Search by BoMiProt ID - Bomi4


Primary Information

BoMiProt ID Bomi4
Protein Name Transthyretin
Organism Bos taurus
Uniprot IdO46375
Milk FractionWhey
Ref Sequence Id NP_776392.1
Amino Acid Lenth 147
Molecular Weight 15727
Fasta Sequence https://www.uniprot.org/uniprot/O46375.fasta
Gene Name TTR
Gene Id 280948
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells Liver, choroid plexus of brain
Protein Function Important role in behavior, cognition, neuropeptide amidation, neurogenesis, nerve regeneration, axonal growth and 14-3-3ζ metabolism; transport of thyroxine and retinol binding protein; causative agent of protein aggregation associated with amyloid fibril deposition
Biochemical Properties Called as prealbumin; homotetrameric protein; synthetized by the liver and the choroid plexus of brain; globular shape with a central hydrophobic channel; low pH promotes the dissociation of transthyretin tetramer into monomers; neutral crystal structure of TTR demonstrated double protonation of His88 to break the hydrogen-bond network, causing destabilization of the TTR tetramer
Significance in milk markers of caloric malnutrition
Additional Comments TTR aggregates are responsible for many amyloidosis such as familial amyloidotic polyneuropathy and cardiomyopathy; TTR levels in plasma change with age - decreased in healthy newborns when compared with adults
Bibliography 1. Blake, C. C., Geisow, M. J., Oatley, S. J., Rérat, B., & Rérat, C. (1978). Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. Journal of Molecular Biology, 121(3), 339–356. https://doi.org/10.1016/0022-2836(78)90368-6.
2. Henze, A., Homann, T., Serteser, M., Can, O., Sezgin, O., Coskun, A., … Ozpinar, A. (2015). Post-translational modifications of transthyretin affect the triiodonine-binding potential. Journal of Cellular and Molecular Medicine, 19(2), 359–370. https://doi.org/10.1111/jcmm.12446.
3. Vahlquist, A., Rask, L., Peterson, P. A., & Berg, T. (1975). The concentrations of retinol-binding protein, prealbumin, and transferrin in the sera of newly delivered mothers and children of various ages. Scandinavian Journal of Clinical and Laboratory Investigation, 35(6), 569–575. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1239075.
4. Aleshire, S. L., Bradley, C. A., Richardson, L. D., & Parl, F. F. (1983). Localization of human prealbumin in choroid plexus epithelium. The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society, 31(5), 608–612. https://doi.org/10.1177/31.5.6341455.
5. Felding, P., & Fex, G. (1982). Cellular origin of prealbumin in the rat. Biochimica et Biophysica Acta, 716(3), 446–449. https://doi.org/10.1016/0304-4165(82)90040-x.
6. Yokoyama, T., Mizuguchi, M., Nabeshima, Y., Kusaka, K., Yamada, T., Hosoya, T., … Niimura, N. (2012). Hydrogen-bond network and pH sensitivity in transthyretin: Neutron crystal structure of human transthyretin. Journal of Structural Biology, 177(2), 283–290. https://doi.org/10.1016/j.jsb.2011.12.022.