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PROSITE documentation PDOC50188 [for PROSITE entry PS50188]

B30.2/SPRY domain profile





Description

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 β-sandwich fold with two additional short α-helices at the N-terminus (see <PDB:2FNJ>). The β-sandwich of the B30.2/SPRY domain consists of two layers of β-sheets: sheet A composed of eight strands and sheet B composed of seven strands. All the β-strands are in antiparallel arrangement [3]. The 5th β-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 α and β 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.

Last update:

April 2006 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

B302_SPRY, PS50188; B30.2/SPRY domain profile  (MATRIX)


References

1AuthorsVernet C. Boretto J. Mattei M.G. Takahashi M. Jack L.J. Mather I.H. Rouquier S. Pontarotti P.
TitleEvolutionary study of multigenic families mapping close to the human MHC class I region.
SourceJ. Mol. Evol. 37:600-612(1993).
PubMed ID8114113

2AuthorsPonting C. Schultz J. Bork P.
TitleSPRY domains in ryanodine receptors (Ca(2+)-release channels).
SourceTrends Biochem. Sci. 22:193-194(1997).
PubMed ID9204703

3AuthorsWoo J.-S. Imm J.-H. Min C.-K. Kim K.-J. Cha S.-S. Oh B.-H.
TitleStructural and functional insights into the B30.2/SPRY domain.
SourceEMBO J. 25:1353-1363(2006).
PubMed ID16498413
DOI10.1038/sj.emboj.7600994

4AuthorsHenry J. Ribouchon M.-T. Offer C. Pontarotti P.
TitleB30.2-like domain proteins: a growing family.
SourceBiochem. Biophys. Res. Commun. 235:162-165(1997).
PubMed ID9196055
DOI10.1006/bbrc.1997.6751

5AuthorsSeto M.H. Liu H.-L.C. Zajchowski D.A. Whitlow M.
TitleProtein fold analysis of the B30.2-like domain.
SourceProteins 35:235-249(1999).
PubMed ID10223295
DOI10.1002/(SICI)1097-0134(19990501)35:2<235::AID-PROT9>3.0.CO;2-X



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