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Txnl1  -  thioredoxin-like 1

Rattus norvegicus

Synonyms: Thioredoxin-like protein 1, Thioredoxin-related protein, Trp
 
 
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Disease relevance of Txnl1

  • For these studies, all 4 Trp residues of rat CRBP II were efficiently labeled with 6-fluorotryptophan (6-F-Trp) by inducing its expression in a tryptophan auxotroph of Escherichia coli [1].
  • These results indicate that the substitution of Arg180 by Trp impairs the cleavage by factor XIa required for activation of this zymogen and that the substitution causes hemophilia BM [2].
  • In rats, hepatocellular carcinomas were induced by Trp-P-1, Glu-P-1, Glu-P-2, and IQ [3].
  • Uptake of heterocyclic amines, Trp-P-1 and Trp-P-2, into clonal rat pheochromocytoma PC12h cells by dopamine uptake system [4].
  • In total, 75 phage clones carrying 43 different peptides were analyzed of which 42 clones carrying 17 different peptides, twelve 12mer and five 7mer peptides, presented a single consensus motif: Leu(Ile, Val)-Tyr(Phe, Trp, Leu)-Gly-Met(Ala) [5].
 

Psychiatry related information on Txnl1

  • The administration of tryptophan (Trp, 150 mg/kg i.p.) 28 h after PCPA pretreatment, causing a significant rise in the brain serotonin (5-HT) concentration, produced a temporary increase in SWS and REMS, and a reduction of motor activity [6].
 

High impact information on Txnl1

  • We show here, by yeast two-hybrid screenings and biochemical assays, that a region at the amino terminus of the human nuclear pore complex protein Nup96 interacts with the WD (Trp-Asp) repeat region of human Sec13 [7].
  • This was not due to the simple replacement of amino acid Arg406 with Trp close to the phosphorylation site, because Ser404 in a R406W peptide was equally phosphorylated in a wild-type peptide [8].
  • The difference in the binding affinity of myristoylated and non-myristoylated proteins to Ca(2+) also was reflected by Trp fluorescence [9].
  • We subsequently determined that the C-6 position of the indole moiety in the N-terminal Trp was brominated [10].
  • Substitution of Tyr or His for Phe-707, but not Leu, Val, Glu, or Trp, partially restored the ability of high [Ca(2+)](o) to activate PLC [11].
 

Chemical compound and disease context of Txnl1

  • Amino acids Arg 101, Asn 106, and Met 305 make no contacts with the inhibitor in the open conformation, unlike the equivalent residues in the E. coli protein (Thr 78, Trp 83, and Val 262). dUMP binding is similar in both proteins, except that there is no covalent adduct to the active site cysteine (Cys 189) in the rat structures [12].
  • They inhibited type A monoamine oxidase more markedly than type B. After culture of a dopamine cell model, clonal pheochromocytoma PC12h cells, with Trp-P-1 activity of tyrosine hydroxylase was decreased by reduction of its affinity to the biopterin cofactor [13].
 

Biological context of Txnl1

  • We have found that other proteins containing these thioredoxin-like active site sequences do not bind the photoreactive peptide probes [14].
  • Rat parvalbumin (PV), an EF-hand type Ca(2+)-binding protein, was expressed in Escherichia coli and mutated by replacing a Phe at position 102 with a unique Trp in order to introduce a distinct fluorescent label into the protein [15].
  • Taking advantage of the Trp residues in the host protein, we first determined metal-binding affinities for Tb3+, Ca2+, and La3+ for all four grafted EF-loops using Tb3+ aromatic resonance energy transfer [16].
  • We conclude that the conserved Trp (1) has similar roles in two different NOS isozymes and (2) regulates delivery of both electrons required for O(2) activation (i.e., kinetics of ferric heme reduction by the NOS flavoprotein domain and reduction of the heme-dioxy intermediate by H(4)B) [17].
  • Thus, we describe a novel interaction between Trp proteins and InsP3R and we provide evidence suggesting that the formation of hTrp4-InsP3R complexes may be regulated by alternative splicing [18].
 

