{PDOC51867}
{PS51867; ZF_RING_GID}
{BEGIN}
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* Gid-type RING finger profile *
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The two  major antagonistic pathways of carbon metabolism in cells, glycolysis
and gluconeogenesis,   are  tigthly  regulated.  In  yeast,  the  switch  from
gluconeogenesis to  glycolysis  is brought about by proteasomal degradation of
the gluconeogenetic  enzyme  fructose-1.6-bisphosphate.  The  ubiquitin ligase
responsible for  polyubiquitylation  of  fructose-1,6-bisphophate  is  the Gid
(glucose induced  degradation  deficient)  complex.  This  complex consists of
seven subunits  of  which two, Gid2/Rmd5 and Gid9/Fyv10, contain a degenerated
RING finger  domain  (see  <PDOC00449>)  providing E3 ligase activity. The two
subunits form  the  heterodimaric  E3 ligase unit of the Gid complex [1,2]. An
orthologous complex,  called the CTLH complex is found in mammalian cells. The
CTLH complex has been linked to several different functions like regulation of
cell morphology,  proteasome-dependent degradation of non-ubiquitinated alpha-
catenin, or   modulation   of   endosome/lysosome-dependent   degradation   of
ubiquitinated proteins  via  interaction  with  HRS (hepatocyte growth factor-
regulated tyrosine kinase substrate) [3,4].

The degenerated  Gid-type RING finger is characterized by an incomplete series
of Zn(2+)  ion-coordinating  residues compared with the canonical RING finger,
which encompasses  eight  Cys/His  residues  coordinating  two  Zn  cations. A
complete cysteine and histidine pattern is not necessarily critical for the E3
function [1,2].

The profile we developed covers the entire Gid-type RING finger.

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

[ 1] Santt O., Pfirrmann T., Braun B., Juretschke J., Kimmig P., Scheel H.,
     Hofmann K., Thumm M., Wolf D.H.
     "The yeast GID complex, a novel ubiquitin ligase (E3) involved in the
     regulation of carbohydrate metabolism."
     Mol. Biol. Cell. 19:3323-3333(2008).
     PubMed=18508925; DOI=10.1091/mbc.e08-03-0328
[ 2] Braun B., Pfirrmann T., Menssen R., Hofmann K., Scheel H., Wolf D.H.
     "Gid9, a second RING finger protein contributes to the ubiquitin
     ligase activity of the Gid complex required for catabolite
     degradation."
     FEBS. Lett. 585:3856-3861(2011).
     PubMed=22044534; DOI=10.1016/j.febslet.2011.10.038
[ 3] Menssen R., Schweiggert J., Schreiner J., Kusevic D., Reuther J.,
     Braun B., Wolf D.H.
     "Exploring the topology of the Gid complex, the E3 ubiquitin ligase
     involved in catabolite-induced degradation of gluconeogenic enzymes."
     J. Biol. Chem. 287:25602-25614(2012).
     PubMed=22645139; DOI=10.1074/jbc.M112.363762
[ 4] Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
     Picotti P., Stoffel M., Peter M.
     "The multi-subunit GID/CTLH E3 ligase promotes proliferation and
     targets the transcription factor Hbp1 for degradation."
     Elife 7:0-0(2018).
     PubMed=29911972; DOI=10.7554/eLife.35528

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