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
Aminoacid Length 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

Secondary 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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.