This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA [(PUBMED:8206918)]. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing. Most family members are associated with two SWAP (Surp) domains SM00648 and an Arginine- serine-rich binding region towards the C-terminus.
This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) splice factor proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA [ (PUBMED:8206918) ]. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing.
Family alignment:
There are 1975 DRY_EERY domains in 1973 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing DRY_EERY domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with DRY_EERY domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing DRY_EERY domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Conservation of regulated alternative splicing and identification of functionaldomains in vertebrate homologs to the Drosophila splicing regulator,suppressor-of-white-apricot.
J Biol Chem. 1994; 269: 16170-9
Display abstract
Although several splicing regulatory proteins have been identified in Drosophila through characterization of various genetic mutations, including sex-lethal,transformer, transformer-2, suppressor-of-white-apricot (su(wa)), and possiblysuppressor-of-sable, none of these have been identified in vertebrates. Wedescribe the cloning and characterization of human (HsSWAP) and mouse (MmSWAP)homologs of the su(wa) gene. Comparison of the Drosophila and mammalian proteins reveals five highly homologous regions, including an arginine/serine-rich domain and two repeated modules that are homologous to regions in the constitutivesplicing factor, SPP91/PRP21. These modules thus define a new motif likelyimportant in the regulatory and constitutive splicing functions of theseproteins. The Drosophila su(wa) gene autoregulates its expression by control ofsplicing of its first two introns. Comparison of mammalian and Drosophila SWAPmRNAs revealed that the splice junctions of these regulated introns are preciselyconserved, showing definitively that these genes are ancestrally related.Moreover, mammalian SWAP mRNAs are also alternatively spliced at the same splice sites, showing that mammalian SWAP expression is regulated (presumablyautogenously) by control of splicing of these two introns. These severalstructural features therefore strongly suggest that the mammalian SWAP genefunctions as a vertebrate alternative splicing regulator.
Links (links to other resources describing this domain)
