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P20918 (PLMN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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

Catalytic activity

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

Enzyme regulation

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

Subunit structure

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.

Subcellular location

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.

Domain

Kringle domains mediate interaction with CSPG4 By similarity.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 5 kringle domains.

Contains 1 PAN domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Hemostasis
Tissue remodeling
   Cellular componentSecreted
   DomainKringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Phosphoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from sequence or structural similarity. Source: HGNC

extracellular matrix disassembly

Inferred from electronic annotation. Source: Ensembl

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

labyrinthine layer blood vessel development

Inferred from mutant phenotype PubMed 12900459. Source: MGI

mononuclear cell migration

Inferred from mutant phenotype PubMed 17690254. Source: MGI

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 11929773. Source: MGI

myoblast differentiation

Inferred from mutant phenotype PubMed 11929773. Source: MGI

negative regulation of angiogenesis

Traceable author statement PubMed 12167431. Source: MGI

negative regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibrinolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibrinolysis

Inferred from electronic annotation. Source: Ensembl

proteolysis involved in cellular protein catabolic process

Inferred from electronic annotation. Source: Ensembl

tissue regeneration

Inferred from mutant phenotype PubMed 11929773. Source: MGI

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

trophoblast giant cell differentiation

Inferred from mutant phenotype PubMed 12900459. Source: MGI

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from sequence or structural similarity. Source: HGNC

extrinsic component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extrinsic component of plasma membrane

Inferred from direct assay PubMed 17690254. Source: MGI

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 812793Plasminogen
PRO_0000028069
Chain20 – 581562Plasmin heavy chain A
PRO_0000028070
Peptide20 – 9778Activation peptide
PRO_0000028071
Chain98 – 581484Plasmin heavy chain A, short form
PRO_0000028072
Chain98 – ?436339Angiostatin
PRO_0000028073
Chain582 – 812231Plasmin light chain B
PRO_0000028074

Regions

Domain20 – 9879PAN
Domain103 – 18179Kringle 1
Domain184 – 26279Kringle 2
Domain275 – 35278Kringle 3
Domain377 – 45478Kringle 4
Domain481 – 56080Kringle 5
Domain582 – 810229Peptidase S1

Sites

Active site6241Charge relay system By similarity
Active site6671Charge relay system By similarity
Active site7621Charge relay system By similarity

Amino acid modifications

Modified residue5981Phosphoserine By similarity
Disulfide bond49 ↔ 73 By similarity
Disulfide bond53 ↔ 61 By similarity
Disulfide bond103 ↔ 181 By similarity
Disulfide bond124 ↔ 164 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond185 ↔ 262 By similarity
Disulfide bond188 ↔ 316 By similarity
Disulfide bond206 ↔ 245 By similarity
Disulfide bond234 ↔ 257 By similarity
Disulfide bond275 ↔ 352 By similarity
Disulfide bond296 ↔ 335 By similarity
Disulfide bond324 ↔ 347 By similarity
Disulfide bond377 ↔ 454 By similarity
Disulfide bond398 ↔ 437 By similarity
Disulfide bond426 ↔ 449 By similarity
Disulfide bond481 ↔ 560 By similarity
Disulfide bond502 ↔ 543 By similarity
Disulfide bond531 ↔ 555 By similarity
Disulfide bond568 ↔ 687Interchain (between A and B chains) By similarity
Disulfide bond578 ↔ 586Interchain (between A and B chains) By similarity
Disulfide bond609 ↔ 625 By similarity
Disulfide bond701 ↔ 768 By similarity
Disulfide bond731 ↔ 747 By similarity
Disulfide bond758 ↔ 786 By similarity

Experimental info

Sequence conflict2351R → H in AAA50168. Ref.1
Sequence conflict5251G → D in AAA50168. Ref.1
Sequence conflict6491L → S in AAM22156. Ref.2
Sequence conflict6491L → S in AAH14773. Ref.4
Sequence conflict6491L → S in AAH57186. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P20918 [UniParc].

