Plasminogen precursor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P20918 (PLMN_MOUSE)

Last modified June 16, 2009. Version 110. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 5 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Activation peptide
    3- Recommended name:
            Angiostatin
    4- Recommended name:
            Plasmin heavy chain A, short form
    5- Recommended name:
            Plasmin light chain B

Gene names

Name:

Plg

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	812 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. 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 with CSPG4 and AMOT By similarity.
Subcellular location	Secreted.
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.

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Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis Tissue remodeling
Cellular component	Secreted
Domain	Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from direct assay. Source: MGI blood coagulation Inferred from sequence or structural similarity. Source: HGNC fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Inferred from direct assay. Source: MGI muscle maintenance Inferred from mutant phenotype. Source: MGI myoblast differentiation Inferred from mutant phenotype. Source: MGI negative regulation of angiogenesis Traceable author statement. Source: MGI tissue regeneration Inferred from mutant phenotype. Source: MGI tissue remodeling Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: HGNC
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from sequence or structural similarity. Source: HGNC serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Chain

20 – 812

793

Plasminogen

PRO_0000028069

Chain

20 – 581

562

Plasmin heavy chain A

PRO_0000028070

Peptide

20 – 97

Activation peptide

PRO_0000028071

Chain

98 – 581

484

Plasmin heavy chain A, short form

PRO_0000028072

Chain

98 – ?436

339

Angiostatin

PRO_0000028073

Chain

582 – 812

231

Plasmin light chain B

PRO_0000028074

Regions

Domain

20 – 98

PAN

Domain

103 – 181

Kringle 1

Domain

184 – 262

Kringle 2

Domain

275 – 352

Kringle 3

Domain

377 – 454

Kringle 4

Domain

481 – 560

Kringle 5

Domain

582 – 810

229

Peptidase S1

Sites

Active site

624

Charge relay system By similarity

Active site

667

Charge relay system By similarity

Active site

762

Charge relay system By similarity

Amino acid modifications

Disulfide bond

49 ↔ 73

By similarity

Disulfide bond

53 ↔ 61

By similarity

Disulfide bond

103 ↔ 181

By similarity

Disulfide bond

124 ↔ 164

By similarity

Disulfide bond

152 ↔ 176

By similarity

Disulfide bond

185 ↔ 262

By similarity

Disulfide bond

188 ↔ 316

By similarity

Disulfide bond

206 ↔ 245

By similarity

Disulfide bond

234 ↔ 257

By similarity

Disulfide bond

275 ↔ 352

By similarity

Disulfide bond

296 ↔ 335

By similarity

Disulfide bond

324 ↔ 347

By similarity

Disulfide bond

377 ↔ 454

By similarity

Disulfide bond

398 ↔ 437

By similarity

Disulfide bond

426 ↔ 449

By similarity

Disulfide bond

481 ↔ 560

By similarity

Disulfide bond

502 ↔ 543

By similarity

Disulfide bond

531 ↔ 555

By similarity

Disulfide bond

568 ↔ 687

Interchain (between A and B chains) By similarity

Disulfide bond

578 ↔ 586

Interchain (between A and B chains) By similarity

Disulfide bond

609 ↔ 625

By similarity

Disulfide bond

701 ↔ 768

By similarity

Disulfide bond

731 ↔ 747

By similarity

Disulfide bond

758 ↔ 786

By similarity

Experimental info

Sequence conflict

235

R → H in AAA50168. Ref.1

Sequence conflict

525

G → D in AAA50168. Ref.1

Sequence conflict

649

S → L in AAA50168. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P20918-1 [UniParc].

Last modified May 30, 2003. Version 2.
Checksum: 24173260E6A2FFD2
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FASTA

812

90,782

        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 AHEEYIRGSD 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

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References

	« Hide 'large scale' referencesShow '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: 2081600] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	"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: 12149246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Strain: 129/SvJ. Tissue: Liver.
[5]	"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: 7525077] [Abstract] Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	J04766 mRNA. Translation: AAA50168.1. AF481053 Genomic DNA. Translation: AAM22156.1. BC014773 mRNA. Translation: AAH14773.1. BC057186 mRNA. Translation: AAH57186.1. AY134430 Genomic DNA. Translation: AAN15805.1.
IPI	IPI00322936.
PIR	PLMS. A38514.
RefSeq	NP_032903.2.
UniGene	Mm.971
3D structure databases
HSSP	HSSP built from PDB template 1BUI based on UniProtKB P00747.
SMR	P20918. Positions 566-812.
ModBase	Search...
Protein family/group databases
MEROPS	S01.233.
PTM databases
PhosphoSite	P20918.
2-D gel databases
REPRODUCTION-2DPAGE	P20918.
Proteomic databases
PRIDE	P20918.
Genome annotation databases
Ensembl	ENSMUSG00000059481. Mus musculus. [Contig view]
GeneID	18815.
KEGG	mmu:18815.
Organism-specific databases
MGI	MGI:97620. Plg.
Phylogenomic databases
HOGENOM	P20918.
HOVERGEN	P20918.
Enzyme and pathway databases
BRENDA	3.4.21.7. 244.
Gene expression databases
Bgee	P20918.
CleanEx	MM_PLG.
GermOnline	ENSMUSG00000059481. Mus musculus.
Family and domain databases
InterPro	IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR003014. PAN-1_domain. IPR003609. Pan_app. IPR011358. Pept_S1A_Plasmin. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR003966. Peptidase_S1A_prothrombin. [Graphical view]
Pfam	PF00051. Kringle. 5 hits. PF00024. PAN_1. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001150. Plasmin. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00018. KRINGLE. PR01505. PROTHROMBIN.
ProDom	PD000395. Kringle. 5 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00130. KR. 5 hits. SM00473. PAN_AP. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
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. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	295166.
PMAP-CutDB	P20918.
SOURCE	Search...

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Entry information

Entry name

PLMN_MOUSE

Accession

Primary (citable) accession number: P20918
Secondary accession number(s): Q8CIS2, Q91WJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 30, 2003
Last modified:	June 16, 2009
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents