| Type: | Family | Name: | Chaperone tailless complex polypeptide 1 (TCP-1) |
| Description: | Protein folding is thought to be the sole result of properties inherent in polypeptide primary sequences. Sometimes, however, additional proteins are required to mediate correct folding and subsequent oligomer assembly []. These `helpers', or chaperones, bind to specific protein surfaces, preventing incorrect folding and formation of non-functional structures [].The tailless complex polypeptide 1 (TCP-1) is a highly structurally conserved molecular chaperone located in the cytosol []. The protein has also been shown to bind to Golgi membranes and to microtubules, this latter property suggesting a role in mitotic spindle formation in dividing cells (especially in sperm, where it is highly abundant) []. TCP-1 forms a double ring structure, similar to the 10kDa and 60kDa chaperonins, with 6-8 subunits per ring. The amino acid sequence is significantly similar to the 60kDa chaperonin, and to TF55, a chaperone from the archaebacterium Sulfolobus shibatae[]. | Short Name: | Chaperone_TCP-1 |
| DB identifier | Type | Name |
|---|---|---|
| IPR012721 | Family | T-complex protein 1, theta subunit |
| IPR012715 | Family | T-complex protein 1, alpha subunit |
| IPR012720 | Family | T-complex protein 1, eta subunit |
| IPR012722 | Family | T-complex protein 1, zeta subunit |
| IPR012718 | Family | T-complex protein 1, epsilon subunit |
| IPR012719 | Family | T-complex protein 1, gamma subunit |
| IPR012716 | Family | T-complex protein 1, beta subunit |
| IPR012717 | Family | T-complex protein 1, delta subunit |
| IPR012714 | Family | Thermosome, archaeal |
