{PDOC50913}
{PS50913; GRIP}
{BEGIN}
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* GRIP domain profile *
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Golgins  are  Golgi-localized  proteins  that  have  an  extended  coiled-coil
conformation, and play an important role in maintaining Golgi structure in all
eukaryotic  cells  from  yeast  to  humans.  A subset of the golgins contain a
carboxy-terminal  region,  called  the  GRIP  domain, that mediates binding to
Golgi membranes. The GRIP domain was named after the four proteins in which it
is found and about which something has been reported (golgin-97, RanBP2-alpha,
Imh1p and p230/golgin-245) [1,2].

ARL1 and ARL3 are required  for  localization of GRIP-domain proteins to Golgi
membranes.  ARL1-GTP interacts specifically with the GRIP domain to recruit it
to membranes,  and  ARL3 is required for normal Golgi localization of ARL1 [3,
4].

The profile we developed covers the whole GRIP domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 2003 / First entry.

[ 1] Munro S., Nichols B.J.
     "The GRIP domain - a novel Golgi-targeting domain found in several
     coiled-coil proteins."
     Curr. Biol. 9:377-380(1999).
     PubMed=10209120
[ 2] Jackson C.L.
     "Membrane traffic: Arl GTPases get a GRIP on the Golgi."
     Curr. Biol. 13:R174-R176(2003).
     PubMed=12620205
[ 3] Panic B., Whyte J.R., Munro S.
     "The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts
     with vesicle-tethering factors at the Golgi apparatus."
     Curr. Biol. 13:405-410(2003).
     PubMed=12620189
[ 4] Setty S.R., Shin M.E., Yoshino A., Marks M.S., Burd C.G.
     "Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is
     regulated by Arf-like GTPase 3."
     Curr. Biol. 13:401-404(2003).
     PubMed=12620188

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