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Reviewed, UniProtKB/Swiss-Prot P06868 (PLMN_BOVIN)

Last modified June 16, 2009. Version 94. 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

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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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 and sialic acid. 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-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.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 812786Plasminogen
PRO_0000028039
Chain27 – 583557Plasmin heavy chain A
PRO_0000028040
Peptide27 – 10478Activation peptide By similarity
PRO_0000028041
Chain105 – 583479Plasmin heavy chain A, short form By similarity
PRO_0000028042
Chain584 – 812229Plasmin light chain B
PRO_0000028043

Regions

Domain29 – 10577PAN
Domain110 – 18879Kringle 1
Domain192 – 26978Kringle 2
Domain282 – 35978Kringle 3
Domain384 – 46178Kringle 4
Domain485 – 56480Kringle 5
Domain584 – 810227Peptidase S1

Sites

Active site6241Charge relay system
Active site6671Charge relay system
Active site7621Charge relay system

Amino acid modifications

Glycosylation3151N-linked (GlcNAc...) Ref.2
CAR_000014
Glycosylation3651O-linked (GalNAc...) Ref.2
CAR_000015
Disulfide bond56 ↔ 80 By similarity
Disulfide bond60 ↔ 68 By similarity
Disulfide bond110 ↔ 188 By similarity
Disulfide bond131 ↔ 171 By similarity
Disulfide bond159 ↔ 183 By similarity
Disulfide bond192 ↔ 269 By similarity
Disulfide bond195 ↔ 323 By similarity
Disulfide bond213 ↔ 252 By similarity
Disulfide bond241 ↔ 264 By similarity
Disulfide bond282 ↔ 359 By similarity
Disulfide bond303 ↔ 342 By similarity
Disulfide bond331 ↔ 354 By similarity
Disulfide bond384 ↔ 461 By similarity
Disulfide bond405 ↔ 444 By similarity
Disulfide bond433 ↔ 456 By similarity
Disulfide bond485 ↔ 564 By similarity
Disulfide bond506 ↔ 547 By similarity
Disulfide bond535 ↔ 559 By similarity
Disulfide bond570 ↔ 687Interchain (between A and B chains) By similarity
Disulfide bond580 ↔ 588Interchain (between A and B chains) By similarity
Disulfide bond609 ↔ 625 By similarity
Disulfide bond701 ↔ 768 By similarity
Disulfide bond731 ↔ 747 By similarity
Disulfide bond758 ↔ 786 By similarity

Experimental info

Sequence conflict3351N → D AA sequence Ref.2
Sequence conflict5161Q → H AA sequence Ref.2
Sequence conflict5551P → L AA sequence Ref.2
Sequence conflict7441T → R in AAA30714. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P06868-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 38A6AA691E220946

FASTA81291,216
        10         20         30         40         50         60 
MLPASPKMEH KAVVFLLLLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG RSVEDCAAKC 

        70         80         90        100        110        120 
EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL YEKRIYLLEC KTGNGQTYRG 

       130        140        150        160        170        180 
TTAETKSGVT CQKWSATSPH VPKFSPEKFP LAGLEENYCR NPDNDENGPW CYTTDPDKRY 

       190        200        210        220        230        240 
DYCDIPECED KCMHCSGENY EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPNKNLKMNY 

       250        260        270        280        290        300 
CRNPDGEPRP WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG 

       310        320        330        340        350        360 
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSEVR WEYCTIPSCE 

       370        380        390        400        410        420 
SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI TGRKCQSWSS MTPHRHLKTP 

       430        440        450        460        470        480 
ENYPNAGLTM NYCRNPDADK SPWCYTTDPR VRWEFCNLKK CSETPEQVPA APQAPGVENP 

       490        500        510        520        530        540 
PEADCMIGTG KSYRGKKATT VAGVPCQEWA AQEPHQHSIF TPETNPQSGL ERNYCRNPDG 

       550        560        570        580        590        600 
DVNGPWCYTM NPRKPFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS 

       610        620        630        640        650        660 
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS VQEIPVSRLF 

       670        680        690        700        710        720 
REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE CYITGWGETQ GTFGEGLLKE 

       730        740        750        760        770        780 
AHLPVIENKV CNRNEYLDGR VKPTELCAGH LIGGTDSCQG DSGGPLVCFE KDKYILQGVT 

       790        800        810 
SWGLGCARPN KPGVYVRVSP YVPWIEETMR RN

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References

[1]"Cloning and characterization of the bovine plasminogen cDNA."
Berglund L., Andersen M.D., Petersen T.E.
Int. Dairy J. 5:593-603(1995) [Agricola: IND20546772]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Complete amino acid sequence of bovine plasminogen. Comparison with human plasminogen."
Schaller J., Moser P.W., Dannegger-Muller G.A.K., Rosselet S.J., Kampfer U., Rickli E.E.
Eur. J. Biochem. 149:267-278(1985) [PubMed: 3846532] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-812, GLYCOSYLATION AT ASN-315 AND SER-365.
[3]"Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen."
Malinowski D.P., Sadler J.E., Davie E.W.
Biochemistry 23:4243-4250(1984) [PubMed: 6148961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 706-812.
[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: STRUCTURE OF CARBOHYDRATES.

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Cross-references

Sequence databases

X79402 mRNA. Translation: CAA55939.1.
K02935 mRNA. Translation: AAA30714.1.
IPIIPI00692205.
PIRPLBO. S45046.
RefSeqNP_776376.1.
UniGeneBt.306

3D structure databases

HSSPHSSP built from PDB template 2PK4 based on UniProtKB P00747.
SMRP06868. Positions 568-812.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

PTM databases

GlycoSuiteDBP06868.

Genome annotation databases

EnsemblENSBTAG00000001271. Bos taurus. [Contig view]
GeneID280897.
KEGGbta:280897.

Phylogenomic databases

HOVERGENP06868.

Enzyme and pathway databases

BRENDA3.4.21.7. 251.

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

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Entry information

Entry namePLMN_BOVIN
AccessionPrimary (citable) accession number: P06868
Secondary accession number(s): Q28162
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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