{PDOC00768} {PS01002; TCTP_1} {PS01003; TCTP_2} {PS51797; TCTP_3} {BEGIN} ********************************************************************************* * Translationally controlled tumor protein (TCTP) domain signatures and profile * ********************************************************************************* The translationally controlled tumor proteins (TCTPs, such as p21, p23 and histamine releasing factor (HRF)) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in a variety of cellular functions, including microtubule stabilization, cell cycle, apoptosis, and cytokine release. TCTP is ubiquitously expressed in all eukaryotic organisms from protozoa such as Plasmodium sp. to plants and mammals [1,2,3,4]. The TCTP domain structure comprises four beta-sheets, designated A-D, and three main helices, designated H1-H3, connected in a complex topology (see ). A central feature of the structure is the four-stranded sheet A, against one face of which packs the three-stranded sheet B and the small helix H1. Helix H3 packs against part of the opposite face of sheet A. Helix H2 packs against helix H3 (forming an alpha-helical hairpin). The final major structural feature is the two-stranded sheet C, which protrudes from the core globular structure formed by the rest of the domain [1]. As signature patterns for the TCTP domain, we selected two of the best conserved regions. We also developed a profile that covers the entire TCTP domain. -Consensus pattern: [IFAED]-[GA]-[GASF]-N-[PAK]-S-[GTA]-E-[GDEVCF]-[PAGEQV]- [DEQGAV] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [FLIV]-x(4)-[FLVH]-[FY]-[MIVCT]-G-E-x(4,7)-[DENP]-[GAST]- x-[LIVM]-[GAVI]-x(3)-[FYWQ] -Sequences known to belong to this class detected by the pattern: ALL, except for the hydra TCTP. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: May 2016 / Text revised; profile added. [ 1] Thaw P., Baxter N.J., Hounslow A.M., Price C., Waltho J.P., Craven C.J. "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones." Nat. Struct. Biol. 8:701-704(2001). PubMed=11473261; DOI=10.1038/90415 [ 2] Choi K.-W., Hsu Y.-C. "To cease or to proliferate: new insights into TCTP function from a Drosophila study." Cell Adh. Migr. 1:129-130(2007). PubMed=19262129 [ 3] Susini L., Besse S., Duflaut D., Lespagnol A., Beekman C., Fiucci G., Atkinson A.R., Busso D., Poussin P., Marine J.-C., Martinou J.-C., Cavarelli J., Moras D., Amson R., Telerman A. "TCTP protects from apoptotic cell death by antagonizing bax function." Cell Death Differ. 15:1211-1220(2008). PubMed=18274553; DOI=10.1038/cdd.2008.18 [ 4] Eichhorn T., Winter D., Buchele B., Dirdjaja N., Frank M., Lehmann W.D., Mertens R., Krauth-Siegel R.L., Simmet T., Granzin J., Efferth T. "Molecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum." Biochem. Pharmacol. 85:38-45(2013). PubMed=23085438; DOI=10.1016/j.bcp.2012.10.006 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}