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PROSITE documentation PDOC51399 [for PROSITE entry PS51399] |
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 (see <PDOC50033>). 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 [1,2].
The sructure of the SEP domain comprises a β-sheet composed of four strands, and two α-helices (see <PDB:1VAZ; A>). One side of the β-sheet faces α1 and α2. The longer helix α1 packs against the four-stranded β-sheet, where as the shorter helix α2 is located at one edge of the globular structure formed by α1 and the four stranded β sheet. A number of highly conserved hydrophobic residues are present in the SEP domain, which are predominantly buried and form the hydrophobic core [1,2].
Some proteins known to contain a SEP domain are listed below:
The profile we developed covers the entire SEP domain.
Last update:August 2008 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Yuan X. Simpson P. Mckeown C. Kondo H. Uchiyama K. Wallis R. Dreveny I. Keetch C. Zhang X. Robinson C. Freemont P. Matthews S. |
Title | Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97. | |
Source | EMBO J. 23:1463-1473(2004). | |
PubMed ID | 15029246 | |
DOI | 10.1038/sj.emboj.7600152 |
2 | Authors | Soukenik M. Diehl A. Leidert M. Sievert V. Buessow K. Leitner D. Labudde D. Ball L.J. Lechner A. Naegler D.K. Oschkinat H. |
Title | The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L. | |
Source | FEBS Lett. 576:358-362(2004). | |
PubMed ID | 15498563 | |
DOI | 10.1016/j.febslet.2004.09.037 |