{PDOC00431} {PS00492; CLUSTERIN_1} {PS00493; CLUSTERIN_2} {BEGIN} ************************ * Clusterin signatures * ************************ 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 3 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 3 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. -Last update: May 2004 / Text revised. [ 1] Jenne D.E., Tschopp J. "Clusterin: the intriguing guises of a widely expressed glycoprotein." Trends Biochem. Sci. 17:154-159(1992). PubMed=1585460 [ 2] Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M. J. Biochem. 112:557-561(1992). -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}