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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51073
RPEL repeat profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51073

Description

RPEL repeat (RPxxxEL) containing proteins are found in a wide range of metazoan organisms. RPEL repeats have been shown to be required for unpolymerized actin binding and proteins containing RPEL repeats are able to modify cell shape and/or are important in the regulation of gene expression by the actin cytoskeleton. RPEL repeats can be found in association with the SAP motif (see <PDOC50800>), which could be involved in DNA binding [1,2].

Some proteins known to contain RPEL repeats are listed below:

  • Mammalian myocardin, heart-specific serum response factor (SRF) co- activator.
  • Vertebrate myocardin-related transcription factor A (MRTF-A or MAL), a signal-regulated SRF co-activator.
  • Vertebrate myocardin-related transcription factor B (MRTF-B).
  • Mammalian phosphatase and actin regulator 1 to 3.

The profile we developed covers the entire RPEL repeat.

Last update:

January 2005 / First entry.

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Technical section

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

RPEL, PS51073; RPEL repeat profile  (MATRIX)


References

1AuthorsMiralles F. Posern G. Zaromytidou A.-I. Treisman R.
TitleActin dynamics control SRF activity by regulation of its coactivator MAL.
SourceCell 113:329-342(2003).
PubMed ID12732141

2AuthorsFavot L. Gillingwater M. Scott C. Kemp P.R.
TitleOverexpression of a family of RPEL proteins modifies cell shape.
SourceFEBS Lett. 579:100-104(2005).
PubMed ID15620697
DOI10.1016/j.febslet.2004.11.054



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