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PROSITE documentation PDOC00431 [for PROSITE entry PS00492]

Clusterin signatures





Description

Clusterin is a vertebrate glycoprotein [1] which is known by various names:

  • In Human as complement-associated protein SP-40,40, complement cytolysis inhibitor (CLI), NA1/NA2, and apolipoprotein J (Apo-J).
  • In rat as sulfated glycoprotein 2 (SGP-2), dimeric acid glycoprotein (DAG), and Testosterone Repressed Prostate Message-2 (TRPM-2).
  • In bovine as glycoprotein III (GP-III).
  • In dog as glycoprotein 80 (gp-80).
  • In quail as protein T64.

The exact function of this protein is not yet clear, it is known to be expressed in a variety of tissues and it seems to be able to bind to cells, membranes, and hydrophobic proteins. It has been associated with programmed cell death.

Clusterin is synthesized as a precursor polypeptide of about 400 amino acids which is post-translationally cleaved to form two subunits (of about 200 amino acids each). The two subunits are linked by five disulfide bonds to form an antiparallel ladder-like structure [2]. In each of the mature subunits the five cysteines that are involved in disulfide bonds are clustered in domains of about 30 amino acids located in the central part of the subunits.

We have developed two signature patterns for clusterin, each of them contains three cysteines, the first pattern is derived from the N-terminal subunit cluster and the second pattern is derived from the C-terminal subunit cluster.

Last update:

May 2004 / Text revised.

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Technical section

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

CLUSTERIN_1, PS00492; Clusterin signature 1  (PATTERN)

CLUSTERIN_2, PS00493; Clusterin signature 2  (PATTERN)


References

1AuthorsJenne D.E. Tschopp J.
TitleClusterin: the intriguing guises of a widely expressed glycoprotein.
SourceTrends Biochem. Sci. 17:154-159(1992).
PubMed ID1585460

2AuthorsChoi-Miura N.H. Takahashi Y. Nakano Y. Tobe T. Tomita M.
SourceJ. Biochem. 112:557-561(1992).



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