Chaperonin TCP-1, conserved site
IPR002194
Definition
The TCP-1 protein [[cite:PMID:1352857], [cite:PMID:15335898]] (Tailless Complex Polypeptide 1) 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. 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 PMID:1630492 with 6 to 8 other different subunits. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [[cite:PMID:7953530], [cite:PMID:7846767]]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins. The CCT subunits are highly related to archaebacterial counterparts: TF55 and TF56 PMID:1836250, a molecular chaperone from Sulfolobus shibatae. TF55 has ATPase activity, is known to bind unfolded polypeptides and forms a oligomeric complex of two stacked nine-membered rings. Thermosome PMID:7794526, from Thermoplasma acidophilum. The thermosome is composed of two subunits (alpha and beta) and also seems to be a chaperone with ATPase activity. It forms an oligomeric complex of eight-membered rings. The TCP-1 family of proteins are weakly, but significantly PMID:1352040, related to the cpn60/groEL chaperonin family (see [interpro:IPR001844]).
9 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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