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15  structures 399  species 1  interaction 650  sequences 9  architectures

Family: TCTP (PF00838)

Summary: Translationally controlled tumour protein

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Translationally controlled tumour protein Edit Wikipedia article

TCTP
PDB 1h7y EBI.jpg
translationally controlled tumor-associated protein p23fyp from schizosaccharomyces pombe
Identifiers
Symbol TCTP
Pfam PF00838
Pfam clan CL0080
InterPro IPR018105
PROSITE PDOC00768
SCOP 1h7y
SUPERFAMILY 1h7y
Translationally Controlled Tumour Protein
Identifiers
Symbol FLJ27337,tpt1,HRF, p02, p23, p21
OMIM 600763

In molecular biology, the protein TCTP, is short for translationally controlled tumour protein (TCTP).The translationally controlled tumour protein, commonly known as TCTP, is a highly conserved protein among many eukaryotic organisms.[1] TCTP is involved in a variety of cellular activities, including microtubule stabilization, calcium-binding activities, and apoptosis.[1] The Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour,[2][3] but which is also expressed in normal cells. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TCTP has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TCTP production is thought to be controlled at the translational as well as the transcriptional level.[4]

Conservation[edit]

TCTP is a hydrophilic protein of 18 to 20 kD. TCTPs do not share significant sequence similarity with any other class of proteins. Recently, the structure of TCTP was determined and exhibited significant structural similarity to the human protein Mss4, which is a guanine nucleotide-free chaperone of the Rab protein.[5] Translationally controlled tumor protein (TCTP) is a highly conserved protein found in eukaryotes, across animal and plant kingdoms and even in yeast. Close homologues have been found in plants,[6] earthworm,[7] Caenorhabditis elegans (F52H2.11), Hydra, Saccharomyces cerevisiae (YKL056c) [8] and Schizosaccharomyces pombe (SpAC1F12.02c). Mammalian TCTP is ubiquitously expressed in various tissues and cell types.

Function[edit]

Translationally-controlled tumor-associated protein (TCTP) has many roles in cellular processes, most notably in the following:

In essence, TCTP functions as molecule that prevents cell death. It reduces cellular stress working as a heat shock protein and a molecular chaperone. It prevents cell death by binding to calcium, an ion that causes cell death. Furthermore, the N-terminal domain of TCTP inhibits apoptosis by binding to apoptotic factors and by inhibiting p53 tumour suppressor-dependent apoptosis by downregulating it.[9]

TCTP interacts with F-actin and regulates cell shape by interacting with the cytoskeleton. Since most cellular processes, such as the cell cycle and cancer, involve changes in the cytoskeleton; it becomes apparent why TCTP is important. Moreover, if the gene encoding TCTP is knocked-out in mice, it becomes embryonic lethal, and they die in utero (in the womb).[10]

Structure[edit]

This structure has a very complex topology composed of four beta-sheets and three alpha helices.[5]

References[edit]

  1. ^ a b Ulrich-Axel Bommer, Bernd-Joachim Thiele (2004). "The translationally controlled tumour protein (TCTP)". IJBCB 36 (3): 379–385. doi:10.1016/S1357-2725(03)00213-9. PMID 14687915. 
  2. ^ Böhm H, Benndorf R, Gaestel M, Gross B, Nürnberg P, Kraft R, Otto A, Bielka H (August 1989). "The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure". Biochem. Int. 19 (2): 277–86. PMID 2479380. 
  3. ^ Chitpatima ST, Makrides S, Bandyopadhyay R, Brawerman G (March 1988). "Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells". Nucleic Acids Res. 16 (5): 2350. doi:10.1093/nar/16.5.2350. PMC 338237. PMID 3357792. 
  4. ^ Thiele H, Berger M, Skalweit A, Thiele BJ (September 2000). "Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP)". Eur. J. Biochem. 267 (17): 5473–81. PMID 10951206. 
  5. ^ a b Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ (August 2001). "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones". Nat. Struct. Biol. 8 (8): 701–4. doi:10.1038/90415. PMID 11473261. 
  6. ^ Pay A, Heberle-Bors E, Hirt H (June 1992). "An alfalfa cDNA encodes a protein with homology to translationally controlled human tumor protein". Plant Mol. Biol. 19 (3): 501–3. PMID 1623194. 
  7. ^ Stürzenbaum SR, Kille P, Morgan AJ (July 1998). "Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellus1". Biochim. Biophys. Acta 1398 (3): 294–304. PMID 9655922. 
  8. ^ Rasmussen SW (April 1994). "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins". Yeast. 10 Suppl A: S63–8. doi:10.1002/yea.320100008. PMID 8091862. 
  9. ^ Nagano-Ito M, Ichikawa S (2012). "Biological effects of Mammalian translationally controlled tumor protein (TCTP) on cell death, proliferation, and tumorigenesis.". Biochem Res Int 2012: 204960. doi:10.1155/2012/204960. PMC 3364544. PMID 22675633. 
  10. ^ Bazile F, Pascal A, Arnal I, Le Clainche C, Chesnel F, Kubiak JZ (2009). "Complex relationship between TCTP, microtubules and actin microfilaments regulates cell shape in normal and cancer cells.". Carcinogenesis 30 (4): 555–65. doi:10.1093/carcin/bgp022. PMC 2831045. PMID 19168579. 

This article incorporates text from the public domain Pfam and InterPro IPR018105

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018105

Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour [PUBMED:2479380, PUBMED:3357792], but which is also expressed in normal cells. The physiological function of TCTP is still not known. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TCTP has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TCTP production is thought to be controlled at the translational as well as the transcriptional level [PUBMED:10951206].

TCTP is a hydrophilic protein of 18 to 20 kD. TCTPs do not share significant sequence similarity with any other class of proteins. Recently, the structure of TCTP was determined and exhibited significant structural similarity to the human protein Mss4, which is a guanine nucleotide-free chaperone of the Rab protein [PUBMED:11473261]. Close homologues have been found in plants [PUBMED:1623194], earthworm [PUBMED:9655922], Caenorhabditis elegans (F52H2.11), Hydra, Saccharomyces cerevisiae (YKL056c) [PUBMED:8091862] and Schizosaccharomyces pombe (SpAC1F12.02c).

Domain organisation

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Pfam Clan

This family is a member of clan Mss4-like (CL0080), which has the following description:

This clan contains TCTP, Mss4 and SelR families [1].

The clan contains the following 3 members:

Mss4 SelR TCTP

Alignments

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(147)
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RP75
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  Seed
(9)
Full
(650)
Representative proteomes NCBI
(645)
Meta
(3)
RP15
(93)
RP35
(147)
RP55
(215)
RP75
(320)
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  Seed
(9)
Full
(650)
Representative proteomes NCBI
(645)
Meta
(3)
RP15
(93)
RP35
(147)
RP55
(215)
RP75
(320)
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Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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External links

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_1548 (release 2.1)
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 9
Number in full: 650
Average length of the domain: 149.40 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 92.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 21.2 21.9
Noise cut-off 20.7 20.7
Model length: 165
Family (HMM) version: 12
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Species distribution

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Interactions

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TCTP

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TCTP domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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