InterPro : IPR017998

Name  Chaperone tailless complex polypeptide 1 (TCP-1) Short Name  Chaperone_TCP-1
Type  Family 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[].
Quick Links:
Quick Links:


InterPro protein domain ID --> Contigs


GO Displayer



8 Child Features

Id Name Short Name Type
IPR012719 T-complex protein 1, gamma subunit Chap_CCT_gamma Family
IPR012720 T-complex protein 1, eta subunit Chap_CCT_eta Family
IPR012721 T-complex protein 1, theta subunit Chap_CCT_theta Family
IPR012716 T-complex protein 1, beta subunit Chap_CCT_beta Family
IPR012722 T-complex protein 1, zeta subunit Chap_CCT_zeta Family
IPR012718 T-complex protein 1, epsilon subunit Chap_CCT_epsi Family
IPR012717 T-complex protein 1, delta subunit Chap_CCT_delta Family
IPR012714 Thermosome, archaeal Thermosome_arc Family

1 Contains

Id Name Short Name Type
IPR002194 Chaperonin TCP-1, conserved site Chaperonin_TCP-1_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002423 Chaperonin Cpn60/TCP-1 Cpn60/TCP-1 Family

4 Publications

First Author Title Year Journal Volume Pages
Hemmingsen SM Homologous plant and bacterial proteins chaperone oligomeric protein assembly. 1988 Nature 333 330-4
Trent JD A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. 1991 Nature 354 490-3
Mori M Cloning of a cDNA encoding the Tcp-1 (t complex polypeptide 1) homologue of Arabidopsis thaliana. 1992 Gene 122 381-2
Ursic D Is yeast TCP1 a chaperonin? 1992 Nature 356 392

To cite PlanMine, please refer to the following publication:

Brandl, H., Moon, H., Vila-Farré, M., Liu, S.-Y., Henry, I., & Rink, J. C.
PlanMine - a mineable resource of planarian biology and biodiversity.
Nucleic Acids Research, gkv1148. doi:10.1093/nar/gkv1148 (2015)