Last modified June 28, 2011. Version 3.
Checksum: E70E1AC8E52844E9

FASTA81290,808
        10         20         30         40         50         60 
MDHKEVILLF LLLLKPGQGD SLDGYISTQG ASLFSLTKKQ LAAGGVSDCL AKCEGETDFV 

        70         80         90        100        110        120 
CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL SECKTGIGNG YRGTMSRTKS 

       130        140        150        160        170        180 
GVACQKWGAT FPHVPNYSPS THPNEGLEEN YCRNPDNDEQ GPWCYTTDPD KRYDYCNIPE 

       190        200        210        220        230        240 
CEEECMYCSG EKYEGKISKT MSGLDCQAWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTTDP TKRWEYCDIP RCTTPPPPPS PTYQCLKGRG ENYRGTVSVT VSGKTCQRWS 

       310        320        330        340        350        360 
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP SCESSASPDQ 

       370        380        390        400        410        420 
SDSSVPPEEQ TPVVQECYQS DGQSYRGTSS TTITGKKCQS WAAMFPHRHS KTPENFPDAG 

       430        440        450        460        470        480 
LEMNYCRNPD GDKGPWCYTT DPSVRWEYCN LKRCSETGGS VVELPTVSQE PSGPSDSETD 

       490        500        510        520        530        540 
CMYGNGKDYR GKTAVTAAGT PCQGWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDVNG 

       550        560        570        580        590        600 
PWCYTTNPRK LYDYCDIPLC ASASSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR 

       610        620        630        640        650        660 
TRFTGQHFCG GTLIAPEWVL TAAHCLEKSS RPEFYKVILG AHEEYIRGLD VQEISVAKLI 

       670        680        690        700        710        720 
LEPNNRDIAL LKLSRPATIT DKVIPACLPS PNYMVADRTI CYITGWGETQ GTFGAGRLKE 

       730        740        750        760        770        780 
AQLPVIENKV CNRVEYLNNR VKSTELCAGQ LAGGVDSCQG DSGGPLVCFE KDKYILQGVT 

       790        800        810 
SWGLGCARPN KPGVYVRVSR FVDWIEREMR NN 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPLMS. A38514.
RefSeqNP_032903.3. NM_008877.3.
UniGeneMm.971.

3D structure databases

ProteinModelPortalP20918.
SMRP20918. Positions 20-812.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP20918. 4 interactions.
MINTMINT-4107912.

Chemistry

ChEMBLCHEMBL1075299.

Protein family/group databases

MEROPSS01.233.

PTM databases

PhosphoSiteP20918.

2D gel databases

REPRODUCTION-2DPAGEP20918.

Proteomic databases

PaxDbP20918.
PRIDEP20918.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000014578; ENSMUSP00000014578; ENSMUSG00000059481.
GeneID18815.
KEGGmmu:18815.
UCSCuc008akt.2. mouse.

Organism-specific databases

CTD5340.
MGIMGI:97620. Plg.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00740000115022.
HOGENOMHOG000112892.
HOVERGENHBG004381.
InParanoidP20918.
KOK01315.
OMAEGLEENY.
OrthoDBEOG75B84T.
TreeFamTF329901.

Gene expression databases

BgeeP20918.
CleanExMM_PLG.
GenevestigatorP20918.

Family and domain databases

Gene3D2.40.20.10. 5 hits.
InterProIPR000001. 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]
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEPS00021. 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]
ProtoNetSearch...

Other

ChiTaRSPLG. mouse.
NextBio295166.
PMAP-CutDBP20918.
PROP20918.
SOURCESearch...

Entry information

Entry namePLMN_MOUSE
AccessionPrimary (citable) accession number: P20918
Secondary accession number(s): Q8CIS2, Q91WJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 28, 2011
Last modified: April 16, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot