Tripartite motif-containing protein 5 also known as RING finger protein 88 is a protein that in humans is encoded by the TRIM5 gene. The alpha isoform of this protein, TRIM5α, is a retrovirus restriction factor, which mediates a species-specific early block to retrovirus infection. TRIM5α is composed of 493 amino acids which is found in the cells of most primates. TRIM5α is an intrinsic immune factor important in the innate immune defense against retroviruses, along with the APOBEC family of proteins, tetherin and TRIM22. Structure TRIM5α belongs to the TRIM protein family (TRIM stands for TRIpartite Motif); this family was first identified by Reddy in 1992 as a set of proteins which contain a RING type zinc finger domain, a B-box zinc binding domain, followed by a coiled-coil region. TRIM5α bears the C-terminal PRY-SPRY or B30.2 domain in addition to the other domains. Function and means of action When a retrovirus enters the host cell cytosol, the retroviral capsid was previously believed to undergo uncoating, though this (the complete uncoating theory) is now doubted; rather the true picture is thought to be that capsid uncoating does indeed take place in the cytosol but that it is a process which takes place progressively as the capsid gets closer and closer to the nucleus, though the uncoating process usually, but not always, completes in the nucleus. Further, the viral genome in the capsid is reverse transcribed inside the viral capsid to enable the production of daughter virions. TRIM5α is present in the cytosol. It recognizes motifs within viral capsid proteins, which causes the TRIM5α to smother the (not yet uncoated) capsid in a reticulatory way so as to form a repeating regular hexagonal net, two sides of each hexagon being made up of two spokes of a three-way hub and spoke trimer and consequently to interfere with the viral capsid uncoating process, thereby preventing (1) transport of the viral genome to the host cell nucleus and (2) successful reverse transcription. The exact mechanism of action has not been shown conclusively, but capsid protein from restricted viruses (that is viruses which are the subject of TRIM5α intervention) is removed by proteasome-dependent degradation. The TRIM5α, once formed into its highly regular reticulatory net recruits ubiquitin for this purpose, which, in turn engages the proteasome. The involvement of other cellular proteins in the inhibition mediated by TRIM5α is suspected but as yet not demonstrated. However,