{PDOC51741}
{PS51741; F_BAR}
{BEGIN}
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* F-BAR domain profile *
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All eukaryotic  cells  are  surrounded  by  a  plasma  membrane, and they also
contain multiple  membrane-based  organelles and structures inside cells. Thus
membrane remodeling is likely to be important for most cellular activities and
development. The  Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins has
been found  to  play a major role in remodeling cellular membranes linked with
organelle biogenesis, membrane trafficking, cell division, cell morphology and
cell migration.  The  BAR  domain  superfamily  of  proteins is evolutionarily
conserved with  representative  members  present  from yeast to man. Currently
there are  three  distinct families of BAR domain proteins: classical BAR (see
<PDOC51021>), F-BAR  (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I-
BAR (inverse-BAR  e.g.,  IRSp53).  The classical BAR, F-BAR, and I-BAR domains
are structurally  similar homodimeric modules with antiparallel arrangement of
monomers [1,2].

The F-BAR  domain  is  emerging  as an important player in membrane remodeling
pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics
associated with  endocytic  pathways  and  filopodium  formation. F-BAR domain
containing proteins  can  be categorized into five sub-families based on their
phylogeny which  is  consistent  with  the  additional  protein  domains  they
possess, for  example,  RhoGAP domains (see <PDOC50238>), Cdc42 binding sites,
SH2 domains  (see  <PDOC50001>),  SH3  domains  (see <PDOC50002>) and tyrosine
kinase domains (see <PDOC00100>) [1]:

 - the Toca subfamily (FBP17, TRIP10 or CIP4, and Toca-1 or FBP1).
 - the Fps/Fes and Fer subfamily of non-receptor tyrosine kinases.
 - the Rho GTPase (RhoGAP) activating protein subfamily.
 - the syndaptin/pacsin subfamily.
 - the GAS7/PSTPI1/FCHO subfamily.

The N-terminal  part  (about  one  third)  of  the F-BAR domain was previously
characterized as  an  FCH  (FER-CIP4  homology) domain. However, the region of
sequence similarity  extends  to  an  adjacent  region with a coiled-coil (CC)
structure. Hence,  the  F-BAR  domain (FCH+CC, ~300 amino acids) has also been
called extended FC (EFC) domain. The F-BAR domain plays a role in dimerization
and membrane  phospholipid  binding. It binds specifically to certain kinds of
lipids and acts as a a dimeric membrane-binding curvature effector [2,3,4].

The F-BAR  domain  is composed of five helices. Its structure is composed of a
short N-terminal helix, three long alpha helices, and a short C-terminal helix
followed by an extended peptide of 17 amino acids  (see <PDB:2EFK>) [2,5].

The profile we developed covers the entire F-BAR domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2014 / First entry.

[ 1] Ahmed S., Bu W., Lee R.T., Maurer-Stroh S., Goh W.I.
     "F-BAR domain proteins: Families and function."
     Commun. Integr. Biol. 3:116-121(2010).
     PubMed=20585502
[ 2] Henne W.M., Kent H.M., Ford M.G.J., Hegde B.G., Daumke O., Butler P.J.G.,
     Mittal R., Langen R., Evans P.R., McMahon H.T.
     "Structure and analysis of FCHo2 F-BAR domain: a dimerizing and
     membrane recruitment module that effects membrane curvature."
     Structure 15:839-852(2007).
     PubMed=17540576; DOI=10.1016/j.str.2007.05.002
[ 3] Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H.,
     De Camilli P.
     "Dynamin and the actin cytoskeleton cooperatively regulate plasma
     membrane invagination by BAR and F-BAR proteins."
     Dev. Cell 9:791-804(2005).
     PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005
[ 4] Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T.,
     Takenawa T.
     "Coordination between the actin cytoskeleton and membrane deformation
     by a novel membrane tubulation domain of PCH proteins is involved in
     endocytosis."
     J. Cell Biol. 172:269-279(2006).
     PubMed=16418535; DOI=10.1083/jcb.200508091
[ 5] Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K.,
     Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L.,
     Liu Z.-J., Wang B.-C., Yamamoto M., Terada T., Miyazawa A., Tanaka A.,
     Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S.
     "Curved EFC/F-BAR-domain dimers are joined end to end into a filament
     for membrane invagination in endocytosis."
     Cell 129:761-772(2007).
     PubMed=17512409; DOI=10.1016/j.cell.2007.03.040

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