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Protein

Plasminogen

Gene

PLG

Organism
Macropus eugenii (Tammar wallaby)
Status
Reviewed-Annotation score: Annotation score: 4 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

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. Activated with catalytic amounts of streptokinase (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei618Charge relay systemBy similarity1
Active sitei661Charge relay systemBy similarity1
Active sitei756Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasminogen (EC:3.4.21.7)
Cleaved into the following 4 chains:
Gene namesi
Name:PLG
OrganismiMacropus eugenii (Tammar wallaby)
Taxonomic identifieri9315 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDiprotodontiaMacropodidaeMacropus

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000002806420 – 806PlasminogenAdd BLAST787
ChainiPRO_000002806520 – 576Plasmin heavy chain ABy similarityAdd BLAST557
PeptideiPRO_000002806620 – 96Activation peptideBy similarityAdd BLAST77
ChainiPRO_000002806797 – 576Plasmin heavy chain A, short formBy similarityAdd BLAST480
ChainiPRO_0000028068577 – 806Plasmin light chain BBy similarityAdd BLAST230

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 bondi371 ↔ 448By similarity
Disulfide bondi392 ↔ 431By similarity
Disulfide bondi420 ↔ 443By similarity
Disulfide bondi476 ↔ 555By similarity
Disulfide bondi497 ↔ 538By similarity
Disulfide bondi526 ↔ 550By similarity
Disulfide bondi563 ↔ 681Interchain (between A and B chains)By similarity
Disulfide bondi573 ↔ 581Interchain (between A and B chains)By similarity
Modified residuei593PhosphoserineBy similarity1
Disulfide bondi603 ↔ 619By similarity
Modified residuei684PhosphoserineBy similarity1
Disulfide bondi695 ↔ 762By similarity
Disulfide bondi725 ↔ 741By similarity
Disulfide bondi752 ↔ 780By similarity

Post-translational modificationi

In the presence of the inhibitor, the activation involves only cleavage after Arg-576, 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

Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

PRIDEiO18783.

Interactioni

Subunit structurei

Interacts with CSPG4 and AMOT. 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

Structurei

3D structure databases

ProteinModelPortaliO18783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 98PANPROSITE-ProRule annotationAdd BLAST79
Domaini102 – 181Kringle 1PROSITE-ProRule annotationAdd BLAST80
Domaini184 – 262Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini274 – 352Kringle 3PROSITE-ProRule annotationAdd BLAST79
Domaini370 – 448Kringle 4PROSITE-ProRule annotationAdd BLAST79
Domaini475 – 555Kringle 5PROSITE-ProRule annotationAdd BLAST81
Domaini577 – 804Peptidase S1PROSITE-ProRule annotationAdd BLAST228

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

HOVERGENiHBG004381.

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.

O18783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYGKVIFLF LLFLKSGQGE SLENYIKTEG ASLSNSQKKQ FVASSTEECE
60 70 80 90 100
ALCEKETEFV CRSFEHYNKE QKCVIMSENS KTSSVERKRD VVLFEKRIYL
110 120 130 140 150
SDCKSGNGRN YRGTLSKTKS GITCQKWSDL SPHVPNYAPS KYPDAGLEKN
160 170 180 190 200
YCRNPDDDVK GPWCYTTNPD IRYEYCDVPE CEDECMHCSG ENYRGTISKT
210 220 230 240 250
ESGIECQPWD SQEPHSHEYI PSKFPSKDLK ENYCRNPDGE PRPWCFTSNP
260 270 280 290 300
EKRWEFCNIP RCSSPPPPPG PMLQCLKGRG ENYRGKIAVT KSGHTCQRWN
310 320 330 340 350
KQTPHKHNRT PENFPCRGLD ENYCRNPDGE LEPWCYTTNP DVRQEYCAIP
360 370 380 390 400
SCGTSSPHTD RVEQSPVIQE CYEGKGENYR GTTSTTISGK KCQAWSSMTP
410 420 430 440 450
HQHKKTPDNF PNADLIRNYC RNPDGDKSPW CYTMDPTVRW EFCNLEKCSG
460 470 480 490 500
TGSTVLNAQT TRVPSVDTTS HPESDCMYGS GKDYRGKRST TVTGTLCQAW
510 520 530 540 550
TAQEPHRHTI FTPDTYPRAG LEENYCRNPD GDPNGPWCYT TNPKKLFDYC
560 570 580 590 600
DIPQCVSPSS FDCGKPRVEP QKCPGRIVGG CYAQPHSWPW QISLRTRFGE
610 620 630 640 650
HFCGGTLIAP QWVLTAAHCL ERSQWPGAYK VILGLHREVN PESYSQEIGV
660 670 680 690 700
SRLFKGPLAA DIALLKLNRP AAINDKVIPA CLPSQDFMVP DRTLCHVTGW
710 720 730 740 750
GDTQGTSPRG LLKQASLPVI DNRVCNRHEY LNGRVKSTEL CAGHLVGRGD
760 770 780 790 800
SCQGDSGGPL ICFEDDKYVL QGVTSWGLGC ARPNKPGVYV RVSRYISWIE

DVMKNN
Length:806
Mass (Da):90,981
Last modified:January 1, 1998 - v1
Checksum:i95FAA86DC20064D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012297 mRNA. Translation: AAB65760.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012297 mRNA. Translation: AAB65760.1.

3D structure databases

ProteinModelPortaliO18783.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.233.

Proteomic databases

PRIDEiO18783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004381.

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_MACEU
AccessioniPrimary (citable) accession number: O18783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 91 of the entry and version 1 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.By similarity
In the presence of the inhibitor, the activation involves only cleavage after Arg-576, 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

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.