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
IPR033162 is a Tubulin-folding cofactor D.
<p>The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [[cite:PUB00077898]].</p> <p>This entry represents tubulin-folding cofactor D (TBCD) and its homologues. Its ability to interact with beta tubulin is regulated via its interaction with ARL2 (ADP ribosylation factor-like protein 2), a small monomeric G protein. ARL2 inhibits the beta-tubulin GTPase activating protein (GAP) activity of TBCD, and its interaction with native tubulin dimers [[cite:PUB00010143], [cite:PUB00077911]].</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 | GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. | ||
| Biological process | Tubulin complex assembly | The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer. | ||
| Biological process | Post-chaperonin tubulin folding pathway | Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors. | ||
| Molecular function | Beta-tubulin binding | Interacting selectively and non-covalently with the microtubule constituent protein beta-tubulin. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: tubulin-specific chaperone D-like [Glycine max] gi|356534400|ref|XP_003535743.1| | 10 | ||
| – | PREDICTED: tubulin-specific chaperone D-like [Glycine max] gi|356534400|ref|XP_003535743.1| | 12 | ||
| – | PREDICTED: tubulin-specific chaperone D-like [Glycine max] gi|356574161|ref|XP_003555220.1| | 10 | ||
| – | Tubulin-folding cofactor d; TAIR: AT3G60740.1 ARM repeat superfamily protein; Swiss-Prot: sp|Q8L5R3|TBCD_ARATH Tubulin-folding cofactor D; TrEMBL-Plants: tr|A0A0B2PUP1|A0A0B2PUP1_GLYSO Tubulin-specific chaperone D; Found in the gene: LotjaGi5g1v0344800 | 11 | ||
| – | Tubulin-folding cofactor d; TAIR: AT3G60740.1 ARM repeat superfamily protein; Swiss-Prot: sp|Q8L5R3|TBCD_ARATH Tubulin-folding cofactor D; TrEMBL-Plants: tr|A0A0B2PUP1|A0A0B2PUP1_GLYSO Tubulin-specific chaperone D; Found in the gene: LotjaGi5g1v0344800 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 20.00 |