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Q7M323 (PLMN_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasminogen

EC=3.4.21.7
Gene names
Name:PLG
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length123 AA.
Sequence statusFragment.
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. Cannot be activated with streptokinase By similarity.

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 By similarity.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains at least 1 kringle 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: UniProtKB-KW

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›123›123Plasminogen
PRO_0000088703

Regions

Domain40 – 11879Kringle

Amino acid modifications

Disulfide bond41 ↔ 118 By similarity
Disulfide bond62 ↔ 101 By similarity
Disulfide bond90 ↔ 113 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1231

Sequences

Sequence LengthMass (Da)Tools
Q7M323 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: E53432C4DA0AC07C

FASTA12313,908
        10         20         30         40         50         60 
DLLDDYVNTQ GASLLTLSRK KLAGRSVEDC AAKCEEEAQD CYHGNGQSYR GTSSTTVTGR 

        70         80         90        100        110        120 
KCQSWSSMIP HRHQKTPESY PNAGLTMNYC RNPDADKSPW CYTTDPRVRW EFCNLKKCSE 


DSE 

« Hide

References

[1]"Structural aspects of the plasminogen of various species."
Schaller J., Rickli E.E.
Enzyme 40:63-69(1988) [PubMed: 3168975] [Abstract]
Cited for: PROTEIN SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRC61545.

3D structure databases

ProteinModelPortalQ7M323.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG105989.

Family and domain databases

InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 1 hit.
PfamPF00051. Kringle. 1 hit.
[Graphical view]
PRINTSPR00018. KRINGLE.
SMARTSM00130. KR. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 1 hit.
PROSITEPS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMN_CAPHI
AccessionPrimary (citable) accession number: Q7M323
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: December 15, 2003
Last modified: November 16, 2011
This is version 41 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