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PROSITE documentation PDOC00732

ER lumen protein retaining receptor signatures





Description

Proteins that reside in the lumen of the endoplasmic reticulum (ER) contain a C-terminal tetrapeptide (generally K-D-E-L or H-D-E-L) that serves as a signal for their retrieval (retrograde transport) from subsequent compartments of the secretory pathway. The signal is recognized by a receptor molecule that is believed to cycle between the cis side of the Golgi apparatus and the ER [1]. This protein is known as the ER lumen protein retaining receptor or also as the 'KDEL receptor'. It has been characterized in a variety of species, including fungi (gene ERD2), plants, Plasmodium, Drosophila and mammals. In mammals two highly related forms of the receptor are known.

Structurally, the receptor is a protein of about 220 residues that seems to contain seven transmembrane regions [2]. The N-terminal part (3 residues) is oriented toward the lumen while the C-terminal tail (about 12 residues) is cytoplasmic. There are three lumenal and three cytoplasmic loops.

We developed two signature patterns for these receptors. The first pattern corresponds to the C-terminal half of the first cytoplasmic loop as well as most of the second transmembrane domain. The second pattern is a perfectly conserved decapeptide that corresponds to the central part of the fifth transmembrane domain.

Last update:

December 2001 / Patterns and text revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

ER_LUMEN_RECEPTOR_1, PS00951; ER lumen protein retaining receptor signature 1  (PATTERN)

ER_LUMEN_RECEPTOR_2, PS00952; ER lumen protein retaining receptor signature 2  (PATTERN)


References

1AuthorsPelham H.R.B.
TitleRecycling of proteins between the endoplasmic reticulum and Golgi complex.
SourceCurr. Opin. Cell Biol. 3:585-591(1991).
PubMed ID1663369

2AuthorsTownsley F.M. Wilson D.W. Pelham H.R.B.
TitleMutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport.
SourceEMBO J. 12:2821-2829(1993).
PubMed ID8392934



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