SEPDomain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47.
|SMART accession number:||SM00553|
|Interpro abstract (IPR012989):|
The SEP (after shp1, eyc and p47) domain is an eukaryotic domain, which occurs frequently and mainly in single units. Almost all proteins containing a SEP domain are succeeded closely by a UBX domain. The function of the SEP domain is as yet unknown but it has been proposed to act as a reversible competitive inhibitor of the lysosomal cysteine protease cathepsin L [(PUBMED:15029246), (PUBMED:15498563)].
The sructure of the SEP domain comprises a beta-sheet composed of four strands, and two alpha-helices. One side of the beta-sheet faces alpha1 and alpha2. The longer helix alpha1 packs against the four- stranded beta-sheet, where as the shorter helix alpha2 is located at one edge of the globular structure formed by alpha1 and the four stranded beta sheet. A number of highly conserved hydrophobic residues are present in the SEP domain, which are predominantly buried and form the hydrophobic core [(PUBMED:15029246), (PUBMED:15498563)].
Some proteins known to contain a SEP domain are listed below:
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)