Description

IPR003877 is a SPRY domain.

<p>The SPRY domain is a ~140-amino-acid protein interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity, or embryonic development [[cite:PUB00041714], [cite:PUB00085899], [cite:PUB00095661]]. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. Functionally, SPRY domains mediate critical interactions in diverse pathways: SSB-2 binds Par-4 to regulate apoptosis, RanBPM/SSB-1 interact with c-Met for signalling modulation, and SPSB proteins target iNOS for ubiquitination in immune regulation [[cite:PUB00039269], [cite:PUB00086126], [cite:PUB00130360]].</p> <p>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 [[cite:PUB00033710]], whereas the SPRY domain was first identified in a Dictyostelium discoideum kinase splA and mammalian calcium-release channels ryanodine receptors [[cite:PUB00005467]]. 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 [[cite:PUB00033711]]. 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 [[cite:PUB00033711]]. The B30.2/SPRY domain contains three highly conserved motifs (LDP, WEVE and LDYE) [[cite:PUB00033712]]. 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 [[cite:PUB00033711]]. The 5th β-strand corresponding to WEVE motif [[cite:PUB00033713]]. Both the N- and C-terminal ends of the B30.2/SPRY domains in general are close to each other [[cite:PUB00033711]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: