Plasminogen precursor - Sus scrofa (Pig)

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P06867 (PLMN_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 121. 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

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	809 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, 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.

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 – 19

Ref.2

Chain

20 – 809

790

Plasminogen

PRO_0000285882

Chain

20 – 579

560

Plasmin heavy chain A

PRO_0000028075

Peptide

20 – 97

Activation peptide By similarity

PRO_0000028076

Chain

98 – 579

482

Plasmin heavy chain A, short form

PRO_0000028077

Chain

580 – 809

230

Plasmin light chain B

PRO_0000028078

Regions

Domain

20 – 98

PAN

Domain

103 – 181

Kringle 1

Domain

185 – 262

Kringle 2

Domain

275 – 352

Kringle 3

Domain

377 – 454

Kringle 4

Domain

480 – 559

Kringle 5

Domain

580 – 807

228

Peptidase S1

Sites

Active site

621

Charge relay system

Active site

664

Charge relay system

Active site

759

Charge relay system

Amino acid modifications

Modified residue

596

Phosphoserine By similarity

Glycosylation

308

N-linked (GlcNAc...) Ref.4

CAR_000019

Glycosylation

359

O-linked (GalNAc...) Ref.4

CAR_000020

Disulfide bond

49 ↔ 73

By similarity

Disulfide bond

53 ↔ 61

By similarity

Disulfide bond

103 ↔ 181

By similarity

Disulfide bond

124 ↔ 164

By similarity

Disulfide bond

152 ↔ 176

By similarity

Disulfide bond

185 ↔ 262

By similarity

Disulfide bond

188 ↔ 316

By similarity

Disulfide bond

206 ↔ 245

By similarity

Disulfide bond

234 ↔ 257

By similarity

Disulfide bond

275 ↔ 352

By similarity

Disulfide bond

296 ↔ 335

By similarity

Disulfide bond

324 ↔ 347

By similarity

Disulfide bond

377 ↔ 454

By similarity

Disulfide bond

398 ↔ 437

By similarity

Disulfide bond

426 ↔ 449

By similarity

Disulfide bond

480 ↔ 559

By similarity

Disulfide bond

501 ↔ 542

By similarity

Disulfide bond

530 ↔ 554

By similarity

Disulfide bond

566 ↔ 684

Interchain (between A and B chains) By similarity

Disulfide bond

576 ↔ 584

Interchain (between A and B chains) By similarity

Disulfide bond

606 ↔ 622

By similarity

Disulfide bond

698 ↔ 765

By similarity

Disulfide bond

728 ↔ 744

By similarity

Disulfide bond

755 ↔ 783

By similarity

Experimental info

Sequence conflict

361

Y → H AA sequence Ref.2

Sequence conflict

599

H → Y AA sequence Ref.3

Sequence conflict

602

G → R AA sequence Ref.3

Sequence conflict

675

I → V AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P06867 [UniParc].

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

FASTA

809

90,615

        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

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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] [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-359, STRUCTURE OF CARBOHYDRATES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ530369 mRNA. Translation: ABF82358.1.
PIR	PLPG. S03733.
RefSeq	NP_001038055.1. NM_001044590.2.
UniGene	Ssc.65489.
3D structure databases
ProteinModelPortal	P06867.
SMR	P06867. Positions 100-352, 376-458, 479-559, 563-809.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000004364.
Protein family/group databases
MEROPS	S01.233.
PTM databases
GlycoSuiteDB	P06867.
Proteomic databases
PaxDb	P06867.
PRIDE	P06867.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	733660.
KEGG	ssc:733660.
Organism-specific databases
CTD	5340.
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000112892.
HOVERGEN	HBG004381.
KO	K01315.
OrthoDB	EOG4RR6GQ.
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. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLMN_PIG

Accession

Primary (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:	April 3, 2013
This is version 121 of the entry and version 3 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

Family and domain databases

Entry information

Relevant documents