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Reviewed, UniProtKB/Swiss-Prot P80009 (PLMN_CANFA)

Last modified June 16, 2009. Version 73. 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

Names and origin

Protein namesRecommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 2 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Plasmin light chain B
Gene names
Name: PLG
OrganismCanis familiaris (Dog)
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 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.

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 By similarity.

Subcellular location

Secreted.

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.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Tissue remodeling
   Cellular componentSecreted
   DomainKringle
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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
P80009-1 [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.

Cross-references

3D structure databases

HSSPHSSP built from PDB template 5HPG based on UniProtKB P00747.
SMRP80009. Positions 87-333.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

Genome annotation databases

EnsemblENSCAFG00000000758. Canis familiaris. [Contig view]

Phylogenomic databases

HOVERGENP80009.

Enzyme and pathway databases

BRENDA3.4.21.7. 463.

Family and domain databases

InterProIPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
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.
ProDomPD000395. Kringle. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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