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Reviewed, UniProtKB/Swiss-Prot P06867 (PLMN_PIG)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 4 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Activation peptide
    3- Recommended name:
            Plasmin heavy chain A, short form
    4- Recommended name:
            Plasmin light chain B
Gene names
Name: PLG
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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.

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 By similarity.

Subcellular location

Secreted.

Domain

Kringle domains mediate interaction with CSPG4 By similarity.

Post-translational modification

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).

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.

Miscellaneous

Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 5 kringle domains.

Contains 1 PAN domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 809790Plasminogen
PRO_0000285882
Chain20 – 579560Plasmin heavy chain A
PRO_0000028075
Peptide20 – 9778Activation peptide By similarity
PRO_0000028076
Chain98 – 579482Plasmin heavy chain A, short form
PRO_0000028077
Chain580 – 809230Plasmin light chain B
PRO_0000028078

Regions

Domain20 – 9879PAN
Domain103 – 18179Kringle 1
Domain185 – 26278Kringle 2
Domain275 – 35278Kringle 3
Domain377 – 45478Kringle 4
Domain480 – 55980Kringle 5
Domain580 – 807228Peptidase S1

Sites

Active site6211Charge relay system
Active site6641Charge relay system
Active site7591Charge relay system

Amino acid modifications

Glycosylation3081N-linked (GlcNAc...) Ref.4
CAR_000019
Glycosylation3591O-linked (GalNAc...) Ref.4
CAR_000020
Disulfide bond49 ↔ 73 By similarity
Disulfide bond53 ↔ 61 By similarity
Disulfide bond103 ↔ 181 By similarity
Disulfide bond124 ↔ 164 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond185 ↔ 262 By similarity
Disulfide bond188 ↔ 316 By similarity
Disulfide bond206 ↔ 245 By similarity
Disulfide bond234 ↔ 257 By similarity
Disulfide bond275 ↔ 352 By similarity
Disulfide bond296 ↔ 335 By similarity
Disulfide bond324 ↔ 347 By similarity
Disulfide bond377 ↔ 454 By similarity
Disulfide bond398 ↔ 437 By similarity
Disulfide bond426 ↔ 449 By similarity
Disulfide bond480 ↔ 559 By similarity
Disulfide bond501 ↔ 542 By similarity
Disulfide bond530 ↔ 554 By similarity
Disulfide bond566 ↔ 684Interchain (between A and B chains) By similarity
Disulfide bond576 ↔ 584Interchain (between A and B chains) By similarity
Disulfide bond606 ↔ 622 By similarity
Disulfide bond698 ↔ 765 By similarity
Disulfide bond728 ↔ 744 By similarity
Disulfide bond755 ↔ 783 By similarity

Experimental info

Sequence conflict3611Y → H AA sequence Ref.2
Sequence conflict5991H → Y AA sequence Ref.3
Sequence conflict6021G → R AA sequence Ref.3
Sequence conflict6751I → V AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P06867-1 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 198261D2082A075D

FASTA80990,615
        10         20         30         40         50         60 
MDHKEVVLLL LLFLKSGLGD SLDDYVNTQG AFLFSLSRKQ VAARSVEECA AKCEAETNFI 

        70         80         90        100        110        120 
CRAFQYHSKD QQCVVMAENS KTSPIARMRD VVLFEKRIYL SECKTGNGKN YRGTTSKTKS 

       130        140        150        160        170        180 
GVICQKWSVS SPHIPKYSPE KFPLAGLEEN YCRNPDNDEK GPWCYTTDPE TRFDYCDIPE 

       190        200        210        220        230        240 
CEDECMHCSG EHYEGKISKT MSGIECQSWG SQSPHAHGYL PSKFPNKNLK MNYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTTDP NKRWEFCDIP RCTTPPPTSG PTYQCLKGRG ENYRGTVSVT ASGHTCQRWS 

       310        320        330        340        350        360 
AQSPHKHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS EVRWDYCKIP SCGSSTTSTE 

       370        380        390        400        410        420 
YLDAPVPPEQ TPVAQDCYRG NGESYRGTSS TTITGRKCQS WVSMTPHRHE KTPGNFPNAG 

       430        440        450        460        470        480 
LTMNYCRNPD ADKSPWCYTT DPRVRWEYCN LKKCSETEQQ VTNFPAIAQV PSVEDLSEDC 

       490        500        510        520        530        540 
MFGNGKRYRG KRATTVAGVP CQEWAAQEPH RHSIFTPETN PRAGLEKNYC RNPDGDDNGP 

       550        560        570        580        590        600 
WCYTTNPQKL FDYCDVPQCV TSSFDCGKPK VEPKKCPARV VGGCVSIPHS WPWQISLRHR 

       610        620        630        640        650        660 
YGGHFCGGTL ISPEWVLTAK HCLEKSSSPS SYKVILGAHE EYHLGEGVQE IDVSKLFKEP 

       670        680        690        700        710        720 
SEADIALLKL SSPAIITDKV IPACLPTPNY VVADRTACYI TGWGETKGTY GAGLLKEARL 

       730        740        750        760        770        780 
PVIENKVCNR YEYLGGKVSP NELCAGHLAG GIDSCQGDSG GPLVCFEKDK YILQGVTSWG 

       790        800 
LGCALPNKPG VYVRVSRFVT WIEEIMRRN 

« Hide

References

[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: 3846533] [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: 3356193] [Abstract]
Cited for: GLYCOSYLATION AT ASN-308 AND THR-359, STRUCTURE OF CARBOHYDRATES.

Cross-references

Sequence databases

DQ530369 mRNA. Translation: ABF82358.1.
PIRPLPG. S03733.
RefSeqNP_001038055.1.
UniGeneSsc.55956

3D structure databases

HSSPHSSP built from PDB template 1BUI based on UniProtKB P00747.
SMRP06867. Positions 563-809.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

PTM databases

GlycoSuiteDBP06867.

Genome annotation databases

GeneID733660.
KEGGssc:733660.

Phylogenomic databases

HOVERGENP06867.

Enzyme and pathway databases

BRENDA3.4.21.7. 249.

Family and domain databases

InterProIPR000001. 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]
Gene3DG3DSA:2.40.20.10. Kringle. 5 hits.
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.
ProDomPD000395. Kringle. 5 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00021. KRINGLE_1. 5 hits.
PS50070. KRINGLE_2. 5 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. False negative.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMN_PIG
AccessionPrimary (citable) accession number: P06867
Secondary accession number(s): Q19AZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 1, 2007
Last modified: June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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) · Sequences · References · Cross-references · Entry information · Relevant documents