Anatomical context of Txnl1

  • The T3 and Trp transport activities of sheep erythrocytes were undetectable [19].
  • Binding of double-stranded calf thymus DNA brings about a moderate quenching of the Tyr and Trp fluorescence emission of both the 31-kDa fragment and beta-polymerase and induces a 6-nm blue shift in the Trp emission maximum of the intact enzyme, but not in the fragment [20].
  • The amino acid control of macroautophagy in the hepatocyte is accomplished by a small group of direct inhibitors (Leu, Tyr/Phe, Gln, Pro, Met, Trp, and His) and the permissive effect of alanine whereas only leucine is involved in myocytes and adipocytes [21].
  • The normally labile ornithine decarboxylase (ODC) becomes unusually stable when Cys-441 is replaced with Trp in the variant cell lines HMOA and DH23b [22].
  • Studies with analogs of this sequence indicated that residues, Leu 111, Phe 114 and Trp 116 are important for T-cell responsiveness [23].
 

Associations of Txnl1 with chemical compounds

  • Converting each Trp residue to Phe and Gly by site-directed mutagenesis allowed us to study the role of these invariant tryptophan residues [24].
  • Intracellular protein degradation in perfused livers of fed rats has been shown to be directly regulated by 7 amino acids (Leu, Tyr, Gln, Pro, Met, His, and Trp) and co-regulated by alanine [25].
  • Similar inhibition was obtained with a known regulatory amino acid mixture (Leu, Met, Pro, Trp, and His), whereas leucine alone (0.8 mM) decreased degradation by 47% [26].
  • Unlabeled aromatic amino acids (e.g. Trp, phenylalanine, tyrosine) competitively inhibited [125I]T3 uptake and unlabeled iodothyronine analogues (e.g. T3, D-T3, thyroxine, thyronine) competitively inhibited [3H]Trp uptake [19].
  • Component I has the amino acid composition Lys6, His, Arg2, Cys3, Asp5, Asn2, Thr3, Ser4, Glu13, Gln3, Pro3, Gly2, Ala6, Val9, Met4, Ile4, Leu8, Tyr6, Phe3, Trp, with serine and asparagine as NH2(-) and COOH-terminal amino acids, respectively [27].
 

Other interactions of Txnl1

 

Analytical, diagnostic and therapeutic context of Txnl1

  • Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa [29].
  • We have studied the membrane organization and dynamics underlying this coupling specificity by using Trp channels as biosensors for real-time detection of PLCbeta products [30].
  • Site-directed mutagenesis was used to generate human and mouse C5aRs with a residue exchange of this Trp residue [31].
  • Trp fluorimetry revealed that in the three mutant PVs the residue Trp-102 is deeply buried in the hydrophobic core.(ABSTRACT TRUNCATED AT 250 WORDS)[32]
  • Calcium titration of CR monitored by Trp fluorescence intensity showed that recombinant CR and some fragments bound Ca2+ with high affinity (Kd below 0.4 microM) and with high cooperativity [33].

