|PROSITE documentation PDOC51783|
The BEACH domain (see <PDOC50197>) defines a large family of eukaryotic proteins that have diverse cellular functions in vesicle trafficking, membrane dynamics, and receptor signaling. The sequence homology among these proteins is limited to their C-terminal region, where they contain the PH-BEACH-WD40 domains. The WD40 domain (see <PDOC00574>) is generally located at the extreme C terminus of these proteins and may be important for protein-protein interactions. The BEACH domain is located just prior to the WD40 domain in these proteins and is the only domain that is highly conserved among them. The pleckstrin homology (PH) domain ( see <PDOC50003>) is weakly conserved among the BEACH proteins and does not share any recognizable sequence similarity with other PH domains. The structural organization of these three domains is highly conserved across all known BEACH domain containing proteins (BDCPs) and might function as an independent cassette within these proteins. Therefore, this region is referred to as the PH-BEACH-WD40 (PBW) module [1,2,3].
The BEACH-type PH domain contains a seven-stranded, antiparallel β-sandwich (β1-β7) and an α helix (α3) near its C terminus (see <PDB:1T77>). This is the typical fold of canonical PH domains, although the PH domains of BEACH proteins share no sequence similarity with these other PH domain. Another feature of the BEACH-type PH domain is the presence of two small helices (α1 and α2) in the loop between strands β3 and β4. These helices partially block the binding site for phospholipid and phosphotyrosine in the other PH domains and suggest that the BEACH-type PH domain may have a different function [1,2].
Some proteins known to contain a PH BEACH-type domain are listed below:
The profile we developed covers the entire PH BEACH-type domain.Last update:
October 2015 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Jogl G. Shen Y. Gebauer D. Li J. Wiegmann K. Kashkar H. Kroenke M. Tong L.|
|Title||Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.|
|Source||EMBO J. 21:4785-4795(2002).|
|2||Authors||Gebauer D. Li J. Jogl G. Shen Y. Myszka D.G. Tong L.|
|Title||Crystal structure of the PH-BEACH domains of human LRBA/BGL.|
|3||Authors||Steffens A. Braeutigam A. Jakoby M. Huelskamp M.|
|Title||The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization.|
|Source||PLoS Biol. 13:E1002188-E1002188(2015).|