{PDOC50188}
{PS50188; B302_SPRY}
{BEGIN}
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* B30.2/SPRY domain profile *
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The B30.2  domain  was first identified as a protein domain encoded by an exon
(named B30-2)  in  the  human  class I major histocompatibility complex region
[1], whereas   the  SPRY  domain  was  first  identified  in  a  Dictyostelium
discoideum kinase  splA   and   mammalian calcium-release  channels  ryanodine
receptors [2].  The  SPRY domains are shorter at the N-terminus than the B30.2
domains and  appear  as a subdomain of the latter. The ~200-residue B30.2/SPRY
(for B30.2  and/or  SPRY) domain is present in a large number of proteins with
diverse individual functions in different biological processes. The B30.2/SPRY
domain in  these  proteins  is  likely  to  function  through  protein-protein
interaction [3].

The N-terminal ~60 residues of B30.2/SPRY domains are poorly conserved and, as
a consequence,  a  new  domain  name  PRY  was  coined  for a group of similar
sequence segments  N-terminal  to  the SPRY domains [3]. The B30.2/SPRY domain
contains three   highly  conserved  motifs  (LDP,  WEVE  and  LDYE)  [4].  The
B30.2/SPRY domain  adopts  a highly distorted, compact beta-sandwich fold with
two additional  short  alpha-helices  at  the N-terminus (see <PDB:2FNJ>). The
beta-sandwich of  the B30.2/SPRY domain consists of two layers of beta-sheets:
sheet A  composed  of eight strands and sheet B composed of seven strands. All
the beta-strands  are  in  antiparallel  arrangement  [3]. The 5th beta-strand
corresponding to  WEVE  motif  [5].  Both  the  N-  and C-terminal ends of the
B30.2/SPRY domains in general are close to each other [3].

Some proteins known to contain a B30.2/SPRY domain are listed below:

 - Dictyostelium  discoideum  splA,  a  dual-specificity kinase that regulates
   spore cell differentiation.
 - Ryanodine  receptors  (RyRs),  involved  in  the  release of Ca2+ ions from
   intracellular stores.
 - SPRY  domain-containing  proteins  with a SOCS boc (SSB). The SOCS proteins
   appear to  form  part  of a classical negative feedback loop that regulates
   cytokine signal transduction.
 - Proteins  of  the  RBCC (RING-finger, B-box and coiled-coil domain) family,
   such as  Sjoegren syndrom type-A or Ro/SS-A antigen, Xenopus nuclear factor
   7 (Xnf7) and pyrin/marenostrin.
 - Proteins  of  the  butyrophilin-related  family. Butyrophilin is a membrane
   protein expressed  in  milk fat globule membrane. Its SPRY domain is linked
   to two  external  immunoglobulin-like  motifs  by  a  single  transmembrane
   segment.
 - Enterophilins,   a  family  of  leucine  zipper  proteins  associated  with
   enterocyte differentiation.
 - The  alpha and beta subunits of stonustoxin (STNX), a secreted protein that
   was purified from the venom of stonefish (Synanceja horrida).

The profile we developed covers the entire B30.2/SPRY domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / First entry.

[ 1] Vernet C., Boretto J., Mattei M.G., Takahashi M., Jack L.J.,
     Mather I.H., Rouquier S., Pontarotti P.
     "Evolutionary study of multigenic families mapping close to the human
     MHC class I region."
     J. Mol. Evol. 37:600-612(1993).
     PubMed=8114113
[ 2] Ponting C., Schultz J., Bork P.
     "SPRY domains in ryanodine receptors (Ca(2+)-release channels)."
     Trends Biochem. Sci. 22:193-194(1997).
     PubMed=9204703
[ 3] Woo J.-S., Imm J.-H., Min C.-K., Kim K.-J., Cha S.-S., Oh B.-H.
     "Structural and functional insights into the B30.2/SPRY domain."
     EMBO J. 25:1353-1363(2006).
     PubMed=16498413; DOI=10.1038/sj.emboj.7600994
[ 4] Henry J., Ribouchon M.-T., Offer C., Pontarotti P.
     "B30.2-like domain proteins: a growing family."
     Biochem. Biophys. Res. Commun. 235:162-165(1997).
     PubMed=9196055; DOI=10.1006/bbrc.1997.6751
[ 5] Seto M.H., Liu H.-L.C., Zajchowski D.A., Whitlow M.
     "Protein fold analysis of the B30.2-like domain."
     Proteins 35:235-249(1999).
     PubMed=10223295; DOI=10.1002/(SICI)1097-0134(19990501)35:2<235::AID-PROT9>3.0.CO;2-X

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