References

  1. 19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol. Li, E., Qian, S.J., Yang, N.C., d'Avignon, A., Gordon, J.I. J. Biol. Chem. (1990) [Pubmed]
  2. Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase. Suehiro, K., Kawabata, S., Miyata, T., Takeya, H., Takamatsu, J., Ogata, K., Kamiya, T., Saito, H., Niho, Y., Iwanaga, S. J. Biol. Chem. (1989) [Pubmed]
  3. Carcinogenicity in mice and rats of heterocyclic amines in cooked foods. Ohgaki, H., Hasegawa, H., Kato, T., Suenaga, M., Ubukata, M., Sato, S., Takayama, S., Sugimura, T. Environ. Health Perspect. (1986) [Pubmed]
  4. Uptake of heterocyclic amines, Trp-P-1 and Trp-P-2, into clonal rat pheochromocytoma PC12h cells by dopamine uptake system. Naoi, M., Takahashi, T., Ichinose, H., Wakabayashi, K., Sugimura, T., Nagatsu, T. Neurosci. Lett. (1989) [Pubmed]
  5. Isolation and structure-functional characterization of phage display library-derived mimotopes of noxiustoxin, a neurotoxin of the scorpion Centruroides noxius Hoffmann. Gazarian, T., Selisko, B., Hérion, P., Gazarian, K. Mol. Immunol. (2000) [Pubmed]
  6. Effect of p-chlorophenylalanine and tryptophan on sleep, EEG and motor activity in the rat. Borbély, A.A., Neuhaus, H.U., Tobler, I. Behav. Brain Res. (1981) [Pubmed]
  7. Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex. Enninga, J., Levay, A., Fontoura, B.M. Mol. Cell. Biol. (2003) [Pubmed]
  8. Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39. Sakaue, F., Saito, T., Sato, Y., Asada, A., Ishiguro, K., Hasegawa, M., Hisanaga, S. J. Biol. Chem. (2005) [Pubmed]
  9. N-terminal myristoylation regulates calcium-induced conformational changes in neuronal calcium sensor-1. Jeromin, A., Muralidhar, D., Parameswaran, M.N., Roder, J., Fairwell, T., Scarlata, S., Dowal, L., Mustafi, S.M., Chary, K.V., Sharma, Y. J. Biol. Chem. (2004) [Pubmed]
  10. Identification of a neuropeptide modified with bromine as an endogenous ligand for GPR7. Fujii, R., Yoshida, H., Fukusumi, S., Habata, Y., Hosoya, M., Kawamata, Y., Yano, T., Hinuma, S., Kitada, C., Asami, T., Mori, M., Fujisawa, Y., Fujino, M. J. Biol. Chem. (2002) [Pubmed]
  11. Amino acids in the second and third intracellular loops of the parathyroid Ca2+-sensing receptor mediate efficient coupling to phospholipase C. Chang, W., Chen, T.H., Pratt, S., Shoback, D. J. Biol. Chem. (2000) [Pubmed]
  12. Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug. Sotelo-Mundo, R.R., Ciesla, J., Dzik, J.M., Rode, W., Maley, F., Maley, G.F., Hardy, L.W., Montfort, W.R. Biochemistry (1999) [Pubmed]
  13. Food-derived heterocyclic amines, 3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole and related amines, as inhibitors of monoamine metabolism. Maruyama, W., Ota, A., Takahashi, A., Nagatsu, T., Naoi, M. J. Neural Transm. Suppl. (1994) [Pubmed]
  14. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. Noiva, R., Freedman, R.B., Lennarz, W.J. J. Biol. Chem. (1993) [Pubmed]
  15. Metal binding properties of recombinant rat parvalbumin wild-type and F102W mutant. Pauls, T.L., Durussel, I., Cox, J.A., Clark, I.D., Szabo, A.G., Gagné, S.M., Sykes, B.D., Berchtold, M.W. J. Biol. Chem. (1993) [Pubmed]
  16. Probing site-specific calmodulin calcium and lanthanide affinity by grafting. Ye, Y., Lee, H.W., Yang, W., Shealy, S., Yang, J.J. J. Am. Chem. Soc. (2005) [Pubmed]
  17. A tryptophan that modulates tetrahydrobiopterin-dependent electron transfer in nitric oxide synthase regulates enzyme catalysis by additional mechanisms. Wang, Z.Q., Wei, C.C., Santolini, J., Panda, K., Wang, Q., Stuehr, D.J. Biochemistry (2005) [Pubmed]
