Plasminogen precursor - Bos taurus (Bovine)

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P06868 (PLMN_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Plasminogen
EC=3.4.21.7

Gene names

Name:

PLG

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	812 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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, 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.
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 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation By similarity.
Subcellular location	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.
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.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis Hemostasis Tissue remodeling
Cellular component	Secreted
Domain	Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW tissue remodeling Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.2

Chain

27 – 812

786

Plasminogen

PRO_0000028039

Chain

27 – 583

557

Plasmin heavy chain A

PRO_0000028040

Peptide

27 – 104

Activation peptide By similarity

PRO_0000028041

Chain

105 – 583

479

Plasmin heavy chain A, short form By similarity

PRO_0000028042

Chain

584 – 812

229

Plasmin light chain B

PRO_0000028043

Regions

Domain

29 – 105

PAN

Domain

110 – 188

Kringle 1

Domain

192 – 269

Kringle 2

Domain

282 – 359

Kringle 3

Domain

384 – 461

Kringle 4

Domain

485 – 564

Kringle 5

Domain

584 – 810

227

Peptidase S1

Sites

Active site

624

Charge relay system

Active site

667

Charge relay system

Active site

762

Charge relay system

Amino acid modifications

Modified residue

600

Phosphoserine By similarity

Glycosylation

315

N-linked (GlcNAc...) Ref.2

CAR_000014

Glycosylation

365

O-linked (GalNAc...) Ref.2

CAR_000015

Disulfide bond

56 ↔ 80

By similarity

Disulfide bond

60 ↔ 68

By similarity

Disulfide bond

110 ↔ 188

By similarity

Disulfide bond

131 ↔ 171

By similarity

Disulfide bond

159 ↔ 183

By similarity

Disulfide bond

192 ↔ 269

By similarity

Disulfide bond

195 ↔ 323

By similarity

Disulfide bond

213 ↔ 252

By similarity

Disulfide bond

241 ↔ 264

By similarity

Disulfide bond

282 ↔ 359

By similarity

Disulfide bond

303 ↔ 342

By similarity

Disulfide bond

331 ↔ 354

By similarity

Disulfide bond

384 ↔ 461

By similarity

Disulfide bond

405 ↔ 444

By similarity

Disulfide bond

433 ↔ 456

By similarity

Disulfide bond

485 ↔ 564

By similarity

Disulfide bond

506 ↔ 547

By similarity

Disulfide bond

535 ↔ 559

By similarity

Disulfide bond

570 ↔ 687

Interchain (between A and B chains) By similarity

Disulfide bond

580 ↔ 588

Interchain (between A and B chains) By similarity

Disulfide bond

609 ↔ 625

By similarity

Disulfide bond

701 ↔ 768

By similarity

Disulfide bond

731 ↔ 747

By similarity

Disulfide bond

758 ↔ 786

By similarity

Experimental info

Sequence conflict

335

N → D AA sequence Ref.2

Sequence conflict

516

Q → H AA sequence Ref.2

Sequence conflict

555

P → L AA sequence Ref.2

Sequence conflict

744

T → R in AAA30714. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P06868 [UniParc].

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

812

91,216

        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] [Europe PMC] 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79402 mRNA. Translation: CAA55939.1. K02935 mRNA. Translation: AAA30714.1.
IPI	IPI00692205.
PIR	PLBO. S45046.
RefSeq	NP_776376.1. NM_173951.2.
UniGene	Bt.306.
3D structure databases
ProteinModelPortal	P06868.
SMR	P06868. Positions 484-566, 568-812.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000049470.
Protein family/group databases
MEROPS	S01.233.
PTM databases
GlycoSuiteDB	P06868.
Proteomic databases
PaxDb	P06868.
PRIDE	P06868.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	280897.
KEGG	bta:280897.
Organism-specific databases
CTD	5340.
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000112892.
HOVERGEN	HBG004381.
InParanoid	P06868.
KO	K01315.
OrthoDB	EOG4RR6GQ.
Enzyme and pathway databases
BioCyc	CATTLE:280897-MONOMER.
Family and domain databases
Gene3D	2.40.20.10. 5 hits.
InterPro	IPR000001. Kringle. IPR013806. Kringle-like. IPR018056. Kringle_CS. IPR003014. PAN-1_domain. IPR003609. Pan_app. IPR023317. Pept_S1A_plasmin. IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00051. Kringle. 5 hits. PF00024. PAN_1. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001150. Plasmin. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00130. KR. 5 hits. SM00473. PAN_AP. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF57440. Kringle-like. 5 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS00021. 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]
ProtoNet	Search...
Other
BindingDB	P06868.
ChEMBL	CHEMBL2957.
NextBio	20805028.

Entry information

Entry name

PLMN_BOVIN

Accession

Primary (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:	May 29, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 4 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents