InterPro : IPR012989

Name  SEP domain Short Name  SEP_domain
Type  Domain Description  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 ). The functionof the SEP domain is as yet unknown but it has been proposed to act as areversible competitive inhibitor of the lysosomal cysteine protease cathepsinL [, ].The sructure of the SEP domain comprises a beta-sheet composed of fourstrands, and two alpha-helices. One side of the beta-sheetfaces alpha1 and alpha2. The longer helix alpha1 packs against the four-stranded beta-sheet, where as the shorter helix alpha2 is located at one edgeof the globular structure formed by alpha1 and the four stranded beta sheet. Anumber of highly conserved hydrophobic residues are present in the SEP domain,which are predominantly buried and form the hydrophobic core [, ].Some proteins known to contain a SEP domain are listed below:- Eukaryotic NSFL1 cofactor p37 (or p97 cofactor p37), an adapter proteinrequired for Golgi and endoplasmic reticulum biogenesis. It is involved inGolgi and endoplasmic reticulum maintenance during interphase and in theirreassembly at the end of mitosis.- Eukaryotic NSFL1 cofactor p47 (or p97 cofactor p47), a major adaptormolecule of the cytosolic AAA-type ATPase (ATPases associated with variouscellular activities) p97. p47 is required for the p97-regulated membranereassembly of the endoplasmic reticulum (ER), the nuclear envelope and theGolgi apparatus.- Vertebrate UBX domain-containing protein 4 (UBXD4).- Plant UBA and UBX domain-containing protein.- Saccharomyces cerevisiae(Baker's yeast) UBX domain-containing protein 1 or Suppressor ofhigh-copy PP1 protein (shp1), the homologue of p47.- Drosophila melanogaster(Fruit fly) eyes closed (eyc).
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

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2 Publications

First Author Title Year Journal Volume Pages
Soukenik M The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L. 2004 FEBS Lett 576 358-62
Yuan X Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97. 2004 EMBO J 23 1463-73



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)