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PROSITE documentation PDOC50188B30.2/SPRY domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC50188
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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Vernet C. Boretto J. Mattei M.G. Takahashi M. Jack L.J. Mather I.H. Rouquier S. Pontarotti P. |
| Title | Evolutionary study of multigenic families mapping close to the human MHC class I region. | |
| Source | J. Mol. Evol. 37:600-612(1993). | |
| PubMed ID | 8114113 |
| 2 | Authors | Ponting C. Schultz J. Bork P. |
| Title | SPRY domains in ryanodine receptors (Ca(2+)-release channels). | |
| Source | Trends Biochem. Sci. 22:193-194(1997). | |
| PubMed ID | 9204703 |
| 3 | Authors | Woo J.-S. Imm J.-H. Min C.-K. Kim K.-J. Cha S.-S. Oh B.-H. |
| Title | Structural and functional insights into the B30.2/SPRY domain. | |
| Source | EMBO J. 25:1353-1363(2006). | |
| PubMed ID | 16498413 | |
| DOI | 10.1038/sj.emboj.7600994 |
| 4 | Authors | Henry J. Ribouchon M.-T. Offer C. Pontarotti P. |
| Title | B30.2-like domain proteins: a growing family. | |
| Source | Biochem. Biophys. Res. Commun. 235:162-165(1997). | |
| PubMed ID | 9196055 | |
| DOI | 10.1006/bbrc.1997.6751 |
| 5 | Authors | Seto M.H. Liu H.-L.C. Zajchowski D.A. Whitlow M. |
| Title | Protein fold analysis of the B30.2-like domain. | |
| Source | Proteins 35:235-249(1999). | |
| PubMed ID | 10223295 | |
| DOI | 10.1002/(SICI)1097-0134(19990501)35:2<235::AID-PROT9>3.0.CO;2-X |
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