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PROSITE documentation PDOC00020 [for PROSITE entry PS00021]

Kringle domain signature and profile





Description

Kringles [1,2,3] are triple-looped, disulfide cross-linked domains found in a varying number of copies, in some serine proteases and plasma proteins. The kringle domain has been found in the following proteins:

  • Apolipoprotein A (38 copies).
  • Blood coagulation factor XII (Hageman factor) (1 copy).
  • Hepatocyte growth factor (HGF) (4 copies).
  • Hepatocyte growth factor like protein (4 copies) [4].
  • Hepatocyte growth factor activator [1] (once) [5].
  • Plasminogen (5 copies).
  • Thrombin (2 copies).
  • Tissue plasminogen activator (TPA) (2 copies).
  • Urokinase-type plasminogen activator (1 copy).

The schematic representation of the structure of a typical kringle domain is shown below:

          +---------------------------------------+
          |                                       |
         xCxxxxxxxxxxxCxxxxxxxxxxCxxxxxCxxxxxxCxxxCx
                      |          |     |      |
                      +----------|-----+      |
                                 +------------+
'C': conserved cysteine involved in a disulfide bond.

Kringle domains are thought to play a role in binding mediators, such as membranes, other proteins or phospholipids, and in the regulation of proteolytic activity. As a signature pattern for this type of domain, we selected a conserved sequence that contains two of the cysteines invovled in disulfide bonds.

Expert(s) to contact by email:

Ikeo K.

Last update:

May 2004 / Text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

KRINGLE_1, PS00021; Kringle domain signature  (PATTERN)

KRINGLE_2, PS50070; Kringle domain profile  (MATRIX)


References

1AuthorsCastellino F.J., Beals J.M.
TitleThe genetic relationships between the kringle domains of human plasminogen, prothrombin, tissue plasminogen activator, urokinase, and coagulation factor XII.
SourceJ. Mol. Evol. 26:358-369(1987).
PubMed ID3131537

2AuthorsPatthy L.
TitleEvolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.
SourceCell 41:657-663(1985).
PubMed ID3891096

3AuthorsIkeo K., Takahashi K., Gojobori T.
TitleEvolutionary origin of numerous kringles in human and simian apolipoprotein(a).
SourceFEBS Lett. 287:146-148(1991).
PubMed ID1879523

4AuthorsFriezner Degen S.J., Stuart L.A., Han S., Jamison C.S.
SourceBiochemistry 30:9781-9791(1991).

5AuthorsMiyazawa K., Shimomura T., Kitamura A., Kondo J., Morimoto Y., Kitamura N.
TitleMolecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII.
SourceJ. Biol. Chem. 268:10024-10028(1993).
PubMed ID7683665



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