{PDOC51860}
{PS51860; REM_1}
{BEGIN}
************************
* REM-1 domain profile *
************************

Rho GTPases  are  molecular  switches  that  regulate  many essential cellular
processes, including    actin   dynamics,   gene   transcription,   cell-cycle
progression and cell adhesion. In the GTP-bound form they are able to interact
with effector  or target molecules to initiate a downstream response, while an
intrinsic GTPase  activity  returns  the  proteins  to the GDP-bound state, to
complete the  cycle  and terminate signal transduction. The Rho effector motif
class 1  (REM-1)  domain specifically binds GTP-Rho and is widely conserved in
the following Rho effector proteins [1,2,3]:

 - Vertebrate  serine/threonine-protein kinases N (PKNs), contain three copies
   of the  REM-1  domain.  Many  proteins that interact with PKNs are involved
   with the  cytoskeletal  network,  e.g. alpha-actinin and vimentin. PKNs are
   also implicated  in  the  control of transcrption factors, mitogenesis, and
   cell regulation.  PKNs have also been shown to play a role in apoptosis and
   to be  involved  in  keratinocyte  cell-cell  adhesion  with  increased PKN
   activity promoting cell-cell adhesion [4,5].
 - Vertebrate PKN-related proteins (Rhophilins, RHPNs).
 - Vertebrate Rhotekins (RTKNs).
 - Animal transducer of Cdc42-dependent actin assembly (TOCA) family proteins,
   comprise an  N-terminal  F-BAR  domain  (see  <PDOC51741>), a central REM-1
   domain, and a C-terminal SH3 domain (see <PDOC50002>) [6].
 - Yeast protein kinase C-like 1 (PKC1).

The REM-1  domain  contains  two  long  alpha  helices  forming  a left-handed
antiparallel coiled-coil fold (see <PDB:5FRG>) termed the antiparallel coiled-
coil (ACC)  finger domain. The two long helices encompass the basic region and
the leucine  repeat  region,  which  are  identified as the Rho-binding region
[4,5,6].

The profile we developed covers the entire REM-1 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2018 / First entry.

[ 1] Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N.,
     Mukai H., Ono Y., Kakizuka A., Narumiya S.
     "Protein kinase N (PKN) and PKN-related protein rhophilin as targets
     of small GTPase Rho."
     Science 271:645-648(1996).
     PubMed=8571126
[ 2] Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
     Fujisawa K., Morii N., Madaule P., Narumiya S.
     "Rhotekin, a new putative target for Rho bearing homology to a
     serine/threonine kinase, PKN, and rhophilin in the rho-binding
     domain."
     J. Biol. Chem. 271:13556-13560(1996).
     PubMed=8662891
[ 3] Bishop A.L., Hall A.
     "Rho GTPases and their effector proteins."
     Biochem. J. 348:241-255(2000).
     PubMed=10816416
[ 4] Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K.,
     Hakoshima T.
     "The structural basis of Rho effector recognition revealed by the
     crystal structure of human RhoA complexed with the effector domain of
     PKN/PRK1."
     Mol. Cell 4:793-803(1999).
     PubMed=10619026
[ 5] Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y.,
     Parker P.J., Blundell T.L., Mott H.R.
     "Molecular dissection of the interaction between the small G proteins
     Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)."
     J. Biol. Chem. 278:50578-50587(2003).
     PubMed=14514689; DOI=10.1074/jbc.M304313200
[ 6] Watson J.R., Fox H.M., Nietlispach D., Gallop J.L., Owen D.,
     Mott H.R.
     "Investigation of the Interaction between Cdc42 and Its Effector
     TOCA1: HANDOVER OF Cdc42 TO THE ACTIN REGULATOR N-WASP IS FACILITATED
     BY DIFFERENTIAL BINDING AFFINITIES."
     J. Biol. Chem. 291:13875-13890(2016).
     PubMed=27129201; DOI=10.1074/jbc.M116.724294

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}