{PDOC51021}
{PS51021; BAR}
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* BAR domain profile *
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The BAR (Bin-Amphiphysin-Rvs) domain is about 200 amino acid long. This domain
can  be  found  alone  or  in  association with other domains such as SH3 (see
<PDOC50002>)  and RhoGAP (see <PDOC50238>). BAR domain containing proteins are
a  unique  class of adaptor proteins characterized by a common N-terminal fold
termed  the  BAR  domain.  This  set of adaptors, which includes the mammalian
proteins  amphiphysin  and  Bin1 and the yeast proteins Rvs167 and Rvs161, has
been  implicated  in  diverse  cellular  processes, including synaptic vesicle
endocytosis,   actin   regulation,   differentiation,   cell   survival,   and
tumorigenesis. Clearly there are two functions associated with the BAR domain,
the  sensing and/or induction of membrane curvature and the binding to a small
GTPase [1,2].

The  resolution of the N-terminus of amphiphysin has shown that the BAR domain
forms   a   crescent-shaped   dimer   of  a  three-helix  coiled-coil  with  a
characteristic  set  of  conserved hydrophobic, aromatic and hydrophilic amino
acids   (see   <PDB:1URU>)   [3,4].  More  structural  studies  revealed  that
dimerization  is a minimal function of BAR-domain-containning proteins. It was
suggested  that  the  V-shaped  dimer  is able to sense and/or induce membrane
bending.

More,  amphiphysin and endophilin contain a short sequence stretch adjacent to
the  N  terminus  of  the  BAR  domain  which  is presumed to be essential for
lipid-binding  and  tubule  formation. This sequence at the N-terminal end was
shown  to form an amphipathic helix, thereby extending the helical backbone of
the  dimer  at  the tips. Together with the BAR domain, this sequence motif is
termed N-BAR and can be found in a subgroup of the BAR-domain family including
amphiphysin. This stretch is not covered by the developed profile.

Some proteins known to contain a BAR domain are listed below:

 - Animal amphiphysin proteins.
 - Yeast Rvs (amphiphysin-like) proteins.
 - Animal endophylin SH3-containing GRB2-like proteins.
 - Animal Bin Myc box dependent interacting proteins [2].
 - Animal nadrins.
 - Animal Tuba proteins [5].

The profile we developed covers the entire BAR domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: This profile picks up the entire Bin-Amphiphysin-Rvs family. But recent
 papers, based  on  sequence  and  structural  similarities  have shown that a
 conserved region  in  more  divergent  families, like oligophrenin, centaurin
 beta, sorting  nexin, ICA69, pick1 or arfaptins, is related to the BAR domain
 [6,7,8]. These  families  are  however  too  divergent to be detected by this
 profile.

-Last update: September 2004 / First entry.

[ 1] Balguerie A., Sivadon P., Bonneu M., Aigle M.
     "Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with
     actin patches."
     J. Cell Sci. 112:2529-2537(1999).
     PubMed=10393809
[ 2] Ge K., Prendergast G.C.
     "Bin2, a functionally nonredundant member of the BAR adaptor gene
     family."
     Genomics 67:210-220(2000).
     PubMed=10903846; DOI=10.1006/geno.2000.6216
[ 3] Zimmerberg J., McLaughlin S.
     "Membrane curvature: how BAR domains bend bilayers."
     Curr. Biol. 14:R250-R252(2004).
     PubMed=15043839; DOI=10.1016/j.cub.2004.02.060
[ 4] Miele A.E., Watson P.J., Evans P.R., Traub L.M., Owen D.J.
     "Two distinct interaction motifs in amphiphysin bind two independent
     sites on the clathrin terminal domain beta-propeller."
     Nat. Struct. Mol. Biol. 11:242-248(2004).
     PubMed=14981508; DOI=10.1038/nsmb736
[ 5] Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
     Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
     "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
     domains, links dynamin to regulation of the actin cytoskeleton."
     J. Biol. Chem. 278:49031-49043(2003).
     PubMed=14506234; DOI=10.1074/jbc.M308104200
[ 6] Habermann B.
     "The BAR-domain family of proteins: a case of bending and binding?"
     EMBO Rep. 5:250-255(2004).
     PubMed=14993925; DOI=10.1038/sj.embor.7400105
[ 7] Peter B.J., Kent H.M., Mills I.G., Vallis Y., Butler P.J.G., Evans P.R.,
     McMahon H.T.
     "BAR domains as sensors of membrane curvature: the amphiphysin BAR
     structure."
     Science 303:495-499(2004).
     PubMed=14645856; DOI=10.1126/science.1092586
[ 8] Richnau N., Fransson A., Farsad K., Aspenstroem P.
     "RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to
     membrane lipids and tubulation of liposomes."
     Biochem. Biophys. Res. Commun. 320:1034-1042(2004).
     PubMed=15240152; DOI=10.1016/j.bbrc.2004.05.221

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