MOUSE
AccessioniPrimary (citable) accession number: P20918
Secondary accession number(s): Q8CIS2, Q91WJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 28, 2011
Last modified: November 2, 2016
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.