H
IPR043136

B30.2/SPRY domain superfamily

InterPro entry
Short nameB30.2/SPRY_sf
Overlapping entries
 
B30.2/SPRY domain (IPR001870)
SPRY domain (IPR003877)
SPRY-associated (IPR006574)

Description

The B30.2 domain was first identified as a protein domain encoded by an exon (named B30-2) in the Homo sapiens class I major histocompatibility complex region
[4]
, whereas the SPRY domain was first identified in a Dictyostelium discoideum kinase splA and mammalian calcium-release channels ryanodine receptors
[5]
. B30.2 domain consists of PRY and SPRY subdomains. The SPRY domains (after SPla and the RYanodine Receptor) are shorter at the N terminus than the B30.2 domains. 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
[2]
. 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
[2]
. The B30.2/SPRY domain contains three highly conserved motifs (LDP, WEVE and LDYE)
[3]
. The B30.2/SPRY domain adopts a highly distorted, compact β-sandwich fold with two additional short β-helices at the N terminus. 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
[2]
. The 5th β-strand corresponding to WEVE motif
[1]
. Both the N- and C-terminal ends of the B30.2/SPRY domains in general are close to each other
[2]
.

This superfamily also matches diverse E3 ubiquitin-protein ligases. This protein is involved in the apoptosis process
[6, 7]
.

References

1.Protein fold analysis of the B30.2-like domain. Seto MH, Liu HL, Zajchowski DA, Whitlow M. Proteins 35, 235-49, (1999). View articlePMID: 10223295

2.Structural and functional insights into the B30.2/SPRY domain. Woo JS, Imm JH, Min CK, Kim KJ, Cha SS, Oh BH. EMBO J. 25, 1353-63, (2006). View articlePMID: 16498413

3.B30.2-like domain proteins: a growing family. Henry J, Ribouchon MT, Offer C, Pontarotti P. Biochem. Biophys. Res. Commun. 235, 162-5, (1997). View articlePMID: 9196055

4.Evolutionary study of multigenic families mapping close to the human MHC class I region. Vernet C, Boretto J, Mattei MG, Takahashi M, Jack LJ, Mather IH, Rouquier S, Pontarotti P. J. Mol. Evol. 37, 600-12, (1993). View articlePMID: 8114113

5.SPRY domains in ryanodine receptors (Ca(2+)-release channels). Ponting C, Schultz J, Bork P. Trends Biochem. Sci. 22, 193-4, (1997). View articlePMID: 9204703

6.TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. Lee SS, Fu NY, Sukumaran SK, Wan KF, Wan Q, Yu VC. Exp. Cell Res. 315, 1313-25, (2009). View articlePMID: 19100260

7.The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1. Huang NJ, Zhang L, Tang W, Chen C, Yang CS, Kornbluth S. J. Cell Biol. 197, 361-7, (2012). PMID: 22529100

Cross References

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