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Q29485 (PLMN_ERIEU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Plasminogen
EC=3.4.21.7

Cleaved into the following 4 chains:

  1. Plasmin heavy chain A
  2. Activation peptide
  3. Plasmin heavy chain A, short form
  4. Plasmin light chain B
Gene names
Name:PLG
OrganismErinaceus europaeus (Western European hedgehog)
Taxonomic identifier9365 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Insectivora › Erinaceidae › Erinaceinae › Erinaceus

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

In the presence of the inhibitor, the activation involves only cleavage after Arg-582, 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 By similarity
Chain20 – 810791Plasminogen
PRO_0000028046
Chain20 – 582563Plasmin heavy chain A By similarity
PRO_0000028047
Peptide20 – 9778Activation peptide By similarity
PRO_0000028048
Chain98 – 582485Plasmin heavy chain A, short form By similarity
PRO_0000028049
Chain583 – 810228Plasmin light chain B By similarity
PRO_0000028050

Regions

Domain20 – 9879PAN
Domain103 – 18179Kringle 1
Domain185 – 26278Kringle 2
Domain275 – 35278Kringle 3
Domain379 – 45678Kringle 4
Domain482 – 56180Kringle 5
Domain582 – 808227Peptidase S1

Sites

Active site6221Charge relay system
Active site6651Charge relay system
Active site7601Charge relay system

Amino acid modifications

Modified residue5981Phosphoserine By similarity
Glycosylation3391N-linked (GlcNAc...) Potential
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 bond379 ↔ 456 By similarity
Disulfide bond400 ↔ 439 By similarity
Disulfide bond428 ↔ 451 By similarity
Disulfide bond482 ↔ 561 By similarity
Disulfide bond503 ↔ 544 By similarity
Disulfide bond532 ↔ 556 By similarity
Disulfide bond569 ↔ 685Interchain (between A and B chains) By similarity
Disulfide bond579 ↔ 586Interchain (between A and B chains) By similarity
Disulfide bond607 ↔ 623 By similarity
Disulfide bond699 ↔ 766 By similarity
Disulfide bond729 ↔ 745 By similarity
Disulfide bond756 ↔ 784 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29485 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 8E75780946017A16

FASTA81090,902
        10         20         30         40         50         60 
MQRKELVLLF LLFLQPGHGI PLDDYVTTQG ASLCSSTKKQ LSVGSTEECA VKCEKETSFI 

        70         80         90        100        110        120 
CRSFQYHSKE QQCVIMAENS KSTPVLRMRD VILFEKKMYL SECKVGNGKY YRGTVSKTKT 

       130        140        150        160        170        180 
GLTCQKWSAE TPHKPRFSPD ENPSEGLDQN YCRNPDNDPK GPWCYTMDPE VRYEYCEIIQ 

       190        200        210        220        230        240 
CEDECMHCSG QNYVGKISRT MSGLECQPWD SQIPHPHGFI PSKFPSKNLK MNYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTMDR NKRWEYCDIP RCTTPPPPSG PTYQCLMGNG EHYQGNVAVT VSGLTCQRWG 

       310        320        330        340        350        360 
EQSPHRHDRT PENYPCKNLD ENYCRNPDGE PAPWCFTTNS SVRWEFCKIP DCVSSASETE 

       370        380        390        400        410        420 
HSDAPVIVPP EQTPVVQECY QGNGQTYRGT SSTTITGKKC QPWTSMRPHR HSKTPENYPD 

       430        440        450        460        470        480 
ADLTMNYCRN PDGDKGPWCY TTDPSVRWEF CNLKKCSGTE MSATNSSPVQ VSSASESSEQ 

       490        500        510        520        530        540 
DCIIDNGKGY RGTKATTGAG TPCQAWAAQE PHRHSIFTPE TNPRADLQEN YCRNPDGDAN 

       550        560        570        580        590        600 
GPWCYTTNPR KLFDYCDIPH CVSPSSADCG KPKVEPKKCP GRVGGCVAHP HSWPWQVSLR 

       610        620        630        640        650        660 
RFGQHFCGGT LISPEWVVTA AHCLEKFSNP AIYKVVLGAH QETRLERDVQ IKGVTKMFLE 

       670        680        690        700        710        720 
PYRADIALLK LSSPAIITDK DHPACLPNSN YMVADRSLCY ITGWGETKGT YGAGLLKEAQ 

       730        740        750        760        770        780 
LPVIENKVCN RQSFLNGRVR STELCAGHLA GGVDSCQGDS GGPLVCFEKD RYILQGVTSW 

       790        800        810 
GLGCARLTRP GVYVRVSRYV SWLQDVMRNN

« Hide

References

[1]"The recurring evolution of lipoprotein(a). Insights from cloning of hedgehog apolipoprotein(a)."
Lawn R.M., Boonmark N.W., Schwartz K., Lindahl G.E., Wade D.P., Byrne C.D., Fong K.J., Meer K., Patthy L.
J. Biol. Chem. 270:24004-24009(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Lawn R.M.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33171 mRNA. Translation: AAC48717.1.
PIRI46260.

3D structure databases

ProteinModelPortalQ29485.
SMRQ29485. Positions 100-352, 568-810.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004381.

Family and domain databases

Gene3D2.40.20.10. 5 hits.
InterProIPR000001. 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]
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 5 hits.
SSF50494. Pept_Ser_Cys. 1 hit.
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...

Entry information

Entry namePLMN_ERIEU
AccessionPrimary (citable) accession number: Q29485
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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