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Reviewed, UniProtKB/Swiss-Prot O18783 (PLMN_MACEU)

Last modified June 16, 2009. Version 57. 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
OrganismMacropus eugenii (Tammar wallaby)
Taxonomic identifier9315 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Diprotodontia › Macropodidae › Macropus

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Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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. Activated with catalytic amounts of streptokinase By similarity.

Subunit structure

Interacts with CSPG4 By similarity.

Subcellular location

Secreted.

Domain

Kringle domains mediate interaction with CSPG4 By similarity.

Post-translational modification

In the presence of the inhibitor, the activation involves only cleavage after Arg-576, 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 By similarity.

In the presence of the inhibitor, the activation involves only cleavage after Arg-576, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide By similarity.

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 – 1919 Potential
Chain20 – 806787Plasminogen
PRO_0000028064
Chain20 – 576557Plasmin heavy chain A By similarity
PRO_0000028065
Peptide20 – 9677Activation peptide By similarity
PRO_0000028066
Chain97 – 576480Plasmin heavy chain A, short form By similarity
PRO_0000028067
Chain577 – 806230Plasmin light chain B By similarity
PRO_0000028068

Regions

Domain20 – 9879PAN
Domain102 – 18180Kringle 1
Domain184 – 26279Kringle 2
Domain274 – 35279Kringle 3
Domain370 – 44879Kringle 4
Domain475 – 55581Kringle 5
Domain577 – 804228Peptidase S1

Sites

Active site6181Charge relay system By similarity
Active site6611Charge relay system By similarity
Active site7561Charge relay system By similarity

Amino acid modifications

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 bond371 ↔ 448 By similarity
Disulfide bond392 ↔ 431 By similarity
Disulfide bond420 ↔ 443 By similarity
Disulfide bond476 ↔ 555 By similarity
Disulfide bond497 ↔ 538 By similarity
Disulfide bond526 ↔ 550 By similarity
Disulfide bond563 ↔ 681Interchain (between A and B chains) By similarity
Disulfide bond573 ↔ 581Interchain (between A and B chains) By similarity
Disulfide bond603 ↔ 619 By similarity
Disulfide bond695 ↔ 762 By similarity
Disulfide bond725 ↔ 741 By similarity
Disulfide bond752 ↔ 780 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O18783-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 95FAA86DC20064D5

FASTA80690,981
        10         20         30         40         50         60 
MEYGKVIFLF LLFLKSGQGE SLENYIKTEG ASLSNSQKKQ FVASSTEECE ALCEKETEFV 

        70         80         90        100        110        120 
CRSFEHYNKE QKCVIMSENS KTSSVERKRD VVLFEKRIYL SDCKSGNGRN YRGTLSKTKS 

       130        140        150        160        170        180 
GITCQKWSDL SPHVPNYAPS KYPDAGLEKN YCRNPDDDVK GPWCYTTNPD IRYEYCDVPE 

       190        200        210        220        230        240 
CEDECMHCSG ENYRGTISKT ESGIECQPWD SQEPHSHEYI PSKFPSKDLK ENYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTSNP EKRWEFCNIP RCSSPPPPPG PMLQCLKGRG ENYRGKIAVT KSGHTCQRWN 

       310        320        330        340        350        360 
KQTPHKHNRT PENFPCRGLD ENYCRNPDGE LEPWCYTTNP DVRQEYCAIP SCGTSSPHTD 

       370        380        390        400        410        420 
RVEQSPVIQE CYEGKGENYR GTTSTTISGK KCQAWSSMTP HQHKKTPDNF PNADLIRNYC 

       430        440        450        460        470        480 
RNPDGDKSPW CYTMDPTVRW EFCNLEKCSG TGSTVLNAQT TRVPSVDTTS HPESDCMYGS 

       490        500        510        520        530        540 
GKDYRGKRST TVTGTLCQAW TAQEPHRHTI FTPDTYPRAG LEENYCRNPD GDPNGPWCYT 

       550        560        570        580        590        600 
TNPKKLFDYC DIPQCVSPSS FDCGKPRVEP QKCPGRIVGG CYAQPHSWPW QISLRTRFGE 

       610        620        630        640        650        660 
HFCGGTLIAP QWVLTAAHCL ERSQWPGAYK VILGLHREVN PESYSQEIGV SRLFKGPLAA 

       670        680        690        700        710        720 
DIALLKLNRP AAINDKVIPA CLPSQDFMVP DRTLCHVTGW GDTQGTSPRG LLKQASLPVI 

       730        740        750        760        770        780 
DNRVCNRHEY LNGRVKSTEL CAGHLVGRGD SCQGDSGGPL ICFEDDKYVL QGVTSWGLGC 

       790        800 
ARPNKPGVYV RVSRYISWIE DVMKNN

« Hide

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References

[1]"Convergent evolution of apolipoprotein(a) in primates and hedgehog."
Lawn R.M., Schwartz K., Patthy L.
Proc. Natl. Acad. Sci. U.S.A. 94:11992-11997(1997) [PubMed: 9342350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

AF012297 mRNA. Translation: AAB65760.1.

3D structure databases

HSSPHSSP built from PDB template 1BUI based on UniProtKB P00747.
SMRO18783. Positions 561-806.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

Phylogenomic databases

HOVERGENO18783.

Enzyme and pathway databases

BRENDA3.4.21.7. 190702.

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_MACEU
AccessionPrimary (citable) accession number: O18783
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 57 of the entry and version 1 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