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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 PDOC51225
MARVEL domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51225

Description

The ~130-residue MAL and related proteins for vesicle trafficking and membrane link (MARVEL) domain is a module with a four transmembrane-helix architecture that has been identified in proteins of the myelin and lymphocyte (MAL), physins, gyrins and occludin families. All described MARVEL domain-containing proteins are consistent with the M-shaped topology: four transmembrane-helix region architecture with cytoplasmic N- and C-terminal regions. Their function could be related to cholesterol-rich membrane apposition events in a variety of cellular processes, such as biogenesis of vesicular transport carriers or tight junction regulation [1].

The profile we developed covers the entire MARVEL domain.

Last update:

August 2006 / First entry.

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Technical section

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

MARVEL, PS51225; MARVEL domain profile  (MATRIX)


Reference

1AuthorsSanchez-Pulido L. Martin-Belmonte F. Valencia A. Alonso M.A.
TitleMARVEL: a conserved domain involved in membrane apposition events.
SourceTrends Biochem. Sci. 27:599-601(2002).
PubMed ID12468223



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