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P80009 (PLMN_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. 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 2 chains:

  1. Plasmin heavy chain A
  2. Plasmin light chain B
Gene names
Name:PLG
OrganismCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length333 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Activated with urokinase and high concentrations of 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.

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 at least 1 kringle domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 103›103Plasmin heavy chain A
PRO_0000028044
Chain104 – 333230Plasmin light chain B
PRO_0000028045

Regions

Domain4 – 8380Kringle 5
Domain104 – 331228Peptidase S1

Sites

Active site1451Charge relay system By similarity
Active site1881Charge relay system By similarity
Active site2831Charge relay system By similarity
Site1521Interaction with streptokinase Probable
Site1861Interaction with streptokinase Probable
Site2641Interaction with streptokinase Probable
Site2771Site of substrate specificity By similarity

Amino acid modifications

Disulfide bond4 ↔ 83 By similarity
Disulfide bond25 ↔ 66 By similarity
Disulfide bond54 ↔ 78 By similarity
Disulfide bond90 ↔ 208Interchain (between A and B chains) By similarity
Disulfide bond100 ↔ 108Interchain (between A and B chains) By similarity
Disulfide bond130 ↔ 146 By similarity
Disulfide bond222 ↔ 289 By similarity
Disulfide bond252 ↔ 268 By similarity
Disulfide bond279 ↔ 307 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P80009 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: C8C0271B6C6AC8D4

FASTA33336,678
        10         20         30         40         50         60 
ASDCMFGNGK GYRGKKATTV MGIPCQEWAA QEPHRHSIFT PETNPQAGLE KNYCRNPDGD 

        70         80         90        100        110        120 
VNGPWCYTMN QRKLFDYCDV PQCVSTSFDC GKPQVEPKKC PGRVVGGCVA NPHSWPWQIS 

       130        140        150        160        170        180 
LRTRYGKHFC GGTLISPEWV LTAAHCLERS SRPASYKVIL GAHKEVNLES DVQEIEVYKL 

       190        200        210        220        230        240 
FLEPTRADIA LLKLSSPAVI TSKVIPACLP PPNYVVADRT LCYITGWGET QGTYGAGLLK 

       250        260        270        280        290        300 
EAQLPVIENK VCNRYEYLNG RVKSTELCAG NLAGGTDSCQ GDSGGPLVCF EKDKYILQGV 

       310        320        330 
TSWGLGCARP NKPGVYVRVS RFVTWIEGIM RNN 

« Hide

References

[1]"Complete amino acid sequence of canine miniplasminogen."
Schaller J., Straub C., Kaempfer U., Rickli E.E.
Protein Seq. Data Anal. 2:445-450(1989) [PubMed: 2626424] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

3D structure databases

ProteinModelPortalP80009.
SMRP80009. Positions 3-85, 87-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGP80009.

Protein family/group databases

MEROPSS01.233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG09109.
HOVERGENHBG008633.
InParanoidP80009.
OrthoDBEOG4RR6GQ.

Family and domain databases

InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 1 hit.
PfamPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
SMARTSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMN_CANFA
AccessionPrimary (citable) accession number: P80009
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 16, 2011
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