{PDOC00270}
{PS00298; HSP90}
{BEGIN}
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* Heat shock hsp90 proteins family signature *
**********************************************

Prokaryotic   and  eukaryotic  organisms   respond  to  heat  shock  or  other
environmental  stress  by  the  induction   of   the  synthesis   of  proteins
collectively known as heat-shock proteins (hsp) [1].  Amongst them is a family
of proteins,  with  an  average  molecular weight of 90 Kd, known as the hsp90
proteins. Proteins known to belong to this family are:

 - Escherichia coli and other bacteria heat shock protein c62.5 (gene htpG).
 - Vertebrate hsp 90-alpha (hsp 86) and hsp 90-beta (hsp 84).
 - Drosophila hsp 82 (hsp 83).
 - Trypanosoma cruzi hsp 85.
 - Plants Hsp82 or Hsp83.
 - Yeast and other fungi HSC82, and HSP82.
 - The endoplasmic reticulum  protein 'endoplasmin'  (also  known  as Erp99 in
   mouse, GRP94 in hamster, and hsp 108 in chicken).

The exact function of  hsp90  proteins is not yet known. In higher eukaryotes,
hsp90  has been found associated with steroid hormone receptors, with tyrosine
kinase oncogene  products of several retroviruses,  with eIF2alpha kinase, and
with actin  and  tubulin.  Hsp90  are probable chaperonins that possess ATPase
activity [2,3].

As a signature pattern for the  hsp90  family of  proteins, we have selected a
highly conserved region found in the N-terminal part of these proteins.

-Consensus pattern: Y-x-[NQHD]-[KHR]-[DE]-[IVA]-F-[LM]-R-[ED]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Lindquist S., Craig E.A.
     "The heat-shock proteins."
     Annu. Rev. Genet. 22:631-677(1988).
     PubMed=2853609; DOI=10.1146/annurev.ge.22.120188.003215
[ 2] Nadeau K., Das A., Walsh C.T.
     "Hsp90 chaperonins possess ATPase activity and bind heat shock
     transcription factors and peptidyl prolyl isomerases."
     J. Biol. Chem. 268:1479-1487(1993).
     PubMed=8419347
[ 3] Jakob U., Buchner J.
     "Assisting spontaneity: the role of Hsp90 and small Hsps as molecular
     chaperones."
     Trends Biochem. Sci. 19:205-211(1994).
     PubMed=7914036

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