  18. Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors. Mery, L., Magnino, F., Schmidt, K., Krause, K.H., Dufour, J.F. FEBS Lett. (2001) [Pubmed]
  19. Evidence for a close link between the thyroid hormone transport system and the aromatic amino acid transport system T in erythrocytes. Zhou, Y., Samson, M., Osty, J., Francon, J., Blondeau, J.P. J. Biol. Chem. (1990) [Pubmed]
  20. Spectroscopic studies of the structural domains of mammalian DNA beta-polymerase. Casas-Finet, J.R., Kumar, A., Morris, G., Wilson, S.H., Karpel, R.L. J. Biol. Chem. (1991) [Pubmed]
  21. Intracellular protein catabolism and its control during nutrient deprivation and supply. Mortimore, G.E., Pösö, A.R. Annu. Rev. Nutr. (1987) [Pubmed]
  22. Ornithine decarboxylase stability in HMOA and DH23b cells is not due to post-translational truncation of a C-terminal recognition site. Mitchell, J.L., Choe, C.Y., Judd, G.G. Biochem. J. (1996) [Pubmed]
  23. Delineation of two encephalitogenic myelin basic protein epitopes for DA rats. Smeltz, R.B., Wolf, N.A., Swanborg, R.H. J. Neuroimmunol. (1998) [Pubmed]
  24. Two invariant tryptophans on the alpha1 subunit define domains necessary for GABA(A) receptor assembly. Srinivasan, S., Nichols, C.J., Lawless, G.M., Olsen, R.W., Tobin, A.J. J. Biol. Chem. (1999) [Pubmed]
  25. Modulation of the amino acid control of hepatic protein degradation by caloric deprivation. Two modes of alanine co-regulation. Mortimore, G.E., Wert, J.J., Adams, C.E. J. Biol. Chem. (1988) [Pubmed]
  26. Amino acid and hormonal control of macromolecular turnover in perfused rat liver. Evidence for selective autophagy. Lardeux, B.R., Mortimore, G.E. J. Biol. Chem. (1987) [Pubmed]
  27. Prostate alpha-protein. Complete amino acid sequence of the component that inhibits nuclear retention of the androgen-receptor complex. Liao, S., Chen, C., Huang, I.Y. J. Biol. Chem. (1982) [Pubmed]
  28. Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions. Chai, Y.C., Jung, C.H., Lii, C.K., Ashraf, S.S., Hendrich, S., Wolf, B., Sies, H., Thomas, J.A. Arch. Biochem. Biophys. (1991) [Pubmed]
  29. Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa. Lee, K.K., Murakawa, M., Takahashi, S., Tsubuki, S., Kawashima, S., Sakamaki, K., Yonehara, S. J. Biol. Chem. (1998) [Pubmed]
  30. Signaling microdomains define the specificity of receptor-mediated InsP(3) pathways in neurons. Delmas, P., Wanaverbecq, N., Abogadie, F.C., Mistry, M., Brown, D.A. Neuron (2002) [Pubmed]
  31. Molecular characterization of the gerbil C5a receptor and identification of a transmembrane domain V amino acid that is crucial for small molecule antagonist interaction. Waters, S.M., Brodbeck, R.M., Steflik, J., Yu, J., Baltazar, C., Peck, A.E., Severance, D., Zhang, L.Y., Currie, K., Chenard, B.L., Hutchison, A.J., Maynard, G., Krause, J.E. J. Biol. Chem. (2005) [Pubmed]
  32. Inactivation of individual Ca(2+)-binding sites in the paired EF-hand sites of parvalbumin reveals asymmetrical metal-binding properties. Pauls, T.L., Durussel, I., Berchtold, M.W., Cox, J.A. Biochemistry (1994) [Pubmed]
  33. Conformational changes and calcium binding by calretinin and its recombinant fragments containing different sets of EF hand motifs. Kuźnicki, J., Strauss, K.I., Jacobowitz, D.M. Biochemistry (1995) [Pubmed]
 
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