Protein Domain : SCAN domain superfamily IPR038269

Type	Homologous_superfamily
Description	A number of C2H2-zinc finger proteins contain a highly conserved N-terminal motif termed the SCAN (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) domain. The SCAN domain has been shown to be able to mediate homo- and hetero-oligomerisation [ ]. These proteins can either activate or repress transcription, although isolated recombinant SCAN domains do not modulate significantly the transcription [, ]. In addition to these zinc finger transcription factors, an isolated SCAN domain without adjacent zinc finger motifs has been identified in some proteins [, ]. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein []. The SCAN domain is enriched in hydrophobic and negatively charged residues with a L-X(6)-L motif at its core. This core is flanked by A, E, L, M, H and C residues that are frequently found in α-helices [ ]. Predictions of the secondary structure of the domain suggest the presence of at least three α-helices that are separated from one another by short looped regions bounded by proline residues []. It has been shown to be a selective oligomerization domain that mediates homotypic and heterotypic interactions between SCAN box containing proteins [, ].
Short Name	SCAN_sf