The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity, or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven ?subunits each, and the inner two rings each consist of seven beta subunits.
Synonyms: HC9, HsT17706, Macropain subunit C9, MGC111191, MGC12467, MGC24813, Multicatalytic endopeptidase complex subunit C9, Proteasome prosome macropain subunit alpha type 4, Proteasome alpha 4 subunit, Proteasome component C9, Proteasome subunit alpha type 4, Proteasome subunit alpha type-4, Proteasome subunit HC9, Proteasome subunit L, PSA4_HUMAN, PSC9, PSMA 4, psmA4.