Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR001298 is a Filamin/ABP280 repeat.
<p>The many different actin cross-linking proteins share a common architecture, consisting of a globular actin-binding domain and an extended rod. Whereas their actin-binding domains consist of two calponin homology domains (see [interpro:IPR001715]), their rods fall into three families.</p> <p>The rod domain of the family including the Dictyostelium discoideum (Slime mould) gelation factor (ABP120) and human filamin (ABP280) is constructed from tandem repeats of a 100-residue motif that is glycine and proline rich [[cite:PUB00003939]]. The gelation factor's rod contains 6 copies of the repeat, whereas filamin has a rod constructed from 24 repeats. The resolution of the 3D structure of rod repeats from the gelation factor has shown that they consist of a β-sandwich, formed by two β-sheets arranged in an immunoglobulin-like fold [[cite:PUB00003939], [cite:PUB00010567]]. Because conserved residues that form the core of the repeats are preserved in filamin, the repeat structure should be common to the members of the gelation factor/filamin family.</p> <p>The head to tail homodimerisation is crucial to the function of the ABP120 and ABP280 proteins. This interaction involves a small portion at the distal end of the rod domains. For the gelation factor it has been shown that the carboxy-terminal repeat 6 dimerises through a double edge-to-edge extension of the β-sheet and that repeat 5 contributes to dimerisation to some extent [[cite:PUB00010566], [cite:PUB00010567], [cite:PUB00010568]].</p>
This description is obtained from EB-eye REST.
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 , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Protein binding | Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | RNA recognition motif-containing protein isoform 2 [Theobroma cacao] gi|508713270|gb|EOY05167.1| | 23 | ||
| – | RNA recognition motif (RRM)-containing protein; TAIR: AT3G23900.1 RNA recognition motif (RRM)-containing protein; Swiss-Prot: sp|Q9LRR6|CID9_ARATH Polyadenylate-binding protein-interacting protein 9; TrEMBL-Plants: tr|V7C647|V7C647_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0372200 | 24 | ||
| – | RNA recognition motif (RRM)-containing protein; TAIR: AT3G23900.1 RNA recognition motif (RRM)-containing protein; Swiss-Prot: sp|Q9LRR6|CID9_ARATH Polyadenylate-binding protein-interacting protein 9; TrEMBL-Plants: tr|V7C647|V7C647_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0372200 | 24 | ||
| – | RNA recognition motif (RRM)-containing protein; TAIR: AT3G23900.1 RNA recognition motif (RRM)-containing protein; Swiss-Prot: sp|Q9LRR6|CID9_ARATH Polyadenylate-binding protein-interacting protein 9; TrEMBL-Plants: tr|V7C647|V7C647_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0372200 | 24 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 25.00 |