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IPR012715 is a T-complex protein 1, alpha subunit.
<p>This family consists exclusively of the CCT alpha subunit (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.</p> <p>Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [[cite:PUB00004127], [cite:PUB00001019]]. Chaperonins are involved in productive folding of proteins [[cite:PUB00080867]]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome [[cite:PUB00080871]]. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [[cite:PUB00004124]], related to the cpn60/groEL chaperonin family (see [interpro:IPR001844]).</p> <p>The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place [[cite:PUB00074264]]. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle [[cite:PUB00004129]] with 6 to 8 other different, but homologous, subunits [[cite:PUB00064264]]. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [[cite:PUB00001034], [cite:PUB00005432]]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [[cite:PUB00080868], [cite:PUB00080869], [cite:PUB00080873]]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [[cite:PUB00074265], [cite:PUB00074266]].</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 | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Biological process | Protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. | ||
| Molecular function | Unfolded protein binding | Interacting selectively and non-covalently with an unfolded protein. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: T-complex protein 1 subunit alpha-like [Cicer arietinum] gi|502140465|ref|XP_004504226.1| | 22 | ||
| – | T-complex protein 1 subunit alpha; TAIR: AT3G20050.1 T-complex protein 1 alpha subunit; Swiss-Prot: sp|P28769|TCPA_ARATH T-complex protein 1 subunit alpha; TrEMBL-Plants: tr|A0A0L9TJL4|A0A0L9TJL4_PHAAN Uncharacterized protein; Found in the gene: LotjaGi4g1v0384900 | 22 | ||
| – | T-complex protein 1 subunit alpha; TAIR: AT3G20050.1 T-complex protein 1 alpha subunit; Swiss-Prot: sp|P28769|TCPA_ARATH T-complex protein 1 subunit alpha; TrEMBL-Plants: tr|A0A0L9TJL4|A0A0L9TJL4_PHAAN Uncharacterized protein; Found in the gene: LotjaGi4g1v0384900 | 21 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd03335 | CDD | 1 | 33.33 |