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Protein

Plasminogen

Gene

PLG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

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)DescriptionActionsGraphical viewLength
Active sitei624Charge relay system1
Active sitei667Charge relay system1
Active sitei762Charge relay system1

GO - Molecular functioni

  • protein domain specific binding Source: AgBase
  • receptor binding Source: AgBase
  • serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • fibrinolysis Source: UniProtKB-KW
  • response to heat Source: AgBase
  • tissue remodeling Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

SABIO-RKP06868.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000002803927 – 812PlasminogenAdd BLAST786
ChainiPRO_000002804027 – 583Plasmin heavy chain AAdd BLAST557
PeptideiPRO_000002804127 – 104Activation peptideBy similarityAdd BLAST78
ChainiPRO_0000028042105 – 583Plasmin heavy chain A, short formBy similarityAdd BLAST479
ChainiPRO_0000028043584 – 812Plasmin light chain BAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 80By similarity
Disulfide bondi60 ↔ 68By similarity
Disulfide bondi110 ↔ 188By similarity
Disulfide bondi131 ↔ 171By similarity
Disulfide bondi159 ↔ 183By similarity
Disulfide bondi192 ↔ 269By similarity
Disulfide bondi195 ↔ 323By similarity
Disulfide bondi213 ↔ 252By similarity
Disulfide bondi241 ↔ 264By similarity
Disulfide bondi282 ↔ 359By similarity
Disulfide bondi303 ↔ 342By similarity
GlycosylationiCAR_000014315N-linked (GlcNAc...)2 Publications1
Disulfide bondi331 ↔ 354By similarity
GlycosylationiCAR_000015365O-linked (GalNAc...)2 Publications1
Disulfide bondi384 ↔ 461By similarity
Disulfide bondi405 ↔ 444By similarity
Disulfide bondi433 ↔ 456By similarity
Disulfide bondi485 ↔ 564By similarity
Disulfide bondi506 ↔ 547By similarity
Disulfide bondi535 ↔ 559By similarity
Disulfide bondi570 ↔ 687Interchain (between A and B chains)By similarity
Disulfide bondi580 ↔ 588Interchain (between A and B chains)By similarity
Modified residuei600PhosphoserineBy similarity1
Disulfide bondi609 ↔ 625By similarity
Disulfide bondi701 ↔ 768By similarity
Disulfide bondi731 ↔ 747By similarity
Disulfide bondi758 ↔ 786By similarity

Post-translational modificationi

N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity).2 Publications
In the presence of the inhibitor, the activation involves only cleavage after Arg-583, 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, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP06868.
PeptideAtlasiP06868.
PRIDEiP06868.

PTM databases

UniCarbKBiP06868.

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

GO - Molecular functioni

  • protein domain specific binding Source: AgBase
  • receptor binding Source: AgBase

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001674.

Chemistry databases

BindingDBiP06868.

Structurei

3D structure databases

ProteinModelPortaliP06868.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 105PANPROSITE-ProRule annotationAdd BLAST77
Domaini110 – 188Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini192 – 269Kringle 2PROSITE-ProRule annotationAdd BLAST78
Domaini282 – 359Kringle 3PROSITE-ProRule annotationAdd BLAST78
Domaini384 – 461Kringle 4PROSITE-ProRule annotationAdd BLAST78
Domaini485 – 564Kringle 5PROSITE-ProRule annotationAdd BLAST80
Domaini584 – 810Peptidase S1PROSITE-ProRule annotationAdd BLAST227

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.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP06868.
KOiK01315.

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.

P06868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPASPKMEH KAVVFLLLLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG
60 70 80 90 100
RSVEDCAAKC EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL
110 120 130 140 150
YEKRIYLLEC KTGNGQTYRG TTAETKSGVT CQKWSATSPH VPKFSPEKFP
160 170 180 190 200
LAGLEENYCR NPDNDENGPW CYTTDPDKRY DYCDIPECED KCMHCSGENY
210 220 230 240 250
EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPNKNLKMNY CRNPDGEPRP
260 270 280 290 300
WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG
310 320 330 340 350
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSEVR
360 370 380 390 400
WEYCTIPSCE SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI
410 420 430 440 450
TGRKCQSWSS MTPHRHLKTP ENYPNAGLTM NYCRNPDADK SPWCYTTDPR
460 470 480 490 500
VRWEFCNLKK CSETPEQVPA APQAPGVENP PEADCMIGTG KSYRGKKATT
510 520 530 540 550
VAGVPCQEWA AQEPHQHSIF TPETNPQSGL ERNYCRNPDG DVNGPWCYTM
560 570 580 590 600
NPRKPFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS
610 620 630 640 650
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS
660 670 680 690 700
VQEIPVSRLF REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE
710 720 730 740 750
CYITGWGETQ GTFGEGLLKE AHLPVIENKV CNRNEYLDGR VKPTELCAGH
760 770 780 790 800
LIGGTDSCQG DSGGPLVCFE KDKYILQGVT SWGLGCARPN KPGVYVRVSP
810
YVPWIEETMR RN
Length:812
Mass (Da):91,216
Last modified:November 1, 1997 - v2
Checksum:i38A6AA691E220946
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti335N → D AA sequence (PubMed:3846532).Curated1
Sequence conflicti516Q → H AA sequence (PubMed:3846532).Curated1
Sequence conflicti555P → L AA sequence (PubMed:3846532).Curated1
Sequence conflicti744T → R in AAA30714 (PubMed:6148961).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79402 mRNA. Translation: CAA55939.1.
K02935 mRNA. Translation: AAA30714.1.
PIRiS45046. PLBO.
RefSeqiNP_776376.1. NM_173951.2.
UniGeneiBt.306.

Genome annotation databases

GeneIDi280897.
KEGGibta:280897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79402 mRNA. Translation: CAA55939.1.
K02935 mRNA. Translation: AAA30714.1.
PIRiS45046. PLBO.
RefSeqiNP_776376.1. NM_173951.2.
UniGeneiBt.306.

3D structure databases

ProteinModelPortaliP06868.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001674.

Chemistry databases

BindingDBiP06868.
ChEMBLiCHEMBL2957.

Protein family/group databases

MEROPSiS01.233.

PTM databases

UniCarbKBiP06868.

Proteomic databases

PaxDbiP06868.
PeptideAtlasiP06868.
PRIDEiP06868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280897.
KEGGibta:280897.

Organism-specific databases

CTDi5340.

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP06868.
KOiK01315.

Enzyme and pathway databases

SABIO-RKP06868.

Miscellaneous databases

PROiP06868.

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_BOVIN
AccessioniPrimary (citable) accession number: P06868
Secondary accession number(s): Q28162
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 150 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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.