SWAPSuppressor-of-White-APricot splicing regulator |
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| SMART accession number: | SM00648
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| Description: |
domain present in regulators which are responsible for pre-mRNA splicing processes |
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| Interpro abstract (IPR000061): |
SWAP is derived from the Suppressor-of-White-APricot splicing regulator from Drosophila melanogaster. The domain is found in regulators responsible for pervasive, nonsex-specific alternative pre-mRNA splicing characteristics and has been found in splicing regulatory proteins [(PUBMED:8206918)]. These ancient, conserved SWAP proteins share a colinearly arrayed series of novel sequence motifs [(PUBMED:7971282)].
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| GO process: | RNA processing (GO:0006396) |
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| GO function: | RNA binding (GO:0003723) |
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| Family alignment: |
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There are 906
SWAP domains in 609 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Binding / catalysis: RNA-binding
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Denhez F, Lafyatis R
- Conservation of regulated alternative splicing and identification of functional domains 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 possibly suppressor-of-sable, none of these have been identified in vertebrates. We describe 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 constitutive splicing factor, SPP91/PRP21. These modules thus define a new motif likely important in the regulatory and constitutive splicing functions of these proteins. The Drosophila su(wa) gene autoregulates its expression by control of splicing of its first two introns. Comparison of mammalian and Drosophila SWAP mRNAs revealed that the splice junctions of these regulated introns are precisely conserved, 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 (presumably autogenously) by control of splicing of these two introns. These several structural features therefore strongly suggest that the mammalian SWAP gene functions as a vertebrate alternative splicing regulator.
- Structure (3D structures containing this domain)
3D Structures of SWAP domains in PDB
| PDB code | Main view | Title | | 1ug0 |  | Solution structure of surp domain in bab30904 |
| 1x4o |  | Solution structure of surp domain in splicing factor 4 |
| 1x4p |  | Solution structure of surp domain in sfrs14 protei |
| 2dt6 |  | Solution structure of the first surp domain of human splicing factor sf3a120 |
| 2dt7 |  | Solution structure of the second surp domain of human splicing factor sf3a120 in complex with a fragment of human splicing factor sf3a60 |
| 2e5z |  | Solution structure of the surp2 domain in splicing factor, arginine/serine-rich 8 |
| 2e60 |  | Solution structure of the surp1 domain in splicing factor, arginine/serine-rich 8 |
- Links (links to other resources describing this domain)
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