Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

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SWAP Suppressor-of-White-APricot splicing regulator

There are 584 SWAP domains in 382 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a SWAP domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with SWAP domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Binding / catalysis: RNA-binding

• Literature (relevant references for this domain)

• 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)

• PFAM	Surp
  INTERPRO	IPR000061