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PDOC00431
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1995-07-26
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* Clusterin signatures *
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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.
-Consensus pattern: C-K-P-C-L-K-x-T-C
[The three C's are involved in disulfide bonds]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Consensus pattern: C-L-[RK]-M-[RK]-x-[EQ]-C-[ED]-K-C
[The three C's are involved in disulfide bonds]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Expert(s) to contact by email: Peitsch M.C.
mcp13936@ggr.co.uk
-Last update: June 1994 / Text revised.
[ 1] Jenne D.E., Tschopp J.
Trends Biochem. Sci. 17:154-159(1992).
[ 2] Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M.
J. Biochem. 112:557-561(1992).