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Protein

Plasminogen

Gene

Plg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

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

  • endopeptidase activity Source: RGD
  • serine-type endopeptidase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-171052. LDL-mediated lipid transport.
R-RNO-186797. Signaling by PDGF.
R-RNO-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-RNO-75205. Dissolution of Fibrin Clot.

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Plg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi619893. 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

  • extracellular region Source: UniProtKB-SubCell
  • extrinsic component of plasma membrane Source: Ensembl
  • intracellular membrane-bounded organelle Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3204.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 812793PlasminogenPRO_0000028079Add
BLAST
Chaini20 – 581562Plasmin heavy chain APRO_0000028080Add
BLAST
Peptidei20 – 9778Activation peptideBy similarityPRO_0000028081Add
BLAST
Chaini98 – 581484Plasmin heavy chain A, short formPRO_0000028082Add
BLAST
Chaini98 – ?436339AngiostatinPRO_0000028083Add
BLAST
Chaini582 – 812231Plasmin light chain BPRO_0000028084Add
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 bondi376 ↔ 454By similarity
Disulfide bondi397 ↔ 437By similarity
Disulfide bondi425 ↔ 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
Modified residuei690 – 6901PhosphoserineBy 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

PaxDbiQ01177.
PRIDEiQ01177.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017223.
ExpressionAtlasiQ01177. baseline and differential.
GenevisibleiQ01177. RN.

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

BioGridi250057. 1 interaction.
STRINGi10116.ENSRNOP00000023370.

Chemistry

BindingDBiQ01177.

Structurei

3D structure databases

ProteinModelPortaliQ01177.
SMRiQ01177. Positions 565-812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879PANPROSITE-ProRule annotationAdd
BLAST
Domaini102 – 18180Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 26279Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 35279Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini375 – 45480Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini480 – 56081Kringle 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

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiQ01177.
KOiK01315.
OMAiFPNKNLK.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ01177.
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.

Q01177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHKEIILLF LLFLKPGQGD SLDGYVSTQG ASLHSLTKKQ LAAGSIADCL
60 70 80 90 100
AKCEGETDFI CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL
110 120 130 140 150
SECKTGIGKG YRGTMSKTKT GVTCQKWSDT SPHVPKYSPS THPSEGLEEN
160 170 180 190 200
YCRNPDNDEQ GPWCYTTDPD QRYEYCNIPE CEEECMYCSG EKYEGKISKT
210 220 230 240 250
MSGLDCQSWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE PRPWCFTTDP
260 270 280 290 300
NKRWEYCDIP RCTTPPPPPG PTYQCLKGRG ENYRGTVSVT ASGKTCQRWS
310 320 330 340 350
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP
360 370 380 390 400
SCGSSVSPDQ SDSSVLPEQT PVVQECYQGN GKSYRGTSST TNTGKKCQSW
410 420 430 440 450
VSMTPHSHSK TPANFPDAGL EMNYCRNPDN DQRGPWCFTT DPSVRWEYCN
460 470 480 490 500
LKRCSETGGG VAESAIVPQV PSAPGTSETD CMYGNGKEYR GKTAVTAAGT
510 520 530 540 550
PCQEWAAQEP HSHRIFTPQT NPRAGLEKNY CRNPDGDVNG PWCYTMNPRK
560 570 580 590 600
LYDYCNIPLC ASLSSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR
610 620 630 640 650
TRFSGQHFCG GTLISPEWVL TAAHCLEKSS RPEFYKVILG AHEERILGSD
660 670 680 690 700
VQQIAVTKLV LEPNDADIAL LKLSRPATIT DNVIPACLPS PNYVVADRTL
710 720 730 740 750
CYITGWGETK GTPGAGRLKE AQLPVIENKV CNRAEYLNNR VKSTELCAGH
760 770 780 790 800
LAGGIDSCQG DSGGPLVCFE KDKYILQGVT SWGLGCARPN KPGVYVRVSR
810
YVNWIEREMR ND
Length:812
Mass (Da):90,536
Last modified:August 31, 2004 - v2
Checksum:i8C703C51410EBC9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti418 – 4181A → S in AAA41884 (PubMed:1645711).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242649 mRNA. Translation: CAB46014.1.
BC091135 mRNA. Translation: AAH91135.1.
M62832 mRNA. Translation: AAA41884.1.
PIRiA40522.
RefSeqiNP_445943.1. NM_053491.2.
UniGeneiRn.20178.

Genome annotation databases

EnsembliENSRNOT00000023368; ENSRNOP00000023370; ENSRNOG00000017223.
GeneIDi85253.
KEGGirno:85253.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242649 mRNA. Translation: CAB46014.1.
BC091135 mRNA. Translation: AAH91135.1.
M62832 mRNA. Translation: AAA41884.1.
PIRiA40522.
RefSeqiNP_445943.1. NM_053491.2.
UniGeneiRn.20178.

3D structure databases

ProteinModelPortaliQ01177.
SMRiQ01177. Positions 565-812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250057. 1 interaction.
STRINGi10116.ENSRNOP00000023370.

Chemistry

BindingDBiQ01177.
ChEMBLiCHEMBL3204.

Protein family/group databases

MEROPSiS01.233.

Proteomic databases

PaxDbiQ01177.
PRIDEiQ01177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023368; ENSRNOP00000023370; ENSRNOG00000017223.
GeneIDi85253.
KEGGirno:85253.

Organism-specific databases

CTDi5340.
RGDi619893. Plg.

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiQ01177.
KOiK01315.
OMAiFPNKNLK.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ01177.
TreeFamiTF329901.

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-171052. LDL-mediated lipid transport.
R-RNO-186797. Signaling by PDGF.
R-RNO-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-RNO-75205. Dissolution of Fibrin Clot.

Miscellaneous databases

PROiQ01177.

Gene expression databases

BgeeiENSRNOG00000017223.
ExpressionAtlasiQ01177. baseline and differential.
GenevisibleiQ01177. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q01177
Secondary accession number(s): Q5BKB6, Q9R0W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: August 31, 2004
Last modified: September 7, 2016
This is version 146 of the entry and version 2 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 (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.