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Protein

Plasminogen

Gene

PLG

Organism
Sus scrofa (Pig)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei621 – 6211Charge relay system
Active sitei664 – 6641Charge relay system
Active sitei759 – 7591Charge relay system

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

Enzyme and pathway databases

SABIO-RKP06867.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 809790PlasminogenPRO_0000285882Add
BLAST
Chaini20 – 579560Plasmin heavy chain APRO_0000028075Add
BLAST
Peptidei20 – 9778Activation peptideBy similarityPRO_0000028076Add
BLAST
Chaini98 – 579482Plasmin heavy chain A, short formPRO_0000028077Add
BLAST
Chaini580 – 809230Plasmin light chain BPRO_0000028078Add
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
Glycosylationi268 – 2681O-linked (GalNAc...)1 PublicationCAR_000020
Disulfide bondi275 ↔ 352By similarity
Disulfide bondi296 ↔ 335By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...)1 PublicationCAR_000019
Disulfide bondi324 ↔ 347By similarity
Disulfide bondi377 ↔ 454By similarity
Disulfide bondi398 ↔ 437By similarity
Disulfide bondi426 ↔ 449By similarity
Disulfide bondi480 ↔ 559By similarity
Disulfide bondi501 ↔ 542By similarity
Disulfide bondi530 ↔ 554By similarity
Disulfide bondi566 ↔ 684Interchain (between A and B chains)By similarity
Disulfide bondi576 ↔ 584Interchain (between A and B chains)By similarity
Modified residuei596 – 5961PhosphoserineBy similarity
Disulfide bondi606 ↔ 622By similarity
Disulfide bondi698 ↔ 765By similarity
Disulfide bondi728 ↔ 744By similarity
Disulfide bondi755 ↔ 783By similarity

Post-translational modificationi

N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity).1 Publication
In the presence of the inhibitor, the activation involves only cleavage after Arg-579, 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

PaxDbiP06867.
PeptideAtlasiP06867.
PRIDEiP06867.

PTM databases

UniCarbKBiP06867.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004364.

Structurei

3D structure databases

ProteinModelPortaliP06867.
SMRiP06867. Positions 100-352, 376-458, 479-559, 563-809.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879PANPROSITE-ProRule annotationAdd
BLAST
Domaini103 – 18179Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini185 – 26278Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 35278Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 45478Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini480 – 55980Kringle 5PROSITE-ProRule annotationAdd
BLAST
Domaini580 – 807228Peptidase 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.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP06867.
KOiK01315.

Family and domain databases

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.
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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHKEVVLLL LLFLKSGLGD SLDDYVNTQG AFLFSLSRKQ VAARSVEECA
60 70 80 90 100
AKCEAETNFI CRAFQYHSKD QQCVVMAENS KTSPIARMRD VVLFEKRIYL
110 120 130 140 150
SECKTGNGKN YRGTTSKTKS GVICQKWSVS SPHIPKYSPE KFPLAGLEEN
160 170 180 190 200
YCRNPDNDEK GPWCYTTDPE TRFDYCDIPE CEDECMHCSG EHYEGKISKT
210 220 230 240 250
MSGIECQSWG SQSPHAHGYL PSKFPNKNLK MNYCRNPDGE PRPWCFTTDP
260 270 280 290 300
NKRWEFCDIP RCTTPPPTSG PTYQCLKGRG ENYRGTVSVT ASGHTCQRWS
310 320 330 340 350
AQSPHKHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS EVRWDYCKIP
360 370 380 390 400
SCGSSTTSTE YLDAPVPPEQ TPVAQDCYRG NGESYRGTSS TTITGRKCQS
410 420 430 440 450
WVSMTPHRHE KTPGNFPNAG LTMNYCRNPD ADKSPWCYTT DPRVRWEYCN
460 470 480 490 500
LKKCSETEQQ VTNFPAIAQV PSVEDLSEDC MFGNGKRYRG KRATTVAGVP
510 520 530 540 550
CQEWAAQEPH RHSIFTPETN PRAGLEKNYC RNPDGDDNGP WCYTTNPQKL
560 570 580 590 600
FDYCDVPQCV TSSFDCGKPK VEPKKCPARV VGGCVSIPHS WPWQISLRHR
610 620 630 640 650
YGGHFCGGTL ISPEWVLTAK HCLEKSSSPS SYKVILGAHE EYHLGEGVQE
660 670 680 690 700
IDVSKLFKEP SEADIALLKL SSPAIITDKV IPACLPTPNY VVADRTACYI
710 720 730 740 750
TGWGETKGTY GAGLLKEARL PVIENKVCNR YEYLGGKVSP NELCAGHLAG
760 770 780 790 800
GIDSCQGDSG GPLVCFEKDK YILQGVTSWG LGCALPNKPG VYVRVSRFVT

WIEEIMRRN
Length:809
Mass (Da):90,615
Last modified:May 1, 2007 - v3
Checksum:i198261D2082A075D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti361 – 3611Y → H AA sequence (Ref. 2) Curated
Sequence conflicti599 – 5991H → Y AA sequence (PubMed:3846533).Curated
Sequence conflicti602 – 6021G → R AA sequence (PubMed:3846533).Curated
Sequence conflicti675 – 6751I → V AA sequence (PubMed:3846533).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ530369 mRNA. Translation: ABF82358.1.
PIRiS03733. PLPG.
RefSeqiNP_001038055.1. NM_001044590.2.
UniGeneiSsc.65489.

Genome annotation databases

GeneIDi733660.
KEGGissc:733660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ530369 mRNA. Translation: ABF82358.1.
PIRiS03733. PLPG.
RefSeqiNP_001038055.1. NM_001044590.2.
UniGeneiSsc.65489.

3D structure databases

ProteinModelPortaliP06867.
SMRiP06867. Positions 100-352, 376-458, 479-559, 563-809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004364.

Protein family/group databases

MEROPSiS01.233.

PTM databases

UniCarbKBiP06867.

Proteomic databases

PaxDbiP06867.
PeptideAtlasiP06867.
PRIDEiP06867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi733660.
KEGGissc:733660.

Organism-specific databases

CTDi5340.

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP06867.
KOiK01315.

Enzyme and pathway databases

SABIO-RKP06867.

Family and domain databases

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.
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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Chen Y., Tan W., Cheng J.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Amino acid sequence of the heavy chain of porcine plasmin. Comparison of the carbohydrate attachment sites with the human and bovine species."
    Schaller J., Marti T., Roesselet S.J., Kaempfer U., Rickli E.E.
    Fibrinolysis 1:91-102(1987)
    Cited for: PROTEIN SEQUENCE OF 20-579.
  3. "Determination of the complete amino-acid sequence of porcine miniplasminogen."
    Marti T., Schaller J., Rickli E.E.
    Eur. J. Biochem. 149:279-285(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 469-809.
  4. "The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns."
    Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., Vliegenthart J.F.G.
    Eur. J. Biochem. 173:57-63(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-308 AND THR-268, STRUCTURE OF CARBOHYDRATES.

Entry informationi

Entry nameiPLMN_PIG
AccessioniPrimary (citable) accession number: P06867
Secondary accession number(s): Q19AZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 1, 2007
Last modified: July 6, 2016
This is version 139 of the entry and version 3 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.