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P20918

- PLMN_MOUSE

UniProt

P20918 - PLMN_MOUSE

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Protein

Plasminogen

Gene

Plg

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei624 – 6241Charge relay systemBy similarity
Active sitei667 – 6671Charge relay systemBy similarity
Active sitei762 – 7621Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: HGNC
  2. fibrinolysis Source: UniProtKB-KW
  3. labyrinthine layer blood vessel development Source: MGI
  4. mononuclear cell migration Source: MGI
  5. muscle cell cellular homeostasis Source: MGI
  6. myoblast differentiation Source: MGI
  7. negative regulation of angiogenesis Source: MGI
  8. proteolysis involved in cellular protein catabolic process Source: Ensembl
  9. tissue regeneration Source: MGI
  10. tissue remodeling Source: UniProtKB-KW
  11. 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

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_222614. LDL-mediated lipid transport.
REACT_235291. Dissolution of Fibrin Clot.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_263353. Signaling by PDGF.
REACT_268398. Orphan transporters.

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Plg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: 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

  1. extracellular region Source: Reactome
  2. extracellular space Source: HGNC
  3. extrinsic component of plasma membrane Source: MGI
  4. intracellular membrane-bounded organelle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 812793PlasminogenPRO_0000028069Add
BLAST
Chaini20 – 581562Plasmin heavy chain APRO_0000028070Add
BLAST
Peptidei20 – 9778Activation peptidePRO_0000028071Add
BLAST
Chaini98 – 581484Plasmin heavy chain A, short formPRO_0000028072Add
BLAST
Chaini98 – ?436339AngiostatinPRO_0000028073Add
BLAST
Chaini582 – 812231Plasmin light chain BPRO_0000028074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 residuei598 – 5981PhosphoserineBy similarity
Disulfide bondi609 ↔ 625By similarity
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.
PRIDEiP20918.

2D gel databases

REPRODUCTION-2DPAGEP20918.

PTM databases

PhosphoSiteiP20918.

Miscellaneous databases

PMAP-CutDBP20918.

Expressioni

Gene expression databases

BgeeiP20918.
CleanExiMM_PLG.
ExpressionAtlasiP20918. baseline.
GenevestigatoriP20918.

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 (the angiostatin peptide) with ATP5A1; the interaction inhibits most of the angiogenic effects of angiostatin (By similarity).By similarity

Protein-protein interaction databases

IntActiP20918. 4 interactions.
MINTiMINT-4107912.

Structurei

3D structure databases

ProteinModelPortaliP20918.
SMRiP20918. Positions 20-812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879PANPROSITE-ProRule annotationAdd
BLAST
Domaini103 – 18179Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 26279Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 35278Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 45478Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 56080Kringle 5PROSITE-ProRule annotationAdd
BLAST
Domaini582 – 810229Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP20918.
KOiK01315.
OMAiEGLEENY.
OrthoDBiEOG75B84T.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.40.20.10. 5 hits.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351R → H in AAA50168. (PubMed:2081600)Curated
Sequence conflicti525 – 5251G → D in AAA50168. (PubMed:2081600)Curated
Sequence conflicti649 – 6491L → S in AAM22156. 1 PublicationCurated
Sequence conflicti649 – 6491L → S in AAH14773. (PubMed:15489334)Curated
Sequence conflicti649 – 6491L → S in AAH57186. (PubMed:15489334)Curated

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 .
CCDSi CCDS28390.1.
PIRi A38514. PLMS.
RefSeqi NP_032903.3. NM_008877.3.
UniGenei Mm.971.

3D structure databases

ProteinModelPortali P20918.
SMRi P20918. Positions 20-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P20918. 4 interactions.
MINTi MINT-4107912.

Chemistry

BindingDBi P20918.
ChEMBLi CHEMBL1075299.

Protein family/group databases

MEROPSi S01.233.

PTM databases

PhosphoSitei P20918.

2D gel databases

REPRODUCTION-2DPAGE P20918.

Proteomic databases

MaxQBi P20918.
PaxDbi P20918.
PRIDEi P20918.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000014578 ; ENSMUSP00000014578 ; ENSMUSG00000059481 .
GeneIDi 18815.
KEGGi mmu:18815.
UCSCi uc008akt.2. mouse.

Organism-specific databases

CTDi 5340.
MGIi MGI:97620. Plg.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000119133.
HOGENOMi HOG000112892.
HOVERGENi HBG004381.
InParanoidi P20918.
KOi K01315.
OMAi EGLEENY.
OrthoDBi EOG75B84T.
TreeFami TF329901.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_222614. LDL-mediated lipid transport.
REACT_235291. Dissolution of Fibrin Clot.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_263353. Signaling by PDGF.
REACT_268398. Orphan transporters.

Miscellaneous databases

NextBioi 295166.
PMAP-CutDB P20918.
PROi P20918.
SOURCEi Search...

Gene expression databases

Bgeei P20918.
CleanExi MM_PLG.
ExpressionAtlasi P20918. baseline.
Genevestigatori P20918.

Family and domain databases

Gene3Di 2.40.20.10. 5 hits.
InterProi IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001150. Plasmin. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the cDNA coding for mouse plasminogen and localization of the gene to mouse chromosome 17."
    Degen S.J., Bell S.M., Schaefer L.A., Elliott R.W.
    Genomics 8:49-61(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic sequence analysis in the mouse T-complex region."
    Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129/Sv.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  5. "Localization of regulatory elements mediating constitutive and cytokine-stimulated plasminogen gene expression."
    Bannach F.G., Gutierrez A., Fowler B.J., Bugge T.H., Degen J.L., Parmer R.J., Miles L.A.
    J. Biol. Chem. 277:38579-38588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    Strain: 129/SvJ.
    Tissue: Liver.
  6. "Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma."
    O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M., Lane W.S., Cao Y., Sage E.H., Folkman J.
    Cell 79:315-328(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.

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 26, 2014
This is version 167 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

External Data

Dasty 3