Lon (also known as endopeptidase La, EC 188.8.131.52) is a multi-domain ATP-dependent protease found throughout all kingdoms of life. It is involved in
protein quality control and several regulatory processes. All Lon proteases
contain an ATPase domain belonging to the AAA+ superfamily of molecular
machines, and a proteolytic domain (see <PDOC51786>) with a serine-lysine
catalytic dyad in which a lysine assists the catalytic serine in proteolytic
cleavage. Lon proteases can be divided into two subfamilies: A type (A-Lons),
which have a large multi-lobed N-terminal domain together with the ATPase and
protease domains, and B type (B-Lons), which lack an N domain, but have a
membrane-anchoring region emerging from the ATPase domain. B-Lons are found in
Archaea, in which they are the lone membrane-anchored ATP-dependent protease.
The soluble A-Lons are found in all bacteria and in eukaryotic cell
organelles, such as mitochondria and peroxisomes, and are needed for recovery
from various stress conditions [1,2,3,4,5,6]. Animal cereblon (CRBN) is a
ubiquitously expressed protein that is part of the cullin-4-containing E3
ubiquitin ligase complex CUL4-RBX1-DDB1 (known as CRL4). It contain an N-terminal domain that ressembles the one of A-Lons . The Lon N-terminal
domain is thought to be involved in substrate binding and might represent a
general protein and polypeptide interaction domain [1,2].
The structure of the Lon N-terminal domain consists of two distinct regions,
connected by an extended loop: a compact β-sheet rich, globular subdomain,
and an additional α-helical subdomain (see <PDB:3M65>) [1,2].
The profile we developed covers the entire Lon N-terminal domain.
Fischer E.S. Boehm K. Lydeard J.R. Yang H. Stadler M.B. Cavadini S. Nagel J. Serluca F. Acker V. Lingaraju G.M. Tichkule R.B. Schebesta M. Forrester W.C. Schirle M. Hassiepen U. Ottl J. Hild M. Beckwith R.E.J. Harper J.W. Jenkins J.L. Thomae N.H.
Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